Real-time single-molecule observation of incipient collagen fibrillogenesis and remodeling.

ABSTRACT: The hierarchic assembly of fibrillar collagen into an extensive and ordered supramolecular protein fibril is critical for extracellular matrix function and tissue mechanics. Despite decades of study, we still know very little about the complex process of fibrillogenesis, particularly at the earliest stages where observation of rapidly forming, nanoscale intermediates challenges the spatial and temporal resolution of most existing microscopy methods. Using video rate scanning atomic force microscopy (VRS-AFM), we can observe details of the first few minutes of collagen fibril formation and growth on a mica surface in solution. A defining feature of fibrillar collagens is a 67-nm periodic banding along the fibril driven by the organized assembly of individual monomers over multiple length sc

SUBMITTER: Roth J 

PROVIDER: S-EPMