Journal articles: 'Biomimetické peptidy'

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Abbas, Manzar, Wojciech P. Lipiński, Jiahua Wang, and Evan Spruijt. "Peptide-based coacervates as biomimetic protocells." Chemical Society Reviews 50, no. 6 (2021): 3690–705. http://dx.doi.org/10.1039/d0cs00307g.

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Shy, Adrianna N., Huaimin Wang, Zhaoqianqi Feng, and Bing Xu. "Heterotypic Supramolecular Hydrogels Formed by Noncovalent Interactions in Inflammasomes." Molecules 26, no. 1 (December 26, 2020): 77. http://dx.doi.org/10.3390/molecules26010077.

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The advance of structural biology has revealed numerous noncovalent interactions between peptide sequences in protein structures, but such information is less explored for developing peptide materials. Here we report the formation of heterotypic peptide hydrogels by the two binding motifs revealed by the structures of an inflammasome. Specifically, conjugating a self-assembling motif to the positively or negatively charged peptide sequence from the ASCPYD filaments of inflammasome produces the solutions of the peptides. The addition of the peptides of the oppositely charged and complementary peptides to the corresponding peptide solution produces the heterotypic hydrogels. Rheology measurement shows that ratios of the complementary peptides affect the viscoelasticity of the resulted hydrogel. Circular dichroism indicates that the addition of the complementary peptides results in electrostatic interactions that modulate self-assembly. Transmission electron microscopy reveals that the ratio of the complementary peptides controls the morphology of the heterotypic peptide assemblies. This work illustrates a rational, biomimetic approach that uses the structural information from the protein data base (PDB) for developing heterotypic peptide materials via self-assembly.

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Boix, Estefania, Valeria Puddu, and Carole C. Perry. "Preparation of hexagonal GeO2 particles with particle size and crystallinity controlled by peptides, silk and silk-peptide chimeras." Dalton Trans. 43, no. 44 (2014): 16902–10. http://dx.doi.org/10.1039/c4dt01974a.

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Synthesis of α-quartz like (hexagonal) GeO₂ by a biomimetic approach using peptides, silk and silk-peptide chimeras to control precipitation yield, particle morphology, size and crystallinity of the mineral.

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Klepel, Florian, and Bart Jan Ravoo. "A dynamic combinatorial library for biomimetic recognition of dipeptides in water." Beilstein Journal of Organic Chemistry 16 (July 2, 2020): 1588–95. http://dx.doi.org/10.3762/bjoc.16.131.

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Small peptides are involved in countless biological processes. Hence selective binding motifs for peptides can be powerful tools for labeling or inhibition. Finding those binding motifs, especially in water which competes for intermolecular H-bonds, poses an enormous challenge. A dynamic combinatorial library can be a powerful method to overcome this issue. We previously reported artificial receptors emerging form a dynamic combinatorial library of peptide building blocks. In this study we aimed to broaden this scope towards recognition of small peptides. Employing CXC peptide building blocks, we found that cyclic dimers of oxidized CFC bind to the aromatic peptides FF and YY (K ≈ 229–702 M−1), while AA binds significantly weaker (K ≈ 65–71 M−1).

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Chantawannakul, Jarinyagon, Paninnuch Chatpattanasiri, Vichugorn Wattayagorn, Mesayamas Kongsema, Tipanart Noikaew, and Pramote Chumnanpuen. "Virtual Screening for Biomimetic Anti-Cancer Peptides from Cordyceps militaris Putative Pepsinized Peptidome and Validation on Colon Cancer Cell Line." Molecules 26, no. 19 (September 23, 2021): 5767. http://dx.doi.org/10.3390/molecules26195767.

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Colorectal cancer is one of the leading causes of cancer-related death in Thailand and many other countries. The standard practice for curing this cancer is surgery with an adjuvant chemotherapy treatment. However, the unfavorable side effects of chemotherapeutic drugs are undeniable. Recently, protein hydrolysates and anticancer peptides have become popular alternative options for colon cancer treatment. Therefore, we aimed to screen and select the anticancer peptide candidates from the in silico pepsin hydrolysate of a Cordyceps militaris (CM) proteome using machine-learning-based prediction servers for anticancer prediction, i.e., AntiCP, iACP, and MLACP. The selected CM-anticancer peptide candidates could be an alternative treatment or co-treatment agent for colorectal cancer, reducing the use of chemotherapeutic drugs. To ensure the anticancer properties, an in vitro assay was performed with “CM-biomimetic peptides” on the non-metastatic colon cancer cell line (HT-29). According to the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay results from peptide candidate treatments at 0–400 µM, the IC50 doses of the CM-biomimetic peptide with no toxic and cancer-cell-penetrating ability, original C. militaris biomimetic peptide (C-ori), against the HT-29 cell line were 114.9 µM at 72 hours. The effects of C-ori compared to the doxorubicin, a conventional chemotherapeutic drug for colon cancer treatment, and the combination effects of both the CM-anticancer peptide and doxorubicin were observed. The results showed that C-ori increased the overall efficiency in the combination treatment with doxorubicin. According to the acridine orange/propidium iodine (AO/PI) staining assay, C-ori can induce apoptosis in HT-29 cells significantly, confirmed by chromatin condensation, membrane blebbing, apoptotic bodies, and late apoptosis which were observed under a fluorescence microscope.

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Agouram, Naima, El Mestafa El Hadrami, and Abdeslem Bentama. "1,2,3-Triazoles as Biomimetics in Peptide Science." Molecules 26, no. 10 (May 14, 2021): 2937. http://dx.doi.org/10.3390/molecules26102937.

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Natural peptides are an important class of chemical mediators, essential for most vital processes. What limits the potential of the use of peptides as drugs is their low bioavailability and enzymatic degradation in vivo. To overcome this limitation, the development of new molecules mimicking peptides is of great importance for the development of new biologically active molecules. Therefore, replacing the amide bond in a peptide with a heterocyclic bioisostere, such as the 1,2,3-triazole ring, can be considered an effective solution for the synthesis of biologically relevant peptidomimetics. These 1,2,3-triazoles may have an interesting biological activity, because they behave as rigid link units, which can mimic the electronic properties of amide bonds and show bioisosteric effects. Additionally, triazole can be used as a linker moiety to link peptides to other functional groups.

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Sivkova, Radoslava, Johanka Táborská, Alain Reparaz, Andres de los Santos Pereira, Ilya Kotelnikov, Vladimir Proks, Jan Kučka, Jan Svoboda, Tomáš Riedel, and Ognen Pop-Georgievski. "Surface Design of Antifouling Vascular Constructs Bearing Biofunctional Peptides for Tissue Regeneration Applications." International Journal of Molecular Sciences 21, no. 18 (September 16, 2020): 6800. http://dx.doi.org/10.3390/ijms21186800.

