ArticleBiomaterials2016
The synthesis and coupling of photoreactive collagen-based peptides to restore integrin reactivity to an inert substrate, chemically-crosslinked collagen.
Article in Biomaterials, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 48 citations in OpenAlex.
- Triple-helical ligands for collagen-binding proteins improve cartilage extracellular matrix production in nasal chondrocytes.Materials today. Bio · 2026Article
- An Asymmetric Dura-Inspired Collagen Hydrogel Patch with Integrated Dense-Porous Architecture Enabled by Dual-Channel Freeze Casting.Advanced healthcare materials · 2026Article
- Impact of Stiffness and Cell-Binding Motif Availability on the Cell-Specific Response to Collagen-Based Macromolecular Materials.Biomacromolecules · 2026Article
- Triple Helical-Peptides: Collagen-Mimicking Tools for Tissue Engineering.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Recombinant human collagen type III microgel: an advanced injectable dermal filler for rejuvenating aging skin.Regenerative biomaterials · 2025Article
- A portable colorimetric immunosensor for highly sensitive point-of-care testing of leather artifacts.Mikrochimica acta · 2024Article
- Versatile Self-Assembly of Triblock Peptides into Stable Collagen Mimetic Heterotrimers.International journal of molecular sciences · 2024Article
- Controllable self-assembly of tyrosine-rich triblock peptides into robust collagen mimetic bioscaffolds for aging skin rejuvenation.Regenerative biomaterials · 2024Article
- Peptide-based direct electrochemical detection of receptor binding domains of SARS-CoV-2 spike protein in pristine samples.Sensors and actuators. B, Chemical · 2023Article
- The effects of inhibition and siRNA knockdown of collagen-binding integrins on human umbilical vein endothelial cell migration and tube formation.Scientific reports · 2022Article
- Possible Treatment of Myocardial Infarct Based on Tissue Engineering Using a Cellularized Solid Collagen Scaffold Functionalized with Arg-Glyc-Asp (RGD) Peptide.International journal of molecular sciences · 2021Review
- Bioactive potential of natural biomaterials: identification, retention and assessment of biological properties.Signal transduction and targeted therapy · 2021Review
- Modulating hESC-derived cardiomyocyte and endothelial cell function with triple-helical peptides for heart tissue engineering.Biomaterials · 2021Article
- Article
- Collagen scaffolds functionalized with triple-helical peptides support 3D HUVEC culture.Regenerative biomaterials · 2020Article
- Tunable bioactivity and mechanics of collagen-based tissue engineering constructs: A comparison of EDC-NHS, genipin and TG2 crosslinkers.Biomaterials · 2020Article
- Natural Biomaterials for Cardiac Tissue Engineering: A Highly Biocompatible Solution.Frontiers in cardiovascular medicine · 2020Review
- Coupling of a specific photoreactive triple-helical peptide to crosslinked collagen films restores binding and activation of DDR2 and VWF.Biomaterials · 2018Article
- Achieving Controlled Biomolecule-Biomaterial Conjugation.Chemical reviews · 2018Review
- Selecting the correct cellular model for assessing of the biological response of collagen-based biomaterials.Acta biomaterialia · 2018Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Collagen is frequently advocated as a scaffold for use in regenerative medicine. Increasing the mechanical stability of a collagen scaffold is widely achieved by cross-linking using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and N-hydroxysuccinimide (NHS). However, this treatment consumes the carboxylate-containing amino acid sidechains that are crucial for recognition by the cell-surface integrins, abolishing cell adhesion. Here, we restore cell reactivity to a cross-linked type I collagen film by covalently linking synthetic triple-helical peptides (THPs), mimicking the structure of collagen. These THPs are ligands containing an active cell-recognition motif, GFOGER, a high-affinity binding site for the collagen-binding integrins. We end-stapled peptide strands containing GFOGER by coupling a short diglutamate-containing peptide to their N-terminus, improving the thermal stability of the resulting THP. A photoreactive Diazirine group was grafted onto the end-stapled THP to allow covalent linkage to the collagen film upon UV activation. Such GFOGER-derivatized collagen films showed restored affinity for the ligand-binding I domain of integrin α2β1, and increased integrin-dependent cell attachment and spreading of HT1080 and Rugli cell lines, expressing integrins α2β1 and α1β1, respectively. The method we describe has wide application, beyond collagen films or scaffolds, since the photoreactive diazirine will react with many organic carbon skeletons.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.