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Updated: Jul 5, 2026
Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
Published on: January 31, 2014
Advances in collagen cross-link analysis
David R Eyre1, Mary Ann Weis, Jiann-Jiu Wu
1Orthopaedic Research Labs, Department of Orthopaedics & Sports Medicine, University of Washington, 1959 NE Pacific Street, Seattle, WA 98195-6500, USA. deyre@u.washington.edu
Abstract:
The combined application of ion-trap mass spectrometry and peptide-specific antibodies for the isolation and structural analysis of collagen cross-linking domains is illustrated with examples of results from various types of collagen with the emphasis on bone and cartilage. We highlight the potential of such methods to advance knowledge on the importance of post-translational modifications (e.g., degrees of lysine hydroxylation and glycosylation) and preferred intermolecular binding partners for telopeptide and helical cross-linking domains in regulating cross-link type and placement.