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Antifouling polymer layers containing extracellular matrix-derived peptide motifs offer promising new options for biomimetic surface engineering. In this contribution, we report the design of antifouling vascular grafts bearing biofunctional peptide motifs for tissue regeneration applications based on hierarchical polymer brushes. Hierarchical diblock poly(methyl ether oligo(ethylene glycol) methacrylate-block-glycidyl methacrylate) brushes bearing azide groups (poly(MeOEGMA-block-GMA-N3)) were grown by surface-initiated atom transfer radical polymerization (SI-ATRP) and functionalized with biomimetic RGD peptide sequences. Varying the conditions of copper-catalyzed alkyne-azide “click” reaction allowed for the immobilization of RGD peptides in a wide surface concentration range. The synthesized hierarchical polymer brushes bearing peptide motifs were characterized in detail using various surface sensitive physicochemical methods. The hierarchical brushes presenting the RGD sequences provided excellent cell adhesion properties and at the same time remained resistant to fouling from blood plasma. The synthesis of anti-fouling hierarchical brushes bearing 1.2 × 103 nmol/cm2 RGD biomimetic sequences has been adapted for the surface modification of commercially available grafts of woven polyethylene terephthalate (PET) fibers. The fiber mesh was endowed with polymerization initiator groups via aminolysis and acylation reactions optimized for the material. The obtained bioactive antifouling vascular grafts promoted the specific adhesion and growth of endothelial cells, thus providing a potential avenue for endothelialization of artificial conduits.

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Foden, Callum S., Saidul Islam, Christian Fernández-García, Leonardo Maugeri, Tom D. Sheppard, and Matthew W. Powner. "Prebiotic synthesis of cysteine peptides that catalyze peptide ligation in neutral water." Science 370, no. 6518 (November 12, 2020): 865–69. http://dx.doi.org/10.1126/science.abd5680.

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Peptide biosynthesis is performed by ribosomes and several other classes of enzymes, but a simple chemical synthesis may have created the first peptides at the origins of life. α-Aminonitriles—prebiotic α–amino acid precursors—are generally produced by Strecker reactions. However, cysteine’s aminothiol is incompatible with nitriles. Consequently, cysteine nitrile is not stable, and cysteine has been proposed to be a product of evolution, not prebiotic chemistry. We now report a high-yielding, prebiotic synthesis of cysteine peptides. Our biomimetic pathway converts serine to cysteine by nitrile-activated dehydroalanine synthesis. We also demonstrate that N-acylcysteines catalyze peptide ligation, directly coupling kinetically stable—but energy-rich—α-amidonitriles to proteinogenic amines. This rare example of selective and efficient organocatalysis in water implicates cysteine as both catalyst and precursor in prebiotic peptide synthesis.

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Govada, Lata, Emmanuel Saridakis, Sean C. Kassen, Ahmad Bin-Ramzi, Rhodri Marc Morgan, Benjamin Chain, John R. Helliwell, and Naomi E. Chayen. "X-ray crystallographic studies of RoAb13 bound to PIYDIN, a part of the N-terminal domain of C-C chemokine receptor 5." IUCrJ 8, no. 4 (July 1, 2021): 678–83. http://dx.doi.org/10.1107/s2052252521005340.

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C-C chemokine receptor 5 (CCR5) is a major co-receptor molecule used by HIV-1 to enter cells. This led to the hypothesis that stimulating an antibody response would block HIV with minimal toxicity. Here, X-ray crystallographic studies of the anti-CCR5 antibody RoAb13 together with two peptides were undertaken: one peptide is a 31-residue peptide containing the PIYDIN sequence and the other is the PIDYIN peptide alone, where PIYDIN is part of the N-terminal region of CCR5 previously shown to be important for HIV entry. In the presence of the longer peptide (the complete N-terminal domain), difference electron density was observed at a site within a hypervariable CDR3 binding region. In the presence of the shorter core peptide PIYDIN, difference electron density is again observed at this CDR3 site, confirming consistent binding for both peptides. This may be useful in the design of a new biomimetic to stimulate an antibody response to CCR5 in order to block HIV infection.

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Kirkham, J., A. Firth, D. Vernals, N. Boden, C. Robinson, R. C. Shore, S. J. Brookes, and A. Aggeli. "Self-assembling Peptide Scaffolds Promote Enamel Remineralization." Journal of Dental Research 86, no. 5 (May 2007): 426–30. http://dx.doi.org/10.1177/154405910708600507.

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Rationally designed β-sheet-forming peptides that spontaneously form three-dimensional fibrillar scaffolds in response to specific environmental triggers may potentially be used in skeletal tissue engineering, including the treatment/prevention of dental caries, via bioactive surface groups. We hypothesized that infiltration of caries lesions with monomeric low-viscosity peptide solutions would be followed by in situ polymerization triggered by conditions of pH and ionic strength, providing a biomimetic scaffold capable of hydroxyapatite nucleation, promoting repair. Our aim was to determine the effect of an anionic peptide applied to caries-like lesions in human dental enamel under simulated intra-oral conditions of pH cycling. Peptide treatment significantly increased net mineral gain by the lesions, due to both increased remineralization and inhibition of demineralization over a five-day period. The assembled peptide was also capable of inducing hydroxyapatite nucleation de novo. The results suggest that self-assembling peptides may be useful in the modulation of mineral behavior during in situ dental tissue engineering.

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Valko, Klara Livia, Gabriela Ivanova-Berndt, Paul Beswick, Mark Kindey, and Dorothy Ko. "Application of biomimetic HPLC to estimate lipophilicity, protein and phospholipid binding of potential peptide therapeutics." ADMET and DMPK 6, no. 2 (June 16, 2018): 162–75. http://dx.doi.org/10.5599/admet.544.

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Peptide therapeutics are new modalities offering several challenges to drug discovery. They are generally less stable and permeable in vivo. The characterization of their lipophilicity cannot be carried out using the traditional in silico or wet octanol/water partition coefficients. The prediction of their in vivo distribution and permeability is also challenging. In this paper, it is demonstrated that the biomimetic properties such as lipophilicity, protein and phospholipid binding can be easily assessed by HPLC using chemically bonded protein and immobilized artificial membrane (IAM) stationary phases. The obtained properties for a set of potential therapeutic peptides with 3 to 33 amino acids have been analysed and it was found that similar characteristics of the properties could be observed as for small molecule drugs. The albumin binding showed correlation with their measured lipophilicity on the C-18 stationary phase with acidic peptides showing stronger than expected albumin binding. The (IAM) chromatography revealed peptide membrane affinity, which was stronger for positively charged peptides (containing arginine) and showed correlation to the alpha-1-acid glycoprotein (AGP) binding, which was also stronger for positively charged compounds. The in vivo volume of distribution and drug efficiency of the peptides have been estimated using the models developed for small molecules. One of the candidate linear peptides has been assessed in various cellular and in vivo assays and the results have confirmed the estimated cell partition and brain to plasma ratio. It can be demonstrated, that up to 21 amino acids, the peaks of the peptides obtained on the protein phase were symmetrical and narrow. The interaction of larger peptides with the protein stationary phases resulted in wide peaks showing multiple equilibrium processes with slow kinetics during chromatography. The larger peptides showed narrow and symmetrical peaks on the IAM column enabling the quantification of peptide - cell membrane interactions.

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Cui, Yue, Sang N. Kim, Rajesh R. Naik, and Michael C. McAlpine. "Biomimetic Peptide Nanosensors." Accounts of Chemical Research 45, no. 5 (January 31, 2012): 696–704. http://dx.doi.org/10.1021/ar2002057.

