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Journal articles on the topic 'Self-assembling Amino Acid'

Author: Grafiati

Published: 7 September 2023

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1

Liu, Yi, Eunkyoung Kim, Rein V. Ulijn, William E. Bentley, and Gregory F. Payne. "Reversible Electroaddressing of Self-assembling Amino-Acid Conjugates." Advanced Functional Materials 21, no. 9 (March 7, 2011): 1575–80. http://dx.doi.org/10.1002/adfm.201002020.

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2

Yokoi, Hidenori, and Takatoshi Kinoshita. "Strategy for Designing Self-Assembling Peptides to Prepare Transparent Nanofiber Hydrogel at Neutral pH." Journal of Nanomaterials 2012 (2012): 1–9. http://dx.doi.org/10.1155/2012/537262.

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This study examined the formation of nanofiber hydrogels at neutral pH for 16 types of peptides with different net charges, hydrophobicities, and degrees of polymerization. The peptides formed various hydrogels depending on the arrangement of charged amino acids in the antiparallelβ-sheet structure. Circular dichroism (CD) measurement, atomic force microscopy (AFM), visible light spectroscopy, and dynamic viscoelasticity measurement showed that the formation of transparent nanofiber hydrogels in peptides requires at least 2 additional positively or negatively charged amino acids per peptide. When designing the amino acid sequence, it is important to consider both the net charge and position of the charged amino acids, and it should be ensured that basic amino acids do not face other basic ones in the antiparallelβ-sheet structure. Peptides that had charged amino acids clustered at the center of the nanofiber formed rigid gels.

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3

Moriuchi, Toshiyuki, and Toshikazu Hirao. "Chirality Organization Induced by Self-Assembling Properties of Amino Acid Units." Journal of Synthetic Organic Chemistry, Japan 59, no. 12 (2001): 1195–203. http://dx.doi.org/10.5059/yukigoseikyokaishi.59.1195.

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4

Warren, James P., Matthew P. Culbert, Danielle E. Miles, Steven Maude, Ruth K. Wilcox, and Paul A. Beales. "Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions." Gels 9, no. 6 (May 26, 2023): 441. http://dx.doi.org/10.3390/gels9060441.

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Self-assembling peptides are a promising biomaterial with potential applications in medical devices and drug delivery. In the right combination of conditions, self-assembling peptides can form self-supporting hydrogels. Here, we describe how balancing attractive and repulsive intermolecular forces is critical for successful hydrogel formation. Electrostatic repulsion is tuned by altering the peptide’s net charge, and intermolecular attractions are controlled through the degree of hydrogen bonding between specific amino acid residues. We find that an overall net peptide charge of +/−2 is optimal to facilitate the assembly of self-supporting hydrogels. If the net peptide charge is too low then dense aggregates form, while a high molecular charge inhibits the formation of larger structures. At a constant charge, altering the terminal amino acids from glutamine to serine decreases the degree of hydrogen bonding within the assembling network. This tunes the viscoelastic properties of the gel, reducing the elastic modulus by two to three orders of magnitude. Finally, hydrogels could be formed from glutamine-rich, highly charged peptides by mixing the peptides in combinations with a resultant net charge of +/−2. These results illustrate how understanding and controlling self-assembly mechanisms through modulating intermolecular interactions can be exploited to derive a range of structures with tuneable properties.

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5

Singh, Pijush, Souvik Misra, Nayim Sepay, Sanjoy Mondal, Debes Ray, Vinod K. Aswal, and Jayanta Nanda. "Self-assembling behaviour of a modified aromatic amino acid in competitive medium." Soft Matter 16, no. 28 (2020): 6599–607. http://dx.doi.org/10.1039/d0sm00584c.

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The self-assembly and photophysical properties of 4-nitrophenylalanine (4NP) are changed with the alteration of solvent and final self-assembly state of 4NP in competitive solvent mixture and are dictated by the solvent ratio.

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6

Tinajero-Díaz, E., A. Martínez de Ilarduya, B. Cavanagh, A. Heise, and S. Muñoz-Guerra. "Poly(amino acid)-grafted polymacrolactones. Synthesis, self-assembling and ionic coupling properties." Reactive and Functional Polymers 143 (October 2019): 104316. http://dx.doi.org/10.1016/j.reactfunctpolym.2019.104316.

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7

Liu, Jing, Can Wu, Guoru Dai, Feng Feng, Yuquan Chi, Keming Xu, and Wenying Zhong. "Molecular self-assembly of a tyroservatide-derived octapeptide and hydroxycamptothecin for enhanced therapeutic efficacy." Nanoscale 13, no. 9 (2021): 5094–102. http://dx.doi.org/10.1039/d0nr08741f.

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A pure l-amino acid-based molecular hydrogel was designed through conjugation of an anticancer tripeptide tyroservatide (YSV) with a self-assembling moiety, which enhanced therapeutic efficacy of both YSV and hydroxycamptothecin in vitro and in vivo.

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8

Arungani NS and Kalaivani Venkadessan. "PEPTIDES IN REMINERALISATION - A REVIEW." International Journal of Community Dentistry 10, no. 1 (June 14, 2022): 18–22. http://dx.doi.org/10.56501/intjcommunitydent.v10i1.48.

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Caries develops when the remineralization and demineralization equilibriums are out of balance. When the demineralization level exceeds 30%, the enamel suffers irreversible damage. As a result, non-invasive techniques for early detection and management of these reversible incipient lesions are recommended. Fluorides are the most important and effective, and their local efficacy has been widely researched. Many new innovations have been introduced for remineralisation of early lesion, such as ACP-CPP, Self-assembling peptides, etc., CPP–ACP is a milk product that aids in remineralization and dental caries prevention. Amorphous calcium phosphate is delivered by casein phosphopeptide, which also aids ACP binding to dental enamel. The natural amino acids Glutamine, Glutamic acid, Phenylalanine, Tryptophan, Serine, and Arginine make up the self-assembling peptide P11-4, which is intended to form brils at low pH and to be monomeric at higher pH. Furthermore, studies to be conducted to learn about the mechanism of Self assembling peptides.

