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Cited by 311

The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.

Self-assembly of synthetic collagen triple helices

Kotch, Frank W., Raines, Ronald T.·2006·Proceedings of the National Academy of Sciences

Abstract

Collagen is the most abundant protein in animals and the major component of connective tissues. Although collagen isolated from natural sources has long served as the basis for some biomaterials, natural collagen is difficult to modify and can engender pathogenic and immunological side effects. Collagen comprises a helix of three strands. Triple helices derived from synthetic peptides are much shorter (<10 nm) than natural collagen (≈300 nm), limiting their utility. Here, we describe the synthesis of short collagen fragments in which the three strands are held in a staggered array by disulfide bonds. Data from CD spectroscopy, dynamic light scattering, analytical ultracentrifugation, atomic force microscopy, and transmission electron microscopy indicate that these “sticky-ended” fragments self-assemble via intermolecular triple-helix formation. The resulting fibrils resemble natural collagen, and some are longer (>400 nm) than any known collagen. We anticipate that our self-assembly strategy can provide synthetic collagen-mimetic materials for a variety of applications.

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Metadata

Authors
Kotch, F. W., & Raines, R. T.
Venue
Proceedings of the National Academy of Sciences
Published
2006-02-17
Volume
103
Issue
9
Pages
3028-3033
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1969946367
Cited by
311
References
42
FWCI
12.74
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Self-assembly of synthetic collagen triple helices. https://app.cochat.ai/papers/10.1073/pnas.0508783103
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Kotch, F. W., & Raines, R. T. (2006). Self-assembly of synthetic collagen triple helices. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0508783103

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