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Tamerler, Candan, and Mehmet Sarikaya. "Molecular Biomimetics: Genetic Synthesis, Assembly, and Formation of Materials Using Peptides." MRS Bulletin 33, no. 5 (May 2008): 504–12. http://dx.doi.org/10.1557/mrs2008.102.

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AbstractIn nature, the molecular-recognition ability of peptides and, consequently, their functions are evolved through successive cycles of mutation and selection. Using biology as a guide, it is now possible to select, tailor, and control peptide–solid interactions and exploit them in novel ways. Combinatorial mutagenesis provides a protocol to genetically select short peptides with specific affinity to the surfaces of a variety of materials including metals, ceramics, and semiconductors. In the articles of this issue, we describe molecular characterization of inorganic-binding peptides; explain their further tailoring using post-selection genetic engineering and bioinformatics; and finally demonstrate their utility as molecular synthesizers, erectors, and assemblers. The peptides become fundamental building blocks of functional materials, each uniquely designed for an application in areas ranging from practical engineering to medicine.

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Wasilewski, Tomasz, Bartosz Szulczyński, Marek Wojciechowski, Wojciech Kamysz, and Jacek Gębicki. "A Highly Selective Biosensor Based on Peptide Directly Derived from the HarmOBP7 Aldehyde Binding Site." Sensors 19, no. 19 (October 3, 2019): 4284. http://dx.doi.org/10.3390/s19194284.

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This paper presents the results of research on determining the optimal length of a peptide chain to effectively bind octanal molecules. Peptides that map the aldehyde binding site in HarmOBP7 were immobilized on piezoelectric transducers. Based on computational studies, four Odorant Binding Protein-derived Peptides (OBPPs) with different sequences were selected. Molecular modelling results of ligand docking with selected peptides were correlated with experimental results. The use of low-molecular synthetic peptides, instead of the whole protein, enabled the construction OBPPs-based biosensors. This work aims at developing a biomimetic piezoelectric OBPPs sensor for selective detection of octanal. Moreover, the research is concerned with the ligand binding affinity depending on different peptides’ chain lengths. The authors believe that the chain length can have a substantial influence on the type and effectiveness of peptide–ligand interaction. A confirmation of in silico investigation results is the correlation with the experimental results, which shows that the highest affinity to octanal is exhibited by the longest peptide (OBPP4 – KLLFDSLTDLKKKMSEC-NH2). We hypothesized that the binding of long chain aldehydes to the peptide, mimicking the binding site of HarmOBP7, induced a conformational change in the peptide deposited on a selected transducer. The constructed OBPP4-based biosensors were able to selectively bind octanal in the gas phase. It was also shown that the sensors were characterized by high selectivity with respect to octanal, as well as to acetaldehyde and benzaldehyde. The results indicate that the OBPP4 peptide, mimicking the binding domain in the Odorant Binding Protein, can provide new opportunities for the development of biomimicking materials in the field of odor biosensors.

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Gharaei, Robabeh, Giuseppe Tronci, Robert P. Davies, Parikshit Goswami, and Stephen J. Russell. "An investigation into the nano-/micro-architecture of electrospun poly (ε-caprolactone) and self-assembling peptide fibers." MRS Advances 1, no. 11 (2016): 711–16. http://dx.doi.org/10.1557/adv.2016.35.

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ABSTRACTSelf-assembling peptides (SAPs) have the ability to spontaneously assemble into ordered nanostructures enabling the manufacture of ‘designer’ nanomaterials. The reversible molecular association of SAPs has been shown to offer great promise in therapeutics via for example, the design of biomimetic assemblies for hard tissue regeneration. This could be further exploited for novel nano/micro diagnostic tools. However, self-assembled peptide gels are often associated with inherent weak and transient mechanical properties. Their incorporation into polymeric matrices has been considered as a potential strategy to enhance their mechanical stability. This study focuses on the incorporation of an 11-residue peptide, P11-8 (peptide sequence: CH3CO-Gln-Gln-Arg-Phe-Orn-Trp-Orn-Phe-Glu-Gln-Gln-NH2) within a fibrous scaffold of poly (ε-caprolactone) (PCL). In this study an electrospinning technique was used to fabricate a biomimetic porous scaffold out of a solution of P11-8 and PCL which resulted in a biphasic structure composed of submicron fibers (diameter of 100-700 nm) and nanofibers (diameter of 10-100 nm). The internal morphology of the fabric and its micro-structure can be easily controlled by changing the peptide concentration. The secondary conformation of P11-8 was investigated in the as-spun fibers by ATR-FTIR spectroscopy and it is shown that peptide self-assembly into β-sheet tapes has taken place during fiber formation and the deposition of the fibrous web.

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Janairo, Jose Isagani B., Kathleen B. Aviso, Michael Angelo B. Promentilla, and Raymond R. Tan. "Enhanced Hyperbox Classifier Model for Nanomaterial Discovery." AI 1, no. 2 (June 17, 2020): 299–311. http://dx.doi.org/10.3390/ai1020020.

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Machine learning tools can be applied to peptide-mediated biomineralization, which is an emerging biomimetic technique of creating functional nanomaterials. In particular, they can be used for the discovery of biomineralization peptides, which currently relies on combinatorial enumeration approaches. In this work, an enhanced hyperbox classifier is developed which can predict if a given peptide sequence has a strong or weak binding affinity towards a gold surface. A mixed-integer linear program is formulated to generate the rule-based classification model. The classifier is optimized to account for false positives and false negatives, and clearly articulates how the classification decision is made. This feature makes the decision-making process transparent, and the results easy to interpret for decision support. The method developed can help accelerate the discovery of more biomineralization peptide sequences, which may expand the utility of peptide-mediated biomineralization as a means for nanomaterial synthesis.

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KATZ, Marina, Haim TSUBERY, Sofiya KOLUSHEVA, Alex SHAMES, Mati FRIDKIN, and Raz JELINEK. "Lipid binding and membrane penetration of polymyxin B derivatives studied in a biomimetic vesicle system." Biochemical Journal 375, no. 2 (October 15, 2003): 405–13. http://dx.doi.org/10.1042/bj20030784.

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Understanding membrane interactions and cell-wall permeation of Gram-negative bacteria is of great importance, owing to increasing bacterial resistance to existing drugs and therapeutic treatments. Here we use biomimetic lipid vesicles to analyse membrane association and penetration by synthetic derivatives of polymyxin B (PMB), a potent naturally occurring antibacterial cyclic peptide. The PMB analogues studied were PMB nonapeptide (PMBN), in which the hydrophobic alkyl residue was cleaved, PMBN diastereomer containing d-instead of l-amino acids within the cyclic ring (dPMBN) and PMBN where the hydrophobic alkyl chain was replaced with an Ala6 repeat (Ala6-PMBN). Peptide binding measurements, colorimetric transitions induced within the vesicles, fluorescence quenching experiments and ESR spectroscopy were applied to investigate the structural parameters underlying the different membrane-permeation profiles and biological activities of the analogues. The experiments point to the role of negatively charged lipids in membrane binding and confirm the prominence of lipopolisaccharide (LPS) in promoting membrane association and penetration by the peptides. Examination of the lipid interactions of the PMB derivatives shows that the cyclic moiety of PMB is not only implicated in lipid attachment and LPS binding, but also affects penetration into the inner bilayer core. The addition of the Ala6 peptide moiety, however, does not significantly promote peptide insertion into the hydrophobic lipid environment. The data also indicate that the extent of penetration into the lipid bilayer is not related to the overall affinity of the peptides to the membrane.