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9

Lamas, Alejandro, Arcadio Guerra, Manuel Amorín, and Juan R. Granja. "New self-assembling peptide nanotubes of large diameter using δ-amino acids." Chemical Science 9, no. 43 (2018): 8228–33. http://dx.doi.org/10.1039/c8sc02276c.

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Here we show that 4-aminocyclohexanecarboxylic acid is a rigid stretcher building block for the preparation of cyclic peptides that self-assemble to form peptide nanotubes with large diameter and hydrophobic pores.

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10

Rang, Alexander, Martin Nieger, Marianne Engeser, Arne Lützen, and Christoph A. Schalley. "Self-assembling squares with amino acid-decorated bipyridines: heterochiral self-sorting of dynamically interconverting diastereomers." Chemical Communications, no. 39 (2008): 4789. http://dx.doi.org/10.1039/b806916f.

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11

Mills, Jeremy H., William Sheffler, Maraia E. Ener, Patrick J. Almhjell, Gustav Oberdorfer, José Henrique Pereira, Fabio Parmeggiani, Banumathi Sankaran, Peter H. Zwart, and David Baker. "Computational design of a homotrimeric metalloprotein with a trisbipyridyl core." Proceedings of the National Academy of Sciences 113, no. 52 (December 8, 2016): 15012–17. http://dx.doi.org/10.1073/pnas.1600188113.

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Metal-chelating heteroaryl small molecules have found widespread use as building blocks for coordination-driven, self-assembling nanostructures. The metal-chelating noncanonical amino acid (2,2′-bipyridin-5yl)alanine (Bpy-ala) could, in principle, be used to nucleate specific metalloprotein assemblies if introduced into proteins such that one assembly had much lower free energy than all alternatives. Here we describe the use of the Rosetta computational methodology to design a self-assembling homotrimeric protein with [Fe(Bpy-ala)3]2+ complexes at the interface between monomers. X-ray crystallographic analysis of the homotrimer showed that the design process had near-atomic-level accuracy: The all-atom rmsd between the design model and crystal structure for the residues at the protein interface is ∼1.4 Å. These results demonstrate that computational protein design together with genetically encoded noncanonical amino acids can be used to drive formation of precisely specified metal-mediated protein assemblies that could find use in a wide range of photophysical applications.

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12

Rosselin, Marie, Grégory Meyer, Pierre Guillet, Thomas Cheviet, Guillaume Walther, Annette Meister, Dimitra Hadjipavlou-Litina, and Grégory Durand. "Divalent Amino-Acid-Based Amphiphilic Antioxidants: Synthesis, Self-Assembling Properties, and Biological Evaluation." Bioconjugate Chemistry 27, no. 3 (February 22, 2016): 772–81. http://dx.doi.org/10.1021/acs.bioconjchem.6b00002.

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13

Guerra, Arcadio, Roberto J. Brea, Manuel Amorín, Luis Castedo, and Juan R. Granja. "Self-assembling properties of all γ-cyclic peptides containing sugar amino acid residues." Organic & Biomolecular Chemistry 10, no. 44 (2012): 8762. http://dx.doi.org/10.1039/c2ob26612a.

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14

Koga, Tomoyuki, Eri Aso, and Nobuyuki Higashi. "Novel Self-Assembling Amino Acid-Derived Block Copolymer with Changeable Polymer Backbone Structure." Langmuir 32, no. 47 (June 24, 2016): 12378–86. http://dx.doi.org/10.1021/acs.langmuir.6b01617.

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15

Moriuchi, Toshiyuki, and Toshikazu Hirao. "ChemInform Abstract: Chirality Organization Induced by Self-Assembling Properties of Amino Acid Units." ChemInform 33, no. 21 (May 21, 2010): no. http://dx.doi.org/10.1002/chin.200221246.

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16

La Manna, Sara, Concetta Di Natale, Valentina Onesto, and Daniela Marasco. "Self-Assembling Peptides: From Design to Biomedical Applications." International Journal of Molecular Sciences 22, no. 23 (November 23, 2021): 12662. http://dx.doi.org/10.3390/ijms222312662.

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Self-assembling peptides could be considered a novel class of agents able to harvest an array of micro/nanostructures that are highly attractive in the biomedical field. By modifying their amino acid composition, it is possible to mime several biological functions; when assembled in micro/nanostructures, they can be used for a variety of purposes such as tissue regeneration and engineering or drug delivery to improve drug release and/or stability and to reduce side effects. Other significant advantages of self-assembled peptides involve their biocompatibility and their ability to efficiently target molecular recognition sites. Due to their intrinsic characteristics, self-assembled peptide micro/nanostructures are capable to load both hydrophobic and hydrophilic drugs, and they are suitable to achieve a triggered drug delivery at disease sites by inserting in their structure’s stimuli-responsive moieties. The focus of this review was to summarize the most recent and significant studies on self-assembled peptides with an emphasis on their application in the biomedical field.

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17

Nelli, Srinivasa Rao, Jhong-Hua Lin, Thi Ngoc Anh Nguyen, Dion Tzu-Huan Tseng, Satish Kumar Talloj, and Hsin-Chieh Lin. "Influence of amino acid side chains on the formation of two component self-assembling nanofibrous hydrogels." New Journal of Chemistry 41, no. 3 (2017): 1229–34. http://dx.doi.org/10.1039/c6nj02820a.

