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Cited by 1,041Collagen: Extraction and CharacterizationWound Healing and TreatmentsElectrospun Nanofibers in Biomedical Applications

Collagen-based biomaterials for wound healing

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Chattopadhyay, Sayani, Raines, Ronald T.·2014·Biopolymers
DOI 10.1002/bip.22486PMC PMC4203321
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Abstract

With its wide distribution in soft and hard connective tissues, collagen is the most abundant of animal proteins. In vitro, natural collagen can be formed into highly organized, three‐dimensional scaffolds that are intrinsically biocompatible, biodegradable, nontoxic upon exogenous application, and endowed with high tensile strength. These attributes make collagen the material of choice for wound healing and tissue engineering applications. In this article, we review the structure and molecular interactions of collagen in vivo; the recent use of natural collagen in sponges, injectables, films and membranes, dressings, and skin grafts; and the on‐going development of synthetic collagen mimetic peptides as pylons to anchor cytoactive agents in wound beds. © 2014 Wiley Periodicals, Inc. Biopolymers 101: 821–833, 2014.

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  • Collagen mimetic peptides and recombinant human collagen offer reduced immunogenicity and antigenicity compared to animal-derived collagen.

    “Collagen mimetic peptides (CMPs) and recombinant human collagen (rhCollagen) offer the benefit of reduced immunogenicity and antigenicity compared to animal-derived collagen, making them less likely to provoke immune responses [37,38,39].”

    From Biomaterials in Postoperative Adhesion Barriers and Uterine Tissue Engineering (2025) · cites this paper as [39]

    The “Collagen In Vivo” section says animal-derived collagen can be complicated by allergic reactions and presents heterologously produced collagen as an alternative. It does not establish that recombinant human collagen or collagen mimetic peptides have lower immunogenicity or antigenicity than animal-derived collagen; the “Collagen Mimetic Peptides” section discusses their other properties instead. Page numbers were not available in our copy. (LLM, conf=0.78)

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Authors
Chattopadhyay, S., & Raines, R. T.
Affiliations
University of Wisconsin–Madison (US)
Corresponding author
Raines, Ronald T.
ORCID
Raines, Ronald T.
Venue
Biopolymers
Publisher
Wiley
Published
2014-05-27
Volume
101
Issue
8
Pages
821-833
ISSN
  • 0006-3525 (ISSN-L)
  • 1097-0282
DOI
10.1002/bip.22486
PMC
PMC4203321
OpenAlex
W2095998281
Cited by
1,041
References
1
Citations by year
2026: 81 · 2025: 108 · 2024: 117 · 2023: 120 · 2022: 115 · 2021: 113 · 2020: 113 · 2019: 96 · 2018: 72 · 2017: 48 · 2016: 33 · 2015: 17 · 2014: 7
FWCI
2.38
Type
journal article
Language
en
Open access
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations
  • Biopolymers (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
NIH (R01 AR044276 and RC2 AR058971)
Topics
  • Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
  • Health Sciences › Medicine › Rehabilitation › Wound Healing and Treatments
  • Physical Sciences › Materials Science › Biomaterials › Electrospun Nanofibers in Biomedical Applications
Keywords
collagen, wound healing, tissue engineering, collagen scaffolds, collagen structure, biodegradable biomaterials, wound dressings, skin grafts, collagen sponge, collagen mimetic peptides
MeSH terms
Animals, Bandages, Biocompatible Materials, Collagen, Cross-Linking Reagents, Humans, Peptides, Skin, Wound Healing

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