Auswahl der wissenschaftlichen Literatur zum Thema „Biomimetické peptidy“

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.

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.

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).

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.

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.

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.

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.

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.

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.

Práca sa zaoberá in silico dizajnom a validáciou peptidov založených na konotoxíne - MrIA, izolovaného z morských slimákov druhu Conus marmoreus a možnosti využitia týchto peptidov v liečbe neuroblastómu pomocou cielenia norepinefrínového transportéru. Päť peptidov založených na tomto konotoxíne bolo simulovaných pomocou simulácii molekulárnej dynamiky, ich trajektórie boli analyzované pre zistenie vlastností týchto peptidov. Dva homologické modely ľudského norepinefrínového transportéru boli vytvorené pre analýzu väzobných vlastností peptidov založených na konotoxíne ku norepinefrínovému transportéru. Peptidy boli následne syntetizované a použité na pokrytie apoferitínových nanočastíc s elipticínom uväzneným vnútri apoferitínu. Vytvorené peptidy a nanočastice boli ďalej skúmané pre objasnenie ich fyzikálo-chemických vlastností. Interakcie a cytotoxicita boli skúmané aplokáciou nanočastíc na bunky neuroblastómu a epitelu. Z in silico a in vitro analýz vyšiel YKL-6 peptid ako najlepší kandidát na ďalší výskum.

In this Master’s Thesis Research the results can be summarized from two major tasks: (1) In our first task, we utilized our two protein system (BAG-1 and HSP 70) as part of beta testing of a computational software 1 that can take three dimensional x-ray crystallography information about protein complexes and predict the strength of atom –atom interactions between amino-acid residues Open Contact predicts binding hotspots that can be used to identify short amino acid chains or peptides that mimic that particular binding segment of the larger protein. These peptides are called pepidyl-biomimetics. The peptide can potentially act as an antagonist drug by binding to the hotspot on protein A before protein B of the A-B complex can form. Two potential peptide candidates were identified. In particular, a helical peptide was discovered that demonstrated a variety of different types of atom-atom interactions. (2) Our second task is to experimentally test the helical peptide for its ability to block the binding that occurs between the 70-kilodalton Heat Shock Protein (HSP-70) and the Bcl-2 Associated Athanogene (BAG-1) Protein. As reviewed here, the binding between HSP-70 and BAG-1 elicits a cascade of cellular events that maintain high cancer growth rates and a greatly increased resistance to chemotherapy. In addition, BAG-1 has been implicated in a number of onco-signal pathways, as reviewed here, and its inhibition alone is believed to act as an agent against cancer cell growth

Thesis (M. Phil.)--Hong Kong University of Science and Technology, 2003.
Includes bibliographical references (leaves 103-107). Also available in electronic version. Access restricted to campus users.

Le passage des médicaments a travers la membrane cellulaire représente souvent une limitation majeur dans un grand nombre de thérapies (anti-cancéreuse, anti-virale par exemple). Des peptides vecteurs connus comme les CPPs (cell penetrating peptides) ont été utilises avec succès pour introduire a l’intérieur des cellules diverses molécules (protéines, peptides, siRNA, quantum dots) et présentent un fort potentiel dans l'adressage de médicaments. Parmi les différents CPPs décrits dans la littérature la plupart sont des peptides basiques ou amphiphiles.Nous nous sommes intéressés a l'utilisation d’oligomères non charges construits a partir de motifs contraints mimes de dipeptides comme vecteurs de pénétration cellulaire. L'internalisation cellulaire et leur localisation ont été établies a l'aide de dérivés fluorescents par microscopie confocale. L' étude de pénétration cellulaire par mesure de fluorescence a montre que des oligomères de (3S)-amino-5-carbonylmethyl-2,3-dihydro-1,5-benzothiazepine-4(5H)-one] (DBT) sont aussi puissants que les oligomères d'arginine (oligoArg), vecteurs de référence. Par microscopie confocale nous avons montré que ces composés sont internalisés dans les lysosomes. L’efficacité d'internalisation de nos composés a été confirmé par une méthode de quantification par spectrométrie de masse MALDI-TOF développée dans notre groupe. Cette méthode repose sur l'utilisation conjointe d'un marqueur UV-absorbant dérivé de l'acide alfa-cyano-4-hydoxycinnamique (HCCA) et d'une matrice MALDI adaptée. Un effet important de discrimination spectrale est obtenu, permettant une amplification du signal de la molécule d' intérêt dans un mélange complexe. Ainsi les faibles concentrations internalisées peuvent être détectées. Grâce a cette technique et l'utilisation d'un étalon deutéré, nous avons calculé la concentration intracellulaire de deux CPP de référence l'octa-arginine et la pénétratine. Nous avons aussi étudier l’internalisation de petits oligomères construits a partir d'acide 2-aminomethyl-phenyl-acetique (AMPA). Par microscopie confocal nous avons constaté que ces petits oligomères sont internalisés par voie endo-lysosomale.L’efficacité de la pénétration cellulaire de ces petits oligomères aromatiques (oligoAMPA et oligoDBT) offre une nouvelle classe de vecteurs qui ont la particularité d’être non-cationiques et hydrophobes. De tels composés pourraient être utilisés pour la délivrance de médicaments dans le traitement des maladies comme le cancer, les maladies lysosomales ou la maladie d'Alzheimer. Afin de montrer que cette nouvelle classe de vecteurs est capable d'internaliser des composés biologiquement actifs, nous les avons associés a un inhibiteur puissant de la Cathepsine D (CD) la pepstatine. CD est une endopeptidase lysosomale qui dans des conditions normales est localisée dans les endosomes et les lysosomes. Pour certains cancers, la CD est surexprimée et secrétée a l’extérieur de la cellule. La CD est probablement impliquée dans la prolifération des cellules cancéreuses par l'activation de certains facteurs de croissances dans les endosomes. La pepstatine est une inhibiteur puissant de la CD. Cependant son efficacité thérapeutique potentielle est limitée par une faible capacité de pénétration des membranes cellulaires et une faible solubilité nécessitant de fortes doses pour l'inactivation de la CD in vitro et in vivo. Afin d’améliorer son efficacité et sa biodisponibilité, des conjugues de la pepstatine avec nos vecteurs de pénétration cellulaire, oligo (AMPA)4 et (DBT)4, et une partie solubilisante ont été développés. Certains de ces bioconjugués ont montre une toxicité élevée (IC50 = 2.10-6) in vitro sur différentes lignées cellulaires tumorales. Des tests in vivo sur des souris sont prévus pour le futur
As a part of a program for foldamer design two ¦Â-turn mimetics (3S)-amino-5-(carboxylmethyl)-2,3-dihydro-1,5-benzothiazepin-4(5H)-one or DBT and 2-aminomethyl-phenyl-acetic acid or AMPA were selected as frameworks from a molecular modeling study for their suitability to adopt helical structure. At first we developed a highly efficient scale up synthesis of the DBT moiety protected by 9-fluorenylmetoxycarbonyl (Fmoc) group. By standard solid phase peptide synthesis (SPPS) we synthesized DBT oligomers of different lenghts and modifications were introduced at their N-terminus. Our first task was to perform structural analysis of the oligomers by NMR and X-Ray. Numerous NOE interactions in the DBT pentamer and hexamer molecules were detected by NMR 2D NOESY experiments. These data strongly suggest the organization of these DBT oligomers. Small crystals were obtained from the same molecules in DMSO but at the time being their size is not importan t enough for X-Ray crystallography studies. In a parallel study we hypothesized that short oligomers constructed by DBT or AMPA frameworks could translocate the cellular membrane and could be used as new cell penetrating non-peptides - CPNP. Even though these compounds are not charged as most cell penetrating peptides (CPP)5 or CPNP, we considered that by virtue of their aromaticity, hydrophobicity and their well-organized structure they could have a non-specific interaction with the lipid bilayer and thus be internalized into the cell. Short oligomers were synthesized on Rink amide (RA) resin following SPPS methodology and