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Li, Yujing, Chin-Yi Chiu, and Yu Huang. "Biomimetic synthesis of inorganic materials and their applications." Pure and Applied Chemistry 83, no. 1 (November 19, 2010): 111–25. http://dx.doi.org/10.1351/pac-con-10-10-28.

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Mimicking the evolution processes of Nature, the combinatorial approach to biomolecular recognition properties attracts much attention due to the potential as a generic scheme to achieving complex material structures and hierarchical assemblies with molecular precision from the bottom up. In this paper, some recent efforts in the biomimetic synthesis of inorganic materials are reviewed, with emphasis placed on in vitro material formation with the use of protein/peptide molecules found in natural organisms as well as those with specific affinities to inorganic materials selected through the molecular evolution process. The applications of material-specific peptides and proteins in sensing and guiding hierarchical material assembly are also briefly discussed at the end.

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Roy, Souvik, Thuy-Ai D. Nguyen, Lu Gan, and Anne K. Jones. "Biomimetic peptide-based models of [FeFe]-hydrogenases: utilization of phosphine-containing peptides." Dalton Transactions 44, no. 33 (2015): 14865–76. http://dx.doi.org/10.1039/c5dt01796c.

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Xu, Jing-Bo, Fei Peng, Youlu Che, Wei Zhang, and Changyun Quan. "Porous hydroxyapatite ceramics coated with biomimetic peptides for induced osteogenesis." Materials Express 10, no. 9 (September 30, 2020): 1524–30. http://dx.doi.org/10.1166/mex.2020.1764.

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Biomimetic peptide has attracted extensive attention in bone tissue repairing owing to its excellent biocompatibility and stability. Hydroxyapatite ceramics (HAP) possess both excellent mechanical properties and good biocompatibility. To study the effects of bionic peptide D9KIPKAS(pSer)VPTELSAISRGDS on the interfacial activity and biological properties of hydroxyapatite ceramics, porous HAP ceramics were prepared using ammonium carbonate as a pore-forming agent. To explore the influence of surface modification on the interfacial activity of porous HAP ceramics when applying different methods, surface modification was carried out using physical adsorption (HAP-p-PP2) and a chemically grafted polypeptide (HAP-c-PP2). X-ray diffraction was used to characterize the crystal morphology of the porous HAP ceramics before and after sintering. The results of FTIR and XPS showed that bionic peptides were successfully grafted onto the surface of a porous HAP ceramic. An SEM graph shows the adhesion and spread of BMSCs on the materials. Meanwhile, the results of in vitro cell experiments showed that HAP-c-PP2 can better promote BMSC proliferation. In conclusion, bionic peptide D9KIPKAS(pSer)VPTELSAISRGDS with multifunctional functional groups is more conducive to the adhesion, proliferation and differentiation of BMSCs which can make it play an effective role in osteoinduction in bone tissue engineering.

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Li, Jianxia, Leilei Zheng, Lin Zeng, Yan Zhang, Lin Jiang, and Jinlin Song. "RGD Peptide-Grafted Graphene Oxide as a New Biomimetic Nanointerface for Impedance-Monitoring Cell Behaviors." Journal of Nanomaterials 2016 (2016): 1–12. http://dx.doi.org/10.1155/2016/2828512.

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A new biomimetic nanointerface was constructed by facile grafting the bioactive arginylglycylaspartic acid (RGD) peptide on the graphene oxide (GO) surface through carbodiimide and N-hydroxysuccinimide coupling amidation reaction. The formed RGD-GO nanocomposites own unique two-dimensional structure and desirable electrochemical performance. The linked RGD peptides could improve GO’s biocompatibility and support the adhesion and proliferation of human periodontal ligament fibroblasts (HPLFs) on RGD-GO biofilm surface. Furthermore the biologically active RGD-GO nanocomposites were demonstrated as a potential biomimetic nanointerface for monitoring cell biobehaviors by electrochemical impedance spectroscopy (EIS). By analysis of the data obtained from equivalent circuit-fitting impedance spectroscopy, the information related to cell membrane capacitance, cell-cell gap resistance, and cell-electrode interface gap resistance in the process of cell adhesion and proliferation could be obtained. Besides, this proposed impedance-based cell sensor could be used to assess the inhibition effect of the lipopolysaccharide (LPS) on the HPLFs proliferation. Findings from this work suggested that RGD peptide functionalized GO nanomaterials may be not only applied in dental tissue engineering but also used as a sensor interface for electrochemical detection and analysis of cell behaviors in vitro.

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Tamerler, Candan, and Mehmet Sarikaya. "Molecular biomimetics: nanotechnology and bionanotechnology using genetically engineered peptides." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 367, no. 1894 (May 13, 2009): 1705–26. http://dx.doi.org/10.1098/rsta.2009.0018.

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Nature provides inspiration for designing materials and systems that derive their functions from highly organized structures. Biological hard tissues are hybrid materials having inorganics within a complex organic matrix, the molecular scaffold controlling the inorganic structures. Biocomposites incorporate both biomacromolecules such as proteins, lipids and polysaccharides, and inorganic materials, such as hydroxyapatite, silica, magnetite and calcite. The ordered organization of hierarchical structures in organisms begins via the molecular recognition of inorganics by proteins that control interactions and is followed by the highly efficient self-assembly across scales. Following the molecular biological principle, proteins could also be used in controlling materials formation in practical engineering via self-assembled, hybrid, functional materials structures. In molecular biomimetics, material-specific peptides could be the key in the molecular engineering of biology-inspired materials. With the recent developments of nanoscale engineering in physical sciences and the advances in molecular biology, we now combine genetic tools with synthetic nanoscale constructs to create a novel methodology. We first genetically select and/or design peptides with specific binding to functional solids, tailor their binding and assembly characteristics, develop bifunctional peptide/protein genetic constructs with both material binding and biological activity, and use these as molecular synthesizers, erectors and assemblers. Here, we give an overview of solid-binding peptides as novel molecular agents coupling bio- and nanotechnology.

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Samaritoni, J., Jacek Martynow, Martin O’Donnell, and William Scott. "Preparation and Use of a General Solid-Phase Intermediate to Biomimetic Scaffolds and Peptide Condensations." Molecules 23, no. 7 (July 18, 2018): 1762. http://dx.doi.org/10.3390/molecules23071762.

