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Updated: Sep 28, 2026

Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers
Published on: July 25, 2012
Localized unfolding of collagen explains collagenase cleavage near imino-poor sites
1Harvard-MIT Division of Health Sciences and Technology, Cambridge, MA 02139, USA. cmstultz@partners.org
Abstract:
Collagenases cleave all three chains of type III collagen at specific sites characterized by a Gly-Leu or a Gly-Ile bond that is upstream from an imino acid-poor region. Molecular dynamics trajectories were used to calculate the free energy of unfolding for collagen-like model peptides. The free energy profiles suggest that such imino-poor regions can adopt a low-energy, partially unfolded state where one of the peptide chains forms a solvent-exposed loop. The results are consistent with a model for collagenase cleavage where partial unfolding of imino-poor regions enables collagenases to gain access to their cleavage sites.
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