labelled at their N-terminus with fluorescein isothiocyanate (FITC). At first the cellular uptake of the (DBT)2-4 oligomers in MDA-MB-231 breast cancer cells was analyzed by fluorescence emission measurement and compared to the potent and well-studied CPP octa-arginine (Arg)8 as a positive control and carboxyfluorescein as a negative control. The highest intracellular fluorescence intensity was found for (DBT)4 with a drastic decrease (>4-times) for (DBT)3 and (DBT)2 oligomers. Thus, the cellular uptake appeared length-dependent with an increase of the internalization with the oligomer size. Moreover, the amount of (DBT)4 that was internalized was more significant than that of (Arg)8 despite the fact that it is uncharged. By confocal microscopy we determined that (DBT)4 is mainly localized in the endosomes after 3 hours of incubation and in the lysosomes after 16 hours of incubation. Altogether, these data indicate the ability of these oligomers to target the endolysosomal pathway. Although most of the initial drug delivery studies aimed to avoid lysosomal addressing to prevent subsequent drug degradation, more recent studies demonstrated the relevant clinical utility to target this compartment for drug delivery in the treatment of lysosomal storage diseases, Alzheimer¡¯s disease, and cancer.While analyzing the internalization efficiency of our CPNP we decided to straightforward evaluate their concentration inside the cells. We studied our compounds internalization by total fluorescence emission measurement and by confocal microscopy but none of these techniques gave us the possibility to determine the exact amount of compound internalized per cell. A study reported by Burlina et al. brought a great improvement in proposing a highly reproducible quantification method based on MALDI-TOF MS to measure the concentration of the internalized peptides. However, after cell lysis, this method requires the capture of the biotin-labelled CPP by streptavidin coated magnetic beads. This step is particularly critical for the accuracy of the quantification. This is the reason why we decided to develop a new general methodology based on MALDI-TOF mass spectrometry (MS) which does not require any purification or separation steps. We studied the internalization of CPP/CPNP compou nds by using an UV light-absorbing tag alpha-cyano-4-hydroxycinnamic acid (HCCA) and preparing the samples in a neutral matrix such as alpha-cyano-4-hydroxycinnamic methyl ester (HCCE). This combination (HCCA tag and HCCE matrix) enabled us to discriminate MS signals induced by peptides of interest that were present in low concentration from those of unlabelled more abundant peptides. By addition of a precise amount of deuterated-HCCA-tagged CPP/CPNP prior the MALDI TOF MS experiment, the internalized CPP/CPNP could be quantified on the basis of the ratio between the [M+H]+ peaks of the deuterated and nondeuterated HCCA-tagged CPP.Another direction for research was to synthesize bioconjugates between our newly discovered CPNP and some biologically active compounds that are unable to cross the cell membrane. We selected pepstatine which is a powerful transition state inhibitor of the Cathepsin D (CD). Pepstatine while a very potent inhibitor of the CD is unable to cross the cellular membrane. Moreover pepstatine activity in vitro or in vivo is hampered by its poor solubility in water. CD is a soluble lysosomal aspartic endopeptidase synthesized in rough endoplasmic reticulum as preprocathepsin D (pCD).12 Upon entering the acidic endosomal and lysosomal compartments proteolytic cleavages of the pCD result in the formation of the active enzymatic form of CD. Under normal physiological conditions pCD is sorted to the lysosomes and found intracellularly but in some pathological and physiological conditions like cancer pCD/CD escape the normal targeting mechanism and is secreted from the cell. Once secreted to the outside, pCD can be endocytosed via M6PR or yet unknown receptor by both cancer cells and fibroblasts. The endocytosed pCD undergoes maturation into the enzymatically active CD. An enzymatic activity of CD outside of the cell or inside the endosomes could be responsible for the activation of several growth factors and growth factor receptors. Several groups have proven that the tumour growth is not inhibited by the powerful CD inhibitor pepstatine. These results exclude the importance of the CD enzymatic activity outside of the cell but as already mentioned pepstatine is unable to penetrate into the cell thus CD activation of growth factors inside the endosomes or the lysosomes is still a possibility. Different CPNP-Pepstatine conjugates were synthesized and tested in vitro for their ability to inhibit MDA-MB-231 breast cancer cells growth. Some of these conjugates showed high cytotoxicity, probably via a Cathepsin D inhibition in the endosomes or the lysosomes. One o f the most potent tested compounds was JMV4463. This compound was obtained by the conjugation of pepstatine with a CPNP as delivery system (AMPA4) and with solubilizing moiety composed of polyethylene glycol and D-Arginine residue. The good in vitro results obtained with the vectorized pepstatine encouraged us to perform in vivo tests. We performed scale up synthesis of JMV4463 in order to obtain enough product for anti-cancer activity on mice in the near future

