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Cited by 3,923Collagen: Extraction and CharacterizationConnective tissue disorders researchSilk-based biomaterials and applications

Collagen Structure and Stability

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Shoulders, Matthew D., Raines, Ronald T.·2009·Annual Review of Biochemistry
DOI 10.1146/annurev.biochem.77.032207.120833PMC PMC2846778
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Abstract

Collagen is the most abundant protein in animals. This fibrous, structural protein comprises a right-handed bundle of three parallel, left-handed polyproline II-type helices. Much progress has been made in elucidating the structure of collagen triple helices and the physicochemical basis for their stability. New evidence demonstrates that stereoelectronic effects and preorganization play a key role in that stability. The fibrillar structure of type I collagen-the prototypical collagen fibril-has been revealed in detail. Artificial collagen fibrils that display some properties of natural collagen fibrils are now accessible using chemical synthesis and self-assembly. A rapidly emerging understanding of the mechanical and structural properties of native collagen fibrils will guide further development of artificial collagenous materials for biomedicine and nanotechnology.

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  • Collagen I presents a consistent and controllable material composition while showing biochemical and biophysical characteristics of tissue microenvironment, including cell adhesion sites.

    “It presents a consistent and controllable material composition while showing biochemical and biophysical characteristics of tissue microenvironment, including cell adhesion sites[60,61].”

    From Efficient Generation of Skin Organoids from Pluripotent Cells via Defined Extracellular Matrix Cues and Morphogen Gradients in a Spindle‐Shaped Microfluidic Device (2024) · cites this paper as [61]

    The Introduction identifies collagen as a major extracellular-matrix component, and the Biological and Biomedical Applications section describes collagen domains that interact with biomolecules and collagen-related peptides that bind cells. However, the Collagenous Biomaterials section says isolated bovine collagen suffers from heterogeneity; it does not establish that collagen I has a consistent, controllable material composition. The paper also says synthetic collagen mimics still lack many properties of natural fibrils. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Sorted by citations

Authors
Shoulders, M. D., & Raines, R. T.
Affiliations
University of Wisconsin–Madison (US)
ORCID
Venue
Annual Review of Biochemistry
Publisher
Annual Reviews
Published
2009-06-01
Volume
78
Issue
1
Pages
929-958
ISSN
  • 0066-4154 (ISSN-L)
  • 1545-4509
DOI
10.1146/annurev.biochem.77.032207.120833
PMC
PMC2846778
OpenAlex
W2161162374
Cited by
3,923
References
1
Citations by year
2026: 351 · 2025: 357 · 2024: 344 · 2023: 346 · 2022: 370 · 2021: 342 · 2020: 290 · 2019: 304 · 2018: 219 · 2017: 210 · 2016: 163 · 2015: 147 · 2014: 128 · 2013: 111 · 2012: 88
FWCI
3.72
Type
journal article
Language
en
Open access
Locations
  • Annual Review of Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute of Arthritis and Musculoskeletal and Skin Diseases (R56AR044276, AR044276, R01AR044276)
Topics
  • Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
  • Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
Keywords
collagen, collagen triple helix, polyproline II helix, collagen stability, stereoelectronic effects, preorganization, type I collagen fibrils, self-assembly, collagen mechanical properties
MeSH terms
Animals, Collagen, Humans, Models, Molecular, Protein Structure, Secondary, Protein Multimerization, Protein Stability

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