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18

Lehrman, Jessica A., Honggang Cui, Wei-Wen Tsai, Tyson J. Moyer, and Samuel I. Stupp. "Supramolecular control of self-assembling terthiophene–peptide conjugates through the amino acid side chain." Chemical Communications 48, no. 78 (2012): 9711. http://dx.doi.org/10.1039/c2cc34375d.

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19

Caplan, Michael R., Elissa M. Schwartzfarb, Shuguang Zhang, Roger D. Kamm, and Douglas A. Lauffenburger. "Control of self-assembling oligopeptide matrix formation through systematic variation of amino acid sequence." Biomaterials 23, no. 1 (January 2002): 219–27. http://dx.doi.org/10.1016/s0142-9612(01)00099-0.

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20

Gaynanova, Gulnara, Leysan Vasileva, Ruslan Kashapov, Darya Kuznetsova, Rushana Kushnazarova, Anna Tyryshkina, Elmira Vasilieva, Konstantin Petrov, Lucia Zakharova, and Oleg Sinyashin. "Self-Assembling Drug Formulations with Tunable Permeability and Biodegradability." Molecules 26, no. 22 (November 10, 2021): 6786. http://dx.doi.org/10.3390/molecules26226786.

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This review focuses on key topics in the field of drug delivery related to the design of nanocarriers answering the biomedicine criteria, including biocompatibility, biodegradability, low toxicity, and the ability to overcome biological barriers. For these reasons, much attention is paid to the amphiphile-based carriers composed of natural building blocks, lipids, and their structural analogues and synthetic surfactants that are capable of self-assembly with the formation of a variety of supramolecular aggregates. The latter are dynamic structures that can be used as nanocontainers for hydrophobic drugs to increase their solubility and bioavailability. In this section, biodegradable cationic surfactants bearing cleavable fragments are discussed, with ester- and carbamate-containing analogs, as well as amino acid derivatives received special attention. Drug delivery through the biological barriers is a challenging task, which is highlighted by the example of transdermal method of drug administration. In this paper, nonionic surfactants are primarily discussed, including their application for the fabrication of nanocarriers, their surfactant-skin interactions, the mechanisms of modulating their permeability, and the factors controlling drug encapsulation, release, and targeted delivery. Different types of nanocarriers are covered, including niosomes, transfersomes, invasomes and chitosomes, with their morphological specificity, beneficial characteristics and limitations discussed.

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21

Pasc, Andreea, Firmin Obounou Akong, Sedat Cosgun, and Christine Gérardin. "Differences between β-Ala and Gly-Gly in the design of amino acids-based hydrogels." Beilstein Journal of Organic Chemistry 6 (October 11, 2010): 973–77. http://dx.doi.org/10.3762/bjoc.6.109.

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Despite the continuous interest in organogels and hydrogels of low molecular weight gelators (LMWG), establishing the relationship between the molecular structure and the gelation mechanism is still a challenge. In this paper our interest focuses on the consequences of slight molecular modifications on the self-assembling behaviour of β-Ala vs Gly-Gly-based hydrogelators. Previously, in our group, amino acid based amphiphiles i.e. Gly-Gly-His-EO2-Alk, a trimodular amphiphile (containing three domains: H-bond donor and acceptor/hydrophilic/hydrophobic domain, respectively) were reported to act as hydrogelators and that the gelation properties were related to hydrogen bonding, hydrophobic interactions and π-π stacking. Herein, β-Ala-His-EO2-Alk was fully characterised by FT-IR, NMR, SAXS and SEM and the gelation mechanism is discussed. It appears that the number of amide groups determines the self-assembling behaviour into 1D or 2D/3D networks as a result of intimate interactions between gelator molecules.

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22

Ahmed, Saleh A., Xavier Sallenave, Frédéric Fages, Gudrun Mieden-Gundert, Walter M. Müller, Ute Müller, Fritz Vögtle, and Jean-Luc Pozzo. "Multiaddressable Self-Assembling Organogelators Based on 2H-Chromene andN-Acyl-1,ω-amino Acid Units†." Langmuir 18, no. 19 (September 2002): 7096–101. http://dx.doi.org/10.1021/la025545g.

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23

Jeong, Woo-jin, Soo hyun Kwon, and Yong-beom Lim. "Modular Self-Assembling Peptide Platform with a Tunable Thermoresponsiveness via a Single Amino Acid Substitution." Advanced Functional Materials 28, no. 35 (July 2, 2018): 1803114. http://dx.doi.org/10.1002/adfm.201803114.

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24

Lesiak, Marta, Aleksandra Augusciak-Duma, Anna Szydlo, Ksymena Pruszczynska, and Aleksander L. Sieron. "Specific inhibition of procollagen C-endopeptidase activity by synthetic peptide with conservative sequence found in chordin." Acta Biochimica Polonica 55, no. 2 (June 7, 2008): 297–305. http://dx.doi.org/10.18388/abp.2008_3076.