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The Distributed Drug Discovery (D3) program develops simple, powerful, and reproducible procedures to enable the distributed synthesis of large numbers of potential drugs for neglected diseases. The synthetic protocols are solid-phase based and inspired by published work. One promising article reported that many biomimetic molecules based on diverse scaffolds with three or more sites of variable substitution can be synthesized in one or two steps from a common key aldehyde intermediate. This intermediate was prepared by the ozonolysis of a precursor functionalized at two variable sites, restricting their presence in the subsequently formed scaffolds to ozone compatible functional groups. To broaden the scope of the groups available at one of these variable sites, we developed a synthetic route to an alternative, orthogonally protected key intermediate that allows the incorporation of ozone sensitive groups after the ozonolysis step. The utility of this orthogonally protected intermediate is demonstrated in the synthesis of several representative biomimetic scaffolds containing ozonolytically labile functional groups. It is compatible with traditional Fmoc peptide chemistry, permitting it to incorporate peptide fragments for use in fragment condensations with peptides containing cysteine at the N-terminus. Overall yields for its synthesis and utilization (as many as 13 steps) indicate good conversions at each step.

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Janairo, Jose Isagani B., and Kazuyasu Sakaguchi. "Synthesis of Bimetallic PdAg Nanoparticles through an Oligomerization- Controlled Biomineralization Peptide." Materials Science Forum 928 (August 2018): 77–82. http://dx.doi.org/10.4028/www.scientific.net/msf.928.77.

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Peptide – mediated biomineralization is an emerging and promising biomimetic approach for the synthesis of nanomaterials. This nature – inspired technique of producing inorganic nanostructures depends on the biomineralization peptide to control the shape and morphology of the prevailing inorganic nanostructure. One of the challenges in peptide – mediated biomineralization is controlling the 3D arrangement and orientation of the peptide. Recently, we have developed a peptide platform that can specify and direct the geometric arrangement and spatial orientation of the biomineralization peptide. The peptide platform is composed of two segments: a metal binding sequence, and the tetramerization domain of the tumor suppressor p53 protein, which acts as the oligomerization control element. The resulting fusion peptide exhibits a spatially – fixed and well – controlled assembly of the palladium binding sequence. This present study demonstrates the utility and efficacy of this peptide platform to bimetallic materials. Monodispersed 5 nm bimetallic PdAg nanoparticles were synthesized using the oligomerization – controlled biomineralization peptide. The synthesis was carried out in an aqueous environment, void of harsh reagents. When other fusion biomineralization peptides were used to synthesize bimetallic PdAg nanoparticles, less ordered nanoparticles were yielded. The results highlight the importance of controlled assembly on bimetallic nanoparticle formation through biomineralization. The presented method offers a straightforward manner of creating monodispersed and extremely small nanoparticles, which are useful in a wide array of applications.

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Di Foggia, Michele, Vitaliano Tugnoli, Stefano Ottani, Monica Dettin, Annj Zamuner, Santiago Sanchez-Cortes, Daniele Cesini, and Armida Torreggiani. "SERS Investigation on Oligopeptides Used as Biomimetic Coatings for Medical Devices." Biomolecules 11, no. 7 (June 29, 2021): 959. http://dx.doi.org/10.3390/biom11070959.

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The surface-enhanced Raman scattering (SERS) spectra of three amphiphilic oligopeptides derived from EAK16 (AEAEAKAK)2 were examined to study systematic amino acid substitution effects on the corresponding interaction with Ag colloidal nanoparticles. Such self-assembling molecular systems, known as “molecular Lego”, are of particular interest for their uses in tissue engineering and as biomimetic coatings for medical devices because they can form insoluble macroscopic membranes under physiological conditions. Spectra were collected for both native and gamma-irradiated samples. Quantum mechanical data on two of the examined oligopeptides were also obtained to clarify the assignment of the prominent significative bands observed in the spectra. In general, the peptide–nanoparticles interaction occurs through the COO− groups, with the amide bond and the aliphatic chain close to the colloid surface. After gamma irradiation, mimicking a free oxidative radical attack, the SERS spectra of the biomaterials show that COO− groups still provide the main peptide–nanoparticle interactions. However, the spatial arrangement of the peptides is different, exhibiting a systematic decrease in the distance between aliphatic chains and colloid nanoparticles.

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Baxter, Richard. "A Macromolecular approach to peptide-based molecular recognition and catalysis." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1588. http://dx.doi.org/10.1107/s2053273314084113.

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Synthetic peptides incorporating non-natural amino acids provide an opportunity to apply biomimetic principles in the design of both chemical scaffolds and novel pharmaceuticals. Crystallographic analysis can be of significant utility in this area just as elsewhere, but blur the line between small-molecule and macromolecular systems. I will present recent examples combining the tools of macromolecular crystallography techniques with chemical biology to elucidate structures of peptide-based binding and catalytic motifs. First, I will discuss recent structures of a beta-peptide known to spontaneously self-assemble into a octameric bundle wih a defined tertiary-fold. By introducing a non-natural amino acid at the solvent-exposed surface, a binding epitope for poly-alcohols is introduced. [1] Conversely, by modifying the hydrophobic core, the tertiary fold can be re-organized. [2] Second, I will discuss a peptide-based catalyst for the site-specific modification of saccharide units in the scaffold of the antibiotic teicoplanin. [3] While glycosylated small-molecules can be challenging structural-targets, native chemical ligation of the peptide to a macromolecular scaffold allowed for structure determination of the peptide and its binding target. Further structure-based design of more complex non-natural amino acid structures is a promising route to novel peptide-based tools and therapeutics.

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Wisdom, Cate, Sarah Kay VanOosten, Kyle W. Boone, Dmytro Khvostenko, Paul M. Arnold, Malcolm L. Snead, and Candan Tamerler. "Controlling the Biomimetic Implant Interface: Modulating Antimicrobial Activity by Spacer Design." Journal of Molecular and Engineering Materials 04, no. 01 (March 2016): 1640005. http://dx.doi.org/10.1142/s2251237316400050.

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Surgical site infection is a common cause of post-operative morbidity, often leading to implant loosening, ultimately requiring revision surgery, increased costs and worse surgical outcomes. Since implant failure starts at the implant surface, creating and controlling the bio-material interface will play a critical role in reducing infection while improving host cell-to-implant interaction. Here, we engineered a biomimetic interface based upon a chimeric peptide that incorporates a titanium binding peptide (TiBP) with an antimicrobial peptide (AMP) into a single molecule to direct binding to the implant surface and deliver an antimicrobial activity against S. mutans and S. epidermidis, two bacteria which are linked with clinical implant infections. To optimize antimicrobial activity, we investigated the design of the spacer domain separating the two functional domains of the chimeric peptide. Lengthening and changing the amino acid composition of the spacer resulted in an improvement of minimum inhibitory concentration by a three-fold against S. mutans. Surfaces coated with the chimeric peptide reduced dramatically the number of bacteria, with up to a nine-fold reduction for S. mutans and a 48-fold reduction for S. epidermidis. Ab initio predictions of antimicrobial activity based on structural features were confirmed. Host cell attachment and viability at the biomimetic interface were also improved compared to the untreated implant surface. Biomimetic interfaces formed with this chimeric peptide offer interminable potential by coupling antimicrobial and improved host cell responses to implantable titanium materials, and this peptide based approach can be extended to various biomaterials surfaces.

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Pędzinski, Tomasz, Katarzyna Grzyb, Konrad Skotnicki, Piotr Filipiak, Krzysztof Bobrowski, Chryssostomos Chatgilialoglu, and Bronislaw Marciniak. "Radiation- and Photo-Induced Oxidation Pathways of Methionine in Model Peptide Backbone under Anoxic Conditions." International Journal of Molecular Sciences 22, no. 9 (April 30, 2021): 4773. http://dx.doi.org/10.3390/ijms22094773.

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Within the reactive oxygen species (ROS) generated by cellular metabolisms, hydroxyl radicals (HO•) play an important role, being the most aggressive towards biomolecules. The reactions of HO• with methionine residues (Met) in peptides and proteins have been intensively studied, but some fundamental aspects remain unsolved. In the present study we examined the biomimetic model made of Ac-Met-OMe, as the simplest model peptide backbone, and of HO• generated by ionizing radiation in aqueous solutions under anoxic conditions. We performed the identification and quantification of transient species by pulse radiolysis and of final products by LC-MS and high-resolution MS/MS after γ-radiolysis. By parallel photochemical experiments, using 3-carboxybenzophenone (CB) triplet with the model peptide, we compared the outcomes in terms of short-lived intermediates and stable product identification. The result is a detailed mechanistic scheme of Met oxidation by HO•, and by CB triplets allowed for assigning transient species to the pathways of products formation.

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Creasey, Rhiannon C. G., A. Bernardus Mostert, Armin Solemanifar, Tuan A. H. Nguyen, Bernardino Virdis, Stefano Freguia, and Bronwyn Laycock. "Biomimetic Peptide Nanowires Designed for Conductivity." ACS Omega 4, no. 1 (January 22, 2019): 1748–56. http://dx.doi.org/10.1021/acsomega.8b02231.

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Oliver‐Cervelló, Lluís, Helena Martin‐Gómez, Leslie Reyes, Fatima Noureddine, Elisabetta Ada Cavalcanti‐Adam, Maria‐Pau Ginebra, and Carlos Mas‐Moruno. "Biomimetic Peptides: An Engineered Biomimetic Peptide Regulates Cell Behavior by Synergistic Integrin and Growth Factor Signaling (Adv. Healthcare Mater. 7/2021)." Advanced Healthcare Materials 10, no. 7 (April 2021): 2170032. http://dx.doi.org/10.1002/adhm.202170032.

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Feese, Elke, Hanna S. Gracz, Paul D. Boyle, and Reza A. Ghiladi. "Towards microbe-targeted photosensitizers: Synthesis, characterization and in vitro photodynamic inactivation of the tuberculosis model pathogen M. smegmatis by porphyrin-peptide conjugates." Journal of Porphyrins and Phthalocyanines 23, no. 11n12 (December 2019): 1414–39. http://dx.doi.org/10.1142/s1088424619501505.

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Porphyrin-peptide conjugates have a breadth of potential applications, including use in photodynamic therapy, boron neutron capture therapy, as fluorescence imaging tags for tracking subcellular localization, as magnetic resonance imaging (MRI) positive-contrast reagents and as biomimetic catalysts. Here, we have explored three general routes to porphyrin-peptide conjugates using the Cu(I)-catalyzed Huisgen-Medal-Sharpless 1,3-dipolar cycloaddition of peptide-containing azides with a terminal alkyne-containing porphyrin, thereby generating porphyrin-peptide conjugates (PPCs) comprised of a cationic porphyrin coupled to short antimicrobial peptides. In addition to characterizing the PPCs using a variety of spectroscopic (UV-vis, [Formula: see text]H- and [Formula: see text]C-NMR) and mass spectrometric methods, we evaluated their efficacy as photosensitizers for the in vitro photodynamic inactivation of Mycobacterium smegmatis as a model for the pathogen Mycobacterium tuberculosis. Difficulties that needed to be overcome for the efficient synthesis of PPCs were the limited solubility of the quaternized pyridyl porphyrin in common solvents, undesired (de)metallation and transmetallation, and chromatographic purification. Photodynamic inactivation studies of a small library of PPCs against Mycobacterium smegmatis confirmed our hypothesis that the porphyrin-based photosensitizer maintains its ability to efficiently inactivate bacteria when conjugated to a small peptide by upwards of 5–6 log units (99.999[Formula: see text]%) using white light illumination (400–700 nm, 60 mW/cm[Formula: see text], 30 min). Further, hemolysis assays revealed the lack of toxicity of the PPCs against sheep blood at concentrations employed for in vitro photodynamic inactivation. Taken together, the results demonstrated the ability of PPCs to maintain their antimicrobial photodynamic inactivation efficacy when possessing a short cationic peptides for enabling the potential targeting of pathogens in vivo.

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Del Favero, Giorgia, Friedrich Bialas, Stephanie Grabher, Anja Wittig, Birgit Bräuer, Dagmar Gerthsen, Cécile Echalier, Meder Kamalov, Doris Marko, and Christian F. W. Becker. "Silica particles with a quercetin–R5 peptide conjugate are taken up into HT-29 cells and translocate into the nucleus." Chemical Communications 55, no. 65 (2019): 9649–52. http://dx.doi.org/10.1039/c9cc02215e.

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Ramos-Martín, Francisco, Claudia Herrera-León, Viviane Antonietti, Pascal Sonnet, Catherine Sarazin, and Nicola D’Amelio. "Antimicrobial Peptide K11 Selectively Recognizes Bacterial Biomimetic Membranes and Acts by Twisting Their Bilayers." Pharmaceuticals 14, no. 1 (December 22, 2020): 1. http://dx.doi.org/10.3390/ph14010001.

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K11 is a synthetic peptide originating from the introduction of a lysine residue in position 11 within the sequence of a rationally designed antibacterial scaffold. Despite its remarkable antibacterial properties towards many ESKAPE bacteria and its optimal therapeutic index (320), a detailed description of its mechanism of action is missing. As most antimicrobial peptides act by destabilizing the membranes of the target organisms, we investigated the interaction of K11 with biomimetic membranes of various phospholipid compositions by liquid and solid-state NMR. Our data show that K11 can selectively destabilize bacterial biomimetic membranes and torque the surface of their bilayers. The same is observed for membranes containing other negatively charged phospholipids which might suggest additional biological activities. Molecular dynamic simulations reveal that K11 can penetrate the membrane in four steps: after binding to phosphate groups by means of the lysine residue at the N-terminus (anchoring), three couples of lysine residues act subsequently to exert a torque in the membrane (twisting) which allows the insertion of aromatic side chains at both termini (insertion) eventually leading to the flip of the amphipathic helix inside the bilayer core (helix flip and internalization).

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Yang, Weitao, Weisheng Guo, Jin Chang, and Bingbo Zhang. "Protein/peptide-templated biomimetic synthesis of inorganic nanoparticles for biomedical applications." Journal of Materials Chemistry B 5, no. 3 (2017): 401–17. http://dx.doi.org/10.1039/c6tb02308h.

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Shih, Han, Hung-Yi Liu, and Chien-Chi Lin. "Improving gelation efficiency and cytocompatibility of visible light polymerized thiol-norbornene hydrogels via addition of soluble tyrosine." Biomaterials Science 5, no. 3 (2017): 589–99. http://dx.doi.org/10.1039/c6bm00778c.

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A biomimetic PEG-peptide hydrogel was developed through tyrosine-assisted visible-light thiol-norbornene crosslinking. Soluble tyrosine improves crosslinking and enhances the cytocompatibility of hydrogels.

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36

Valko, Klara Livia, Mark Kindy, James Evans, and Dorothy Ko. "In vitro biomimetic HPLC and in vivo characterisation of GM6, an endogenous regulator peptide drug candidate for amyotrophic lateral sclerosis." ADMET and DMPK 6, no. 2 (June 16, 2018): 176–89. http://dx.doi.org/10.5599/admet.547.

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Amyotrophic lateral sclerosis (ALS) is an idiopathic, fatal neurodegenerative disease of the human motor system. Subunits of the 33-amino acid containing motorneurontrophic factor (MNTF) have been investigated and GM6 has been found as a potential peptide therapeutic for ALS. This linear peptide drug candidate has been characterized by HPLC based physicochemical and biomimetic measurements to estimate its in vivo distribution behavior and to estimate its cell penetration and brain to plasma concentration ratio. The free tissue concentration vs time profile has been estimated using the measured physicochemical and biomimetic properties of the intact GM6 molecules and its microsomal stability. The in vitro and in vivo measurements supported the estimated in vivo distribution behavior of GM6.

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Gharaei, Robabeh, Giuseppe Tronci, Parikshit Goswami, Robert P. Wynn Davies, Jennifer Kirkham, and Stephen J. Russell. "Biomimetic peptide enriched nonwoven scaffolds promote calcium phosphate mineralisation." RSC Advances 10, no. 47 (2020): 28332–42. http://dx.doi.org/10.1039/d0ra02446e.

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38

Levin, Aviad, Tuuli A. Hakala, Lee Schnaider, Gonçalo J. L. Bernardes, Ehud Gazit, and Tuomas P. J. Knowles. "Biomimetic peptide self-assembly for functional materials." Nature Reviews Chemistry 4, no. 11 (September 15, 2020): 615–34. http://dx.doi.org/10.1038/s41570-020-0215-y.

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39

Tamaki, Makoto, Seiji Komiya, Sadatoshi Akabori, and Ichiro Muramatsu. "Biomimetic synthesis of a peptide antibiotic, gratisin." Journal of the Chemical Society, Perkin Transactions 1, no. 14 (1997): 2045–50. http://dx.doi.org/10.1039/a701537b.

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40

Lunkad, Raju, Anastasiia Murmiliuk, Zdeněk Tošner, Miroslav Štěpánek, and Peter Košovan. "Role of pKA in Charge Regulation and Conformation of Various Peptide Sequences." Polymers 13, no. 2 (January 9, 2021): 214. http://dx.doi.org/10.3390/polym13020214.

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Peptides containing amino acids with ionisable side chains represent a typical example of weak ampholytes, that is, molecules with multiple titratable acid and base groups, which generally exhibit charge regulating properties upon changes in pH. Charged groups on an ampholyte interact electrostatically with each other, and their interaction is coupled to conformation of the (macro)molecule, resulting in a complex feedback loop. Their charge-regulating properties are primarily determined by the pKA of individual ionisable side-chains, modulated by electrostatic interactions between the charged groups. The latter is determined by the amino acid sequence in the peptide chain. In our previous work we introduced a simple coarse-grained model of a flexible peptide. We validated it against experiments, demonstrating its ability to quantitatively predict charge on various peptides in a broad range of pH. In the current work, we investigated two types of peptide sequences: diblock and alternating, each of them consisting of an equal number of amino acids with acid and base side-chains. We showed that changing the sequence while keeping the same overall composition has a profound effect on the conformation, whereas it practically does not affect total charge on the peptide. Nevertheless, the sequence significantly affects the charge state of individual groups, showing that the zero net effect on the total charge is a consequence of unexpected cancellation of effects. Furthermore, we investigated how the difference between the pKA of acid and base side chains affects the charge and conformation of the peptide, showing that it is possible to tune the charge-regulating properties by following simple guiding principles based on the pKA and on the amino acid sequence. Our current results provide a theoretical basis for understanding of the complex coupling between the ionisation and conformation in flexible polyampholytes, including synthetic polymers, biomimetic materials and biological molecules, such as intrinsically disordered proteins, whose function can be regulated by changes in the pH.

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41

Lunkad, Raju, Anastasiia Murmiliuk, Zdeněk Tošner, Miroslav Štěpánek, and Peter Košovan. "Role of pKA in Charge Regulation and Conformation of Various Peptide Sequences." Polymers 13, no. 2 (January 9, 2021): 214. http://dx.doi.org/10.3390/polym13020214.

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Peptides containing amino acids with ionisable side chains represent a typical example of weak ampholytes, that is, molecules with multiple titratable acid and base groups, which generally exhibit charge regulating properties upon changes in pH. Charged groups on an ampholyte interact electrostatically with each other, and their interaction is coupled to conformation of the (macro)molecule, resulting in a complex feedback loop. Their charge-regulating properties are primarily determined by the pKA of individual ionisable side-chains, modulated by electrostatic interactions between the charged groups. The latter is determined by the amino acid sequence in the peptide chain. In our previous work we introduced a simple coarse-grained model of a flexible peptide. We validated it against experiments, demonstrating its ability to quantitatively predict charge on various peptides in a broad range of pH. In the current work, we investigated two types of peptide sequences: diblock and alternating, each of them consisting of an equal number of amino acids with acid and base side-chains. We showed that changing the sequence while keeping the same overall composition has a profound effect on the conformation, whereas it practically does not affect total charge on the peptide. Nevertheless, the sequence significantly affects the charge state of individual groups, showing that the zero net effect on the total charge is a consequence of unexpected cancellation of effects. Furthermore, we investigated how the difference between the pKA of acid and base side chains affects the charge and conformation of the peptide, showing that it is possible to tune the charge-regulating properties by following simple guiding principles based on the pKA and on the amino acid sequence. Our current results provide a theoretical basis for understanding of the complex coupling between the ionisation and conformation in flexible polyampholytes, including synthetic polymers, biomimetic materials and biological molecules, such as intrinsically disordered proteins, whose function can be regulated by changes in the pH.

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Wang, Kun, Xiuqing Wang, Haoran Li, Sainan Zheng, Qian Ren, Yufei Wang, Yumei Niu, Wei Li, Xuedong Zhou, and Linglin Zhang. "A statherin-derived peptide promotes hydroxyapatite crystallization and in situ remineralization of artificial enamel caries." RSC Advances 8, no. 3 (2018): 1647–55. http://dx.doi.org/10.1039/c7ra12032j.

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A novel biomimetic peptide inspired by salivary statherin was developed and exhibited beneficial potentials in promoting remineralization of hydroxyapatite on tooth enamel surface, providing a desirable alternative restorative strategy against dental caries.

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43

Devnarain, Nikita, Ayman Y. Waddad, Beatriz G. de la Torre, Fernando Albericio, and Thirumala Govender. "Novel Biomimetic Human TLR2-Derived Peptides for Potential Targeting of Lipoteichoic Acid: An In Silico Assessment." Biomedicines 9, no. 8 (August 21, 2021): 1063. http://dx.doi.org/10.3390/biomedicines9081063.

