ArticleBiophysical journal2020
Modeling Fibrillogenesis of Collagen-Mimetic Molecules.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Free energy of collagen-mimetic peptide dimerization and implications for fibrillization.Biophysical journal · 2026Article
- Supramolecular Assembly of Collagen-Mimetic Peptide D-Periodic Fibrils and Nanoassemblies.Biomacromolecules · 2026Article
- Recombinant collagen in regenerative medicine: Expression strategies, structural design, and translational applications.Materials today. Bio · 2025Review
- Diffusion model assisted designing self-assembling collagen mimetic peptides as biocompatible materials.Briefings in bioinformatics · 2024Article
- In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures.ACS nano · 2024Article
- Elucidating the role of water in collagen self-assembly by isotopically modulating collagen hydration.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Theoretical and Data-Driven Approaches for Biomolecular Condensates.Chemical reviews · 2023Review
- Engineered Peptides Enable Biomimetic Route for Collagen Intrafibrillar Mineralization.International journal of molecular sciences · 2023Article
- Design of synthetic collagens that assemble into supramolecular banded fibers as a functional biomaterial testbed.Nature communications · 2022Article
- Collagen fibril assembly: New approaches to unanswered questions.Matrix biology plus · 2021Article
- Effects of size, cooperativity, and competitive binding on protein positioning on DNA.Biophysical journal · 2021Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One of the most robust examples of self-assembly in living organisms is the formation of collagen architectures. Collagen type I molecules are a crucial component of the extracellular matrix, where they self-assemble into fibrils of well-defined axial striped patterns. This striped fibrillar pattern is preserved across the animal kingdom and is important for the determination of cell phenotype, cell adhesion, and tissue regulation and signaling. The understanding of the physical processes that determine such a robust morphology of self-assembled collagen fibrils is currently almost completely missing. Here, we develop a minimal coarse-grained computational model to identify the physical principles of the assembly of collagen-mimetic molecules. We find that screened electrostatic interactions can drive the formation of collagen-like filaments of well-defined striped morphologies. The fibril axial pattern is determined solely by the distribution of charges on the molecule and is robust to the changes in protein concentration, monomer rigidity, and environmental conditions. We show that the striped fibrillar pattern cannot be easily predicted from the interactions between two monomers but is an emergent result of multibody interactions. Our results can help address collagen remodeling in diseases and aging and guide the design of collagen scaffolds for biotechnological applications.
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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.