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Procollagen C-endopeptidase (BMP-1) and N-endopeptidase (ADAMTS-2) are key enzymes for correct and efficient conversion of fibrillar procollagens to their self assembling monomers. Thus, they have an essential role in building and controlling the quality of extracellular matrices (ECMs). Here, we tested inhibition of activity of the largest variant of BMP-1, a recombinant mammalian tolloid (mTld), in vitro by three synthetic peptides with conservative amino-acid sequences found in chordin using procollagen type I as a substrate. We also verified the specific action of best inhibitory 16 amino-acid peptide in the procollagen type I cleavage assay with the use of ADAMTS-2 (procollagen N-endopeptidase). Subsequently, we determined the critical residues and minimal sequence of six amino acids in the original 16 amino-acid peptide required to maintain the inhibitory potential. Studies on the interactions of 6 and 16 amino acid long peptides with the enzyme revealed their binding to non-catalytic, regulatory domains of mTld; the inhibitory activity was not due to the competition of peptides with the substrate for the enzyme active center, because mTld did not cleave the peptides. However, in the presence of mTld both peptides underwent cyclization by disulfide bond formation. Concluding, we have shown that procollagen C-endopeptidase may be specifically blocked via its non-catalytic domains by synthetic peptide consisting of 6 amino acids in the sequence found in highly conservative region of chordin. Thus, we hypothesize that the 6 amino-acid peptide could be a good candidate for anti-fibrotic drug development.

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25

Petropoulou, Katerina, Varvara Platania, Maria Chatzinikolaidou, and Anna Mitraki. "A Doubly Fmoc-Protected Aspartic Acid Self-Assembles into Hydrogels Suitable for Bone Tissue Engineering." Materials 15, no. 24 (December 14, 2022): 8928. http://dx.doi.org/10.3390/ma15248928.

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Hydrogels have been used as scaffolds for biomineralization in tissue engineering and regenerative medicine for the repair and treatment of many tissue types. In the present work, we studied an amino acid-based material that is attached to protecting groups and self-assembles into biocompatible and stable nanostructures that are suitable for tissue engineering applications. Specifically, the doubly protected aspartic residue (Asp) with fluorenyl methoxycarbonyl (Fmoc) protecting groups have been shown to lead to the formation of well-ordered fibrous structures. Many amino acids and small peptides which are modified with protecting groups display relatively fast self-assembly and exhibit remarkable physicochemical properties leading to three-dimensional (3D) networks, the trapping of solvent molecules, and forming hydrogels. In this study, the self-assembling fibrous structures are targeted toward calcium binding and act as nucleation points for the binding of the available phosphate groups. The cell viability, proliferation, and osteogenic differentiation of pre-osteoblastic cells cultured on the formed hydrogel under various conditions demonstrate that hydrogel formation in CaCl2 and CaCl2-Na2HPO4 solutions lead to calcium ion binding onto the hydrogels and enrichment with phosphate groups, respectively, rendering these mechanically stable hydrogels osteoinductive scaffolds for bone tissue engineering.

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26

Li, Mingyu, Mingyuan Liu, Yuna Shang, Chunhua Ren, Jianfeng Liu, Hongxing Jin, and Zhongyan Wang. "The substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides." RSC Advances 10, no. 23 (2020): 13900–13906. http://dx.doi.org/10.1039/c9ra10325b.

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27

Akkan, Cagri K., Deniz Hür, Lokman Uzun, and Bora Garipcan. "Amino acid conjugated self assembling molecules for enhancing surface wettability of fiber laser treated titanium surfaces." Applied Surface Science 366 (March 2016): 284–91. http://dx.doi.org/10.1016/j.apsusc.2016.01.083.

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28

Fung, Shan-Yu, Hong Yang, Parisa Sadatmousavi, Yuebiao Sheng, Tewodros Mamo, Reyhaneh Nazarian, and P. Chen. "Amino Acid Pairing for De Novo Design of Self-Assembling Peptides and Their Drug Delivery Potential." Advanced Functional Materials 21, no. 13 (May 2, 2011): 2456–64. http://dx.doi.org/10.1002/adfm.201002497.

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29

Koda, Yuta, and Yukio Nagasaki. "Newly Designed Cysteine-Based Self-Assembling Prodrugs for Sepsis Treatment." Pharmaceutics 15, no. 6 (June 20, 2023): 1775. http://dx.doi.org/10.3390/pharmaceutics15061775.

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Reactive oxygen species (ROS) are essential signaling molecules that maintain intracellular redox balance; however, the overproduction of ROS often causes dysfunction in redox homeostasis and induces serious diseases. Antioxidants are crucial candidates for reducing overproduced ROS; however, most antioxidants are less effective than anticipated. Therefore, we designed new polymer-based antioxidants based on the natural amino acid, cysteine (Cys). Amphiphilic block copolymers, composed of a hydrophilic poly(ethylene glycol) (PEG) segment and a hydrophobic poly(cysteine) (PCys) segment, were synthesized. In the PCys segment, the free thiol groups in the side chain were protected by thioester moiety. The obtained block copolymers formed self-assembling nanoparticles (NanoCys(Bu)) in water, and the hydrodynamic diameter was 40–160 nm, as determined by dynamic light scattering (DLS) measurements. NanoCys(Bu) was stable from pH 2 to 8 under aqueous conditions, as confirmed by the hydrodynamic diameter of NanoCys(Bu). Finally, NanoCys(Bu) was applied to sepsis treatment to investigate the potential of NanoCys(Bu). NanoCys(Bu) was supplied to BALB/cA mice by free drinking for two days, and lipopolysaccharide (LPS) was intraperitoneally injected into the mice to prepare a sepsis shock model (LPS = 5 mg per kg body weight (BW)). Compared with the Cys and no-treatment groups, NanoCys(Bu) prolonged the half-life by five to six hours. NanoCys(Bu), designed in this study, shows promise as a candidate for enhancing antioxidative efficacy and mitigating the adverse effect of cysteine.

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30

Koch, Franziska, Anne Wolff, Stephanie Mathes, Uwe Pieles, Sina Saxer, Bernd Kreikemeyer, and Kirsten Peters. "Amino acid composition of nanofibrillar self-assembling peptide hydrogels affects responses of periodontal tissue cells in vitro." International Journal of Nanomedicine Volume 13 (October 2018): 6717–33. http://dx.doi.org/10.2147/ijn.s173702.

