Decoding collagen's thermally induced unfolding and refolding pathways.

ABSTRACT: Collagen has been evolutionarily selected as the preferred building block of extracellular structures. Despite inherent thermodynamic instability of individual proteins at body temperature, collagen manages to assemble into higher-order structures that provide mechanical support to tissues. Sequence features that enhance collagen stability have been deduced primarily from studies of collagen-mimetic peptides, as collagen's large size has precluded high-resolution studies of its structure. Thus, methods are needed to analyze the structure and mechanics of full-length collagen proteins. In this study, we used AFM imaging to investigate the thermal response of collagen type IV, a key component of basement membranes. We observed a time-dependent loss of folded structures upon exposure to body

SUBMITTER: Al-Shaer A 

PROVIDER: S-EPMC12107170 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature