ArticleBiomacromolecules2009
Supramolecular assembly of electrostatically stabilized, hydroxyproline-lacking collagen-mimetic peptides.
Article in Biomacromolecules, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 87 citations in OpenAlex.
- β-Turn Mimicking Crosslinking Provides Hyperstability and Fast Folding Kinetics for Short Collagen Triple Helices.Chembiochem : a European journal of chemical biology · 2025Article
- Designing collagens to shed light on the multi-scale structure-function mapping of matrix disorders.Matrix biology plus · 2024Review
- Controllable self-assembly of tyrosine-rich triblock peptides into robust collagen mimetic bioscaffolds for aging skin rejuvenation.Regenerative biomaterials · 2024Article
- Molecular Engineering of Rigid Hydrogels Co-assembled from Collagenous Helical Peptides Based on a Single Triplet Motif.ACS applied materials & interfaces · 2022Article
- Article
- Selective covalent capture of collagen triple helices with a minimal protecting group strategy.Chemical science · 2022Article
- Biomaterials via peptide assembly: Design, characterization, and application in tissue engineering.Acta biomaterialia · 2022Review
- Collagen- and hyaluronic acid-based hydrogels and their biomedical applications.Materials science & engineering. R, Reports : a review journal · 2021Article
- Formation of Microcages from a Collagen Mimetic Peptide via Metal-Ligand Interactions.Molecules (Basel, Switzerland) · 2021Article
- Combining simulations and experiments for the molecular engineering of multifunctional collagen mimetic peptide-based materials.Soft matter · 2021Article
- Photo-responsive azobenzene interactions promote hierarchical self-assembly of collagen triple-helical peptides to various higher-order structures.RSC advances · 2020Article
- Hierarchically structured hydrogels utilizing multifunctional assembling peptides for 3D cell culture.Biomaterials science · 2020Article
- Designing a bioactive scaffold from coassembled collagen-laminin short peptide hydrogels for controlling cell behaviour.RSC advances · 2019Article
- Crafting of functional biomaterials by directed molecular self-assembly of triple helical peptide building blocks.Interface focus · 2017Review
- ECM turnover-stimulated gene delivery through collagen-mimetic peptide-plasmid integration in collagen.Acta biomaterialia · 2017Article
- Thermoresponsive Elastin-b-Collagen-Like Peptide Bioconjugate Nanovesicles for Targeted Drug Delivery to Collagen-Containing Matrices.Biomacromolecules · 2017Article
- Metal-Promoted Assembly of Two Collagen Mimetic Peptides into a Biofunctional "Spiraled Horn" Scaffold.Materials (Basel, Switzerland) · 2016Article
- Evolution of hierarchical porous structures in supramolecular guest-host hydrogels.Soft matter · 2016Article
- Integration of growth factor gene delivery with collagen-triggered wound repair cascades using collagen-mimetic peptides.Bioengineering & translational medicine · 2016Article
- Rational design of fiber forming supramolecular structures.Experimental biology and medicine (Maywood, N.J.) · 2016Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The mechanical and biological functions of the native collagens remain an inspiration in materials design, but widespread application of de novo collagens has been limited in part by the need for hydroxylated proline in the formation of stable triple helical structures. To address this continued need and to expand the potential for recombinant expression of functional, hydroxyproline-lacking collagen-mimetic peptides, we have designed a hydrophilic, nonrepetitive, and thermally stable collagen-mimetic peptide via the incorporation of triple-helix-stabilizing charged triplets. The peptide sequence is also equipped with a type III-collagen-mimetic cystine knot at the C-terminus to facilitate covalent cross-linking of the triple helix via simple air oxidation. Circular dichroic spectroscopy (CD) studies of this collagen-mimetic peptide revealed a typical, thermally stable, collagen triple helix signature with a weak positive maximum at 225 nm and a triple helix melting temperature (T(m)) of 35 and 43 degrees C for the reduced and oxidized forms, respectively. The thermal behavior was confirmed via analysis by differential scanning calorimetry. Interestingly, this hydroxyproline-lacking, collagen-mimetic peptide also assembles into nanorods and microfibrillar structures as observed via transmission electron microscopy. The identification and demonstrated useful collagen-mimetic properties of this peptide suggests important opportunities in the recombinant design of new collagen-based biomaterials.
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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.