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31

Taniguchi, Suguru, Noriko Watanabe, Takeru Nose, and Iori Maeda. "Development of short and highly potent self-assembling elastin-derived pentapeptide repeats containing aromatic amino acid residues." Journal of Peptide Science 22, no. 1 (December 10, 2015): 36–42. http://dx.doi.org/10.1002/psc.2837.

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32

Seoudi, Rania S., Annette Dowd, Mark Del Borgo, Ketav Kulkarni, Patrick Perlmutter, Marie-Isabel Aguilar, and Adam Mechler. "Amino acid sequence controls the self-assembled superstructure morphology of N-acetylated tri-β3-peptides." Pure and Applied Chemistry 87, no. 9-10 (October 1, 2015): 1021–28. http://dx.doi.org/10.1515/pac-2015-0108.

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AbstractPeptides based on unnatural β3-amino acids offer a versatile platform for the design of self-assembling nanostructures due to the folding stability of the 14-helix and the high symmetry of the side chains inherent in this geometry. We have previously described that N-terminal acetylation (Ac-) forms a supramolecular self-assembly motif that allows β3-peptides to assemble head-to-tail into a helical nanorod which then further bundles into hierarchical superstructures. Here we investigate the effect of the topography of the 14-helical nanorod on lateral self-assembly. Specifically, we report on the variations in the superstructure of three isomeric peptides comprising the same three β3-amino acid residues: β3-leucine (L), β3-isoleucine (I) β3-alanine (A) to give peptides Ac-β3[LIA], Ac-β3[IAL] and Ac-β3[ALI]. AFM imaging shows markedly different superstructures for the three peptides. Well defined synchrotron far-infrared spectra reveal uniform geometries with a high degree of similarity between the isomeric peptides in the amide modes of the 400–650 wavenumber range. Far-IR also confirms that the C-terminal carboxyl group is free in the assemblies, thus it is solvated in the dispersant. Hence, the differences in the superstructures formed by the fibers are defined primarily by van der Waals energy minimization between the varied cross sectional morphologies of the core nanorods.

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33

Caplan, Michael R., Elissa M. Schwartzfarb, Shuguang Zhang, Roger D. Kamm, and Douglas A. Lauffenburger. "Effects of systematic variation of amino acid sequence on the mechanical properties of a self-assembling, oligopeptide biomaterial." Journal of Biomaterials Science, Polymer Edition 13, no. 3 (January 2002): 225–36. http://dx.doi.org/10.1163/156856202320176493.

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34

Pacheco, Shaun, Takashi Kanou, Shan-Yu Fung, Kenny Chen, Daiyoon Lee, Xiaohui Bai, Shaf Keshavjee, and Mingyao Liu. "Formulation of hydrophobic therapeutics with self-assembling peptide and amino acid: A new platform for intravenous drug delivery." Journal of Controlled Release 239 (October 2016): 211–22. http://dx.doi.org/10.1016/j.jconrel.2016.08.038.

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35

Carter, Daniel C., Brenda Wright, W. Gray Jerome, John P. Rose, and Ellen Wilson. "A Unique Protein Self-Assembling Nanoparticle with Significant Advantages in Vaccine Development and Production." Journal of Nanomaterials 2020 (January 4, 2020): 1–10. http://dx.doi.org/10.1155/2020/4297937.

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Nanoparticles are playing an increasingly powerful role in vaccine development. Here, we report the repurposing of nonstructural proteins 10 and 11 (hereafter NSP10) from the replicase polyprotein 1a (pp1a) of the human SARS coronavirus (severe acute respiratory syndrome) as a novel self-assembling platform for bioengineered nanoparticles for a variety of applications including vaccines. NSP10 represents a 152 amino acid, 17 kD zinc finger transcription/regulatory protein which self-assembles to form a spherical 84 Å diameter nanoparticle with dodecahedral trigonal 32 point symmetry. As a self-assembling nanoparticle, NSP10 possesses numerous advantages in vaccine development and antigen display, including the unusual particle surface disposition of both the N- and C-termini. Each set of N- or C-termini is spatially disposed in a tetrahedral arrangement and positioned at optimal distances from the 3-fold axes (8-10 Å) to nucleate and stabilize the correct folding of complex helical or fibrous trimeric receptors, such as those responsible for viral tropism and cell infection. An application example in the exploratory development of a therapeutic vaccine for idiopathic pulmonary fibrosis (IPF), including preliminary analysis and immunogenic properties, is presented. The use of this system could accelerate the discovery and development of vaccines for a number of human, livestock, and veterinary applications.

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36

Šimoliūnas, Eugenijus, Lidija Truncaitė, Rasa Rutkienė, Simona Povilonienė, Karolis Goda, Algirdas Kaupinis, Mindaugas Valius, and Rolandas Meškys. "The Robust Self-Assembling Tubular Nanostructures Formed by gp053 from Phage vB_EcoM_FV3." Viruses 11, no. 1 (January 11, 2019): 50. http://dx.doi.org/10.3390/v11010050.