Thesis (Ph. D.)--Chemistry and Biochemistry, Georgia Institute of Technology, 2010.
Committee Chair: Bridgette Barry; Committee Member: David Collard; Committee Member: Ingeborg Schmidt-Krey; Committee Member: Jake Soper; Committee Member: Mira Josowicz. Part of the SMARTech Electronic Thesis and Dissertation Collection.

An ever-growing demand for food products with minimal chemical additives has generated a necessity for exploring new alternatives for food preservation. In this context, more recently, bacteriocins, the peptides having antimicrobial property, synthesized ribosomally by numerous bacteria have been attracting a lot of attention. They are known to possess the potential to restrict the growth of microorganisms causing food spoilage without causing any harm to the bacteria themselves owing to the presence of self-defensive proteins. In particular, the bacteriocins of lactic acid bacteria have been considered harmless and safe for consumption and are indicated to evade the development of unwanted bacteria. Use of bacteriocins as biopreservatives has been studied in various food industries, and they have been established to elevate the shelf life of minimally processed food items by exerting killing mechanism. They restrict the growth of undesirable bacteria by breaking the target cell membrane and finally resulting into pore formation. The current article provides an insight on bacteriocins of lactic acid bacteria, their biosynthesis, mechanism of action, and promising applications of these antimicrobial peptides in the food sector.

In this study, we utilize a novel microfluidic device to perform simultaneous electrical interrogation of an array of droplet interface bilayers (DIB) that feature asymmetric phospholipid leaflet compositions. While asymmetry is vital to many cellular functions, it is has received very little attention in membrane-based engineered material systems for sensing, energy conversion, or actuation. This gap is due to challenges in constructing and interrogating networks of asymmetric membranes, limiting our understanding of how lipid asymmetry affects membrane active peptides, and vice versa. Our system overcomes these difficulties by enabling asymmetric membrane formation between many pairs of lipid-coated droplets in oil. We demonstrate its use in probing the interactions between alamethicin, a membrane-active peptide that forms voltage-induced ion channels, and asymmetric DPhPC:DOPhPC membranes, a choice that creates an intrinsic intramembrane potential of |137 mV| due to differences in their respective dipole potentials. Our experiments show that adding alamethicin peptides to one side of the membrane causes this inherent membrane potential to decrease over time, and it alters the value of external voltage that must be applied to drive alamethicin insertion for ion channel formation. These effects take place over the course of 1 to 5 hours after membrane formation, and both results are consistent with translocation and mixing of lipids across the leaflets of the membrane.

It is well established that the pore size and distribution affect the rate of cell migration and the extent of extracellular matrix formation. The objective of this work was to develop a process for fabrication of biodegradable and shape-specific polymeric scaffolds with well-defined pore geometry, functionalized with covalently attached bioactive peptides, for applications in tissue regeneration. We have used the Fused Deposition Modeling (FDM) RP technology to fabricate degradable and functional scaffolds with well-defined pore geometry. Computer aided design (CAD) using SolidWorks was used to create models of the cubic orthogonal geometry. The models were used to create the machine codes necessary to build the scaffolds with FDM with wax as the build material. A novel biodegradable in-situ crosslinkable macromer, poly(lactide-co-glycolide fumarate) or PLGF, mixed with reactive functional peptides was infused in the scaffold and allowed to crosslink. The scaffold was then immersed in a hydrocarbon solvent to remove the wax, leaving just the PLGF behind as the support material dissolved. The pore morphology of the PLGF scaffold was imaged with micro-computed tomography and scanning electron microscopy. Cellular function in the PLFG scaffolds with well-defined pore geometry was studied with bone marrow stromal cells isolated from rats. Results demonstrate that the scaffolds support homogeneous formation of mineralized tissue.

Damaged tendons often do not heal completely and lack full functionality. Tissue engineering employing collagen based biomaterials is a viable option to repair damaged tendons. However, most existing constructs lack the desired mechanical strength needed to reconstruct such load bearing tissues. We have previously reported a novel methodology to synthesize highly ordered electrochemically aligned collagen (ELAC) threads that are mechanically stronger and more amenable to cell migration compared to randomly oriented collagen constructs. While the ELAC mimics the orientational anisotropy of tendon it can be further improved by the incorporation of small leucine rich proteoglycans like decorin. Decorin consists of a protein core that binds to collagen and a glycosaminoglycan (GAG) chain. The GAG chains of adjacent collagen fibrils associate with one another to form crosslinks and are suggested to enhance the mechanical properties of tendon by allowing fibrillar slippage. Based on the structure of natural decorin, we have previously synthesized a novel peptidoglycan (DS-SILY) containing a collagen binding peptide (SILY) and a dermatan sulfate (DS) GAG chain. DS-SILY mimics decorin both structurally and functionally. In this study, we investigated the effects of the incorporation of DS-SILY on the mechanical properties and structural organization of ELAC threads by monotonic mechanical testing, swelling ratio and differential scanning calorimetry.