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Antimicrobial resistance is one of the most significant threats to health and economy around the globe and has been compounded by the emergence of COVID-19, raising important consequences for antimicrobial resistance development. Contrary to conventional targeting approaches, the use of biomimetic application via nanoparticles for enhanced cellular targeting, cell penetration and localized antibiotic delivery has been highlighted as a superior approach to identify novel targeting ligands for combatting antimicrobial resistance. Gram-positive bacterial cell walls contain lipoteichoic acid (LTA), which binds specifically to Toll-like receptor 2 (TLR2) on human macrophages. This phenomenon has the potential to be exploited for the design of biomimetic peptides for antibacterial application. In this study, we have derived peptides from sequences present in human TLR2 that bind to LTA with high affinity. In silico approaches including molecular modelling, molecular docking, molecular dynamics, and thermodynamics have enabled the identification of these crucial binding amino acids, the design of four novel biomimetic TLR2-derived peptides and their LTA binding potential. The outcomes of this study have revealed that one of these novel peptides binds to LTA more strongly and stably than the other three peptides and has the potential to enhance LTA targeting and bacterial cell penetration.

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44

Cheraghi, Roya, Mahboobeh Nazari, Mohsen Alipour, and Saman Hosseinkhani. "Stepwise Development of Biomimetic Chimeric Peptides for Gene Delivery." Protein & Peptide Letters 27, no. 8 (September 24, 2020): 698–710. http://dx.doi.org/10.2174/0929866527666200206153328.

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Gene-based therapy largely relies on the vector type that allows a selective and efficient transfection into the target cells with maximum efficacy and minimal toxicity. Although, genes delivered utilizing modified viruses transfect efficiently and precisely, these vectors can cause severe immunological responses and are potentially carcinogenic. A promising method of overcoming this limitation is the use of non-viral vectors, including cationic lipids, polymers, dendrimers, and peptides, which offer potential routes for compacting DNA for targeted delivery. Although non-viral vectors exhibit reduced transfection efficiency compared to their viral counterpart, their superior biocompatibility, non-immunogenicity and potential for large-scale production make them increasingly attractive for modern therapy. There has been a great deal of interest in the development of biomimetic chimeric peptides. Biomimetic chimeric peptides contain different motifs for gene translocation into the nucleus of the desired cells. They have motifs for gene targeting into the desired cell, condense DNA into nanosize particles, translocate the gene into the nucleus and enhance the release of the particle into the cytoplasm. These carriers were developed in recent years. This review highlights the stepwise development of the biomimetic chimeric peptides currently being used in gene delivery.

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Raja, Iruthayapandi Selestin, Chuntae Kim, Su-Jin Song, Yong Cheol Shin, Moon Sung Kang, Suong-Hyu Hyon, Jin-Woo Oh, and Dong-Wook Han. "Virus-Incorporated Biomimetic Nanocomposites for Tissue Regeneration." Nanomaterials 9, no. 7 (July 15, 2019): 1014. http://dx.doi.org/10.3390/nano9071014.

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Owing to the astonishing properties of non-harmful viruses, tissue regeneration using virus-based biomimetic materials has been an emerging trend recently. The selective peptide expression and enrichment of the desired peptide on the surface, monodispersion, self-assembly, and ease of genetic and chemical modification properties have allowed viruses to take a long stride in biomedical applications. Researchers have published many reviews so far describing unusual properties of virus-based nanoparticles, phage display, modification, and possible biomedical applications, including biosensors, bioimaging, tissue regeneration, and drug delivery, however the integration of the virus into different biomaterials for the application of tissue regeneration is not yet discussed in detail. This review will focus on various morphologies of virus-incorporated biomimetic nanocomposites in tissue regeneration and highlight the progress, challenges, and future directions in this area.

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Calvelo, Martín, Saulo Vázquez, and Rebeca García-Fandiño. "Molecular dynamics simulations for designing biomimetic pores based on internally functionalized self-assembling α,γ-peptide nanotubes." Physical Chemistry Chemical Physics 17, no. 43 (2015): 28586–601. http://dx.doi.org/10.1039/c5cp04200c.

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Internally functionalized peptide nanotubes composed of α- and γ-amino acids self assembled in lipid bilayers are studied using Molecular Dynamics simulations, projecting a promising future for their use as biomimetic channels when properly innerderivatized.

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Rauschenberg, Melanie, Susanne Bomke, Uwe Karst, and Bart Jan Ravoo. "Dynamic Peptides as Biomimetic Carbohydrate Receptors." Angewandte Chemie International Edition 49, no. 40 (August 26, 2010): 7340–45. http://dx.doi.org/10.1002/anie.201002847.

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48

Paterson, D. J., J. Reboud, R. Wilson, M. Tassieri, and J. M. Cooper. "Integrating microfluidic generation, handling and analysis of biomimetic giant unilamellar vesicles." Lab Chip 14, no. 11 (2014): 1806–10. http://dx.doi.org/10.1039/c4lc00199k.

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Al Nahas, K., J. Cama, M. Schaich, K. Hammond, S. Deshpande, C. Dekker, M. G. Ryadnov, and U. F. Keyser. "A microfluidic platform for the characterisation of membrane active antimicrobials." Lab on a Chip 19, no. 5 (2019): 837–44. http://dx.doi.org/10.1039/c8lc00932e.

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Peng, Fei, Wensheng Zhang, and Feng Qiu. "Self-assembling Peptides in Current Nanomedicine: Versatile Nanomaterials for Drug Delivery." Current Medicinal Chemistry 27, no. 29 (September 2, 2020): 4855–81. http://dx.doi.org/10.2174/0929867326666190712154021.

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Background: The development of modern nanomedicine greatly depends on the involvement of novel materials as drug delivery system. In order to maximize the therapeutic effects of drugs and minimize their side effects, a number of natural or synthetic materials have been widely investigated for drug delivery. Among these materials, biomimetic self-assembling peptides (SAPs) have received more attention in recent years. Considering the rapidly growing number of SAPs designed for drug delivery, a summary of how SAPs-based drug delivery systems were designed, would be beneficial. Method: We outlined research works on different SAPs that have been investigated as carriers for different drugs, focusing on the design of SAPs nanomaterials and how they were used for drug delivery in different strategies. Results: Based on the principle rules of chemical complementarity and structural compatibility, SAPs such as ionic self-complementary peptide, peptide amphiphile and surfactant-like peptide could be designed. Determined by the features of peptide materials and the drugs to be delivered, different strategies such as hydrogel embedding, hydrophobic interaction, electrostatic interaction, covalent conjugation or the combination of them could be employed to fabricate SAPs-drug complex, which could achieve slow release, targeted or environment-responsive delivery of drugs. Furthermore, some SAPs could also be combined with other types of materials for drug delivery, or even act as drug by themselves. Conclusion: Various types of SAPs have been designed and used for drug delivery following various strategies, suggesting that SAPs as a category of versatile nanomaterials have promising potential in the field of nanomedicine.

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Journal articles on the topic 'Biomimetické peptidy'

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