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The recombinant phage tail sheath protein, gp053, from Escherichia coli infecting myovirus vB_EcoM_FV3 (FV3) was able to self-assemble into long, ordered and extremely stable tubular structures (polysheaths) in the absence of other viral proteins. TEM observations revealed that those protein nanotubes varied in length (~10–1000 nm). Meanwhile, the width of the polysheaths (~28 nm) corresponded to the width of the contracted tail sheath of phage FV3. The formed protein nanotubes could withstand various extreme treatments including heating up to 100 °C and high concentrations of urea. To determine the shortest variant of gp053 capable of forming protein nanotubes, a set of N- or/and C-truncated as well as poly-His-tagged variants of gp053 were constructed. The TEM analysis of these mutants showed that up to 25 and 100 amino acid residues could be removed from the N and C termini, respectively, without disturbing the process of self-assembly. In addition, two to six copies of the gp053 encoding gene were fused into one open reading frame. All the constructed oligomers of gp053 self-assembled in vitro forming structures of different regularity. By using the modification of cysteines with biotin, the polysheaths were tested for exposed thiol groups. Polysheaths formed by the wild-type gp053 or its mutants possess physicochemical properties, which are very attractive for the construction of self-assembling nanostructures with potential applications in different fields of nanosciences.

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Hong, Yooseong, Raymond L. Legge, S. Zhang, and P. Chen. "Effect of Amino Acid Sequence and pH on Nanofiber Formation of Self-Assembling Peptides EAK16-II and EAK16-IV." Biomacromolecules 4, no. 5 (September 2003): 1433–42. http://dx.doi.org/10.1021/bm0341374.

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Jeong, Woo-jin, Soo hyun Kwon, and Yong-beom Lim. "Peptide Self-Assembly: Modular Self-Assembling Peptide Platform with a Tunable Thermoresponsiveness via a Single Amino Acid Substitution (Adv. Funct. Mater. 35/2018)." Advanced Functional Materials 28, no. 35 (August 2018): 1870243. http://dx.doi.org/10.1002/adfm.201870243.

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Lee, Aejin, McKensie L. Mason, Tao Lin, Shashi Bhushan Kumar, Devan Kowdley, Jacob H. Leung, Danah Muhanna, et al. "Amino Acid Nanofibers Improve Glycemia and Confer Cognitive Therapeutic Efficacy to Bound Insulin." Pharmaceutics 14, no. 1 (December 29, 2021): 81. http://dx.doi.org/10.3390/pharmaceutics14010081.

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Diabetes poses a high risk for debilitating complications in neural tissues, regulating glucose uptake through insulin-dependent and predominantly insulin-independent pathways. Supramolecular nanostructures provide a flexible strategy for combinatorial regulation of glycemia. Here, we compare the effects of free insulin to insulin bound to positively charged nanofibers comprised of self-assembling amino acid compounds (AACs) with an antioxidant-modified side chain moiety (AAC2) in both in vitro and in vivo models of type 1 diabetes. Free AAC2, free human insulin (hINS) and AAC2-bound-human insulin (AAC2-hINS) were tested in streptozotocin (STZ)-induced mouse model of type 1 diabetes. AAC2-hINS acted as a complex and exhibited different properties compared to free AAC2 or hINS. Mice treated with the AAC2-hINS complex were devoid of hypoglycemic episodes, had improved levels of insulin in circulation and in the brain, and increased expression of neurotransmitter taurine transporter, Slc6a6. Consequently, treatment with AAC2-hINS markedly advanced both physical and cognitive performance in mice with STZ-induced and genetic type 1 diabetes compared to treatments with free AAC2 or hINS. This study demonstrates that the flexible nanofiber AAC2 can serve as a therapeutic platform for the combinatorial treatment of diabetes and its complications.

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Matsusaki, Michiya, Ken-ichiro Hiwatari, Mariko Higashi, Tatsuo Kaneko, and Mitsuru Akashi. "Stably-dispersed and Surface-functional Bionanoparticles Prepared by Self-assembling Amphipathic Polymers of Hydrophilic Poly(γ-glutamic acid) Bearing Hydrophobic Amino Acids." Chemistry Letters 33, no. 4 (April 2004): 398–99. http://dx.doi.org/10.1246/cl.2004.398.

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Małuch, Izabela, Oktawian Stachurski, Paulina Kosikowska-Adamus, Marta Makowska, Marta Bauer, Dariusz Wyrzykowski, Aleksandra Hać, et al. "Double-Headed Cationic Lipopeptides: An Emerging Class of Antimicrobials." International Journal of Molecular Sciences 21, no. 23 (November 25, 2020): 8944. http://dx.doi.org/10.3390/ijms21238944.

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Antimicrobial peptides (AMPs) constitute a promising tool in the development of novel therapeutic agents useful in a wide range of bacterial and fungal infections. Among the modifications improving pharmacokinetic and pharmacodynamic characteristics of natural AMPs, an important role is played by lipidation. This study focuses on the newly designed and synthesized lipopeptides containing multiple Lys residues or their shorter homologues with palmitic acid (C16) attached to the side chain of a residue located in the center of the peptide sequence. The approach resulted in the development of lipopeptides representing a model of surfactants with two polar headgroups. The aim of this study is to explain how variations in the length of the peptide chain or the hydrocarbon side chain of an amino acid residue modified with C16, affect biological functions of lipopeptides, their self-assembling propensity, and their mode of action.

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Niwa, T., Masayoshi Tanaka, and Takatoshi Kinoshita. "Construction of Self-Organized Interface via Monodisperse Block Copolypeptide Amphiphile." Advanced Materials Research 11-12 (February 2006): 635–38. http://dx.doi.org/10.4028/www.scientific.net/amr.11-12.635.

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In order to construct an intelligent functional nano-interface, the self-organized structure of Langmuir-Blodgett (LB) film was investigated by atomic force microscopy (AFM). As a building block, a monodisperse loop-helix-helix triblock copolypeptide containing the helix of which hydrophobic L-leucine residues align on a single face, “leucine zipper”, was synthesized by recombinant DNA techniques with a designed amino acid sequence. AFM observation on the surface structure of LB films constructed at surface pressures of 2, 5 and 18 mN/m revealed that structural transition from ring- or disk-like aggregations to a lane-like fabrication occurred with compression of the copolypeptide membrane on the water of pH 4. The leucine zipper in the copolypeptide was suggested to perform as an important basis for nanostructure formation through a hydrophobic interaction. Exploitation of the recognition and specific binding sites in the copolypeptide will allow the self-assembling mechanism of the copolypeptide to be developed to a novel nano-template.

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Price, Joshua L., W. Seth Horne, and Samuel H. Gellman. "Structural Consequences of β-Amino Acid Preorganization in a Self-Assembling α/β-Peptide: Fundamental Studies of Foldameric Helix Bundles." Journal of the American Chemical Society 132, no. 35 (September 8, 2010): 12378–87. http://dx.doi.org/10.1021/ja103543s.

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Zhang, Huixi Violet, Frank Polzer, Michael J. Haider, Yu Tian, Jose A. Villegas, Kristi L. Kiick, Darrin J. Pochan, and Jeffery G. Saven. "Computationally designed peptides for self-assembly of nanostructured lattices." Science Advances 2, no. 9 (September 2016): e1600307. http://dx.doi.org/10.1126/sciadv.1600307.

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Folded peptides present complex exterior surfaces specified by their amino acid sequences, and the control of these surfaces offers high-precision routes to self-assembling materials. The complexity of peptide structure and the subtlety of noncovalent interactions make the design of predetermined nanostructures difficult. Computational methods can facilitate this design and are used here to determine 29-residue peptides that form tetrahelical bundles that, in turn, serve as building blocks for lattice-forming materials. Four distinct assemblies were engineered. Peptide bundle exterior amino acids were designed in the context of three different interbundle lattices in addition to one design to produce bundles isolated in solution. Solution assembly produced three different types of lattice-forming materials that exhibited varying degrees of agreement with the chosen lattices used in the design of each sequence. Transmission electron microscopy revealed the nanostructure of the sheetlike nanomaterials. In contrast, the peptide sequence designed to form isolated, soluble, tetrameric bundles remained dispersed and did not form any higher-order assembled nanostructure. Small-angle neutron scattering confirmed the formation of soluble bundles with the designed size. In the lattice-forming nanostructures, the solution assembly process is robust with respect to variation of solution conditions (pH and temperature) and covalent modification of the computationally designed peptides. Solution conditions can be used to control micrometer-scale morphology of the assemblies. The findings illustrate that, with careful control of molecular structure and solution conditions, a single peptide motif can be versatile enough to yield a wide range of self-assembled lattice morphologies across many length scales (1 to 1000 nm).

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Ilyukhin, Andrey B., Pavel S. Koroteev, and Vladimir M. Novotortsev. "Supramolecular interactions and self-assembling in adducts of cymantrenecarboxylic acid with amino derivatives of five- and six-membered heterocyclic N-bases." Journal of Molecular Structure 1187 (July 2019): 38–49. http://dx.doi.org/10.1016/j.molstruc.2019.03.054.

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Abdelghafour, Mohamed M., Ágota Deák, Tamás Kiss, Mária Budai-Szűcs, Gábor Katona, Rita Ambrus, Bálint Lőrinczi, et al. "Self-Assembling Injectable Hydrogel for Controlled Drug Delivery of Antimuscular Atrophy Drug Tilorone." Pharmaceutics 14, no. 12 (December 6, 2022): 2723. http://dx.doi.org/10.3390/pharmaceutics14122723.

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A two-component injectable hydrogel was suitably prepared for the encapsulation and prolonged release of tilorone which is an antimuscular atrophy drug. The rapid (7–45 s, depending on the polymer concentration) in situ solidifications of the hydrogel were evoked by the evolving Schiff-base bonds between the aldehyde groups of modified PVA (4-formyl benzoate PVA, PVA-CHO, 5.9 mol% functionalization degree) and the amino groups of 3-mercaptopropionate chitosan (CHIT-SH). The successful modification of the initial polymers was confirmed by both FTIR and NMR measurements; moreover, a new peak appeared in the FTIR spectrum of the 10% w/v PVA-CHO/CHIT-SH hydrogel at 1647 cm−1, indicating the formation of a Schiff base (–CH=N–) and confirming the interaction between the NH2 groups of CHIT–SH and the CHO groups of PVA-CHO for the formation of the dynamic hydrogel. The reaction between the NH2 and CHO groups of the modified biopolymers resulted in a significant increase in the hydrogel’s viscosity which was more than one thousand times greater (9800 mPa·s) than that of the used polymer solutions, which have a viscosity of only 4.6 and 5.8 mPa·s, respectively. Furthermore, the initial chitosan was modified with mercaptopropionic acid (thiol content = 201.85 ± 12 µmol/g) to increase the mucoadhesive properties of the hydrogel. The thiolated chitosan showed a significant increase (~600 mN/mm) in adhesion to the pig intestinal membrane compared to the initial one (~300 mN/mm). The in vitro release of tilorone from the hydrogel was controlled with the crosslinking density/concentration of the hydrogel; the 10% w/v PVA-CHO/CHIT-SH hydrogel had the slowest releasing (21.7 h−1/2) rate, while the 2% w/v PVA-CHO/CHIT-SH hydrogel had the fastest releasing rate (34.6 h−1/2). Due to the characteristics of these hydrogels, their future uses include tissue regeneration scaffolds, wound dressings for skin injuries, and injectable or in situ forming drug delivery systems. Eventually, we hope that the developed hydrogel will be useful in the local treatment of muscle atrophy, such as laryngotracheal atrophy.

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Tarvirdipour, Shabnam, Xinan Huang, Voichita Mihali, Cora-Ann Schoenenberger, and Cornelia G. Palivan. "Peptide-Based Nanoassemblies in Gene Therapy and Diagnosis: Paving the Way for Clinical Application." Molecules 25, no. 15 (July 31, 2020): 3482. http://dx.doi.org/10.3390/molecules25153482.

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Nanotechnology approaches play an important role in developing novel and efficient carriers for biomedical applications. Peptides are particularly appealing to generate such nanocarriers because they can be rationally designed to serve as building blocks for self-assembling nanoscale structures with great potential as therapeutic or diagnostic delivery vehicles. In this review, we describe peptide-based nanoassemblies and highlight features that make them particularly attractive for the delivery of nucleic acids to host cells or improve the specificity and sensitivity of probes in diagnostic imaging. We outline the current state in the design of peptides and peptide-conjugates and the paradigms of their self-assembly into well-defined nanostructures, as well as the co-assembly of nucleic acids to form less structured nanoparticles. Various recent examples of engineered peptides and peptide-conjugates promoting self-assembly and providing the structures with wanted functionalities are presented. The advantages of peptides are not only their biocompatibility and biodegradability, but the possibility of sheer limitless combinations and modifications of amino acid residues to induce the assembly of modular, multiplexed delivery systems. Moreover, functions that nature encoded in peptides, such as their ability to target molecular recognition sites, can be emulated repeatedly in nanoassemblies. Finally, we present recent examples where self-assembled peptide-based assemblies with “smart” activity are used in vivo. Gene delivery and diagnostic imaging in mouse tumor models exemplify the great potential of peptide nanoassemblies for future clinical applications.

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Zahedi, Farhad, Akram Abouie Mehrizi, Soroush Sardari, and Iran Alemzadeh. "Design and development of a self-assembling protein nanoparticle displaying PfHAP2 antigenic determinants recognized by natural acquired antibodies." PLOS ONE 17, no. 9 (September 12, 2022): e0274275. http://dx.doi.org/10.1371/journal.pone.0274275.

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Backgrounds In order to move towards the elimination and eradication of malaria in the world, the development of vaccines is inevitable. Many modern vaccines are based on recombinant technology; however, they may not provide a fully protective, long-lasting immune response. One of the strategies to improve recombinant vaccines is designing the nanovaccines such as self-assembling protein nanoparticles (SAPNs). Hence, the presentation of epitopes in a repeat array and correct conformation should be considered. P. falciparum generative cell-specific 1 (PfGCS1) is a main transmission-blocking vaccine candidate with two highly conserved fragments, HAP2-GCS1 and cd loop, inducing partial malaria transmission inhibitory antibodies. Therefore, to design an effective malaria vaccine, we used cd loop and HAP2-GCS1 fragments at the amino and carboxy terminuses of the SAPN-forming amino acid sequence, respectively. Methodology/Principal findings The SAPN monomer (PfGCS1-SAPN) sequence was designed, and the three-dimensional (3D) structure was predicted. The result of this prediction ensured the presence of antigens on the SAPN surface. Then the accuracy of the predicted 3D structure and its stability were confirmed by 100 ns molecular dynamics (MD) simulation. The designed SAPN substructure sequence was synthesized, cloned, and expressed in Escherichia coli. With a gradual decrease in urea concentration in dialysis solutions, the purified proteins progressed to the final desired structure of the SAPN, which then was confirmed by Dynamic Light Scattering (DLS) and Field Emission Scanning Electron Microscopy (FESEM) tests. According to the Enzyme-Linked Immunosorbent Assay (ELISA), antigenic determinants were presented on the SAPN surface and interacted with antibodies in the serum of malaria patients. Conclusions/Significance Our results show that the SAPN formed by PfGCS1-SAPN has produced the correct shape and size, and the antigenic determinants are presented on the surface of the SAPN, which indicates that the designed SAPN has great potential to be used in the future as a malaria vaccine.

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Southern, Emily J., Valentin Besnard, Bastien Lahaye, Andy M. Tyrrell, and Shuhei Miyashita. "Catalytic self-folding of 2D structures through cascading magnet reactions." Royal Society Open Science 6, no. 7 (July 2019): 182128. http://dx.doi.org/10.1098/rsos.182128.

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While thousands of proteins involved in development of the human body are capable of self-assembling in a distributed manner from merely 20 types of amino acid, macroscopic products that can be assembled spontaneously from ‘alive’ components remains an aspiration in engineering. To attain such a mechanism, a major challenge lies in understanding which attributes from the bio-molecular realm must be leveraged at the macro-scale. Inspired by protein folding, we present a centimetre-size 1D tile chain whose self-folding processes are directed by structure-embedded magnetic interactions, which can theoretically self-assemble into convex 2D structures of any size or shape without the aid of a global ‘controller’. Each tile holds two magnets contained in paths designed to control their interactions. Once initiated by a magnetic unit (termed Catalyst), the chain self-reconfigures by consuming magnetic potential energy stored between magnet pairs, until the final 2D structure is reached at an energetic minimum. Both simulation and experimental results are presented to illustrate the method’s efficacy on chains of arbitrary length. Results demonstrate the promise of a physically implemented, bottom-up, and scalable self-assembly method for novel 2D structure manufacturing, bridging the bio-molecular and mechanical realms.

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Protopapa, Elisabeth, Lovisa Ringstad, Amalia Aggeli, and Andrew Nelson. "Interaction of self-assembling β-sheet peptides with phospholipid monolayers: The effect of serine, threonine, glutamine and asparagine amino acid side chains." Electrochimica Acta 55, no. 9 (March 2010): 3368–75. http://dx.doi.org/10.1016/j.electacta.2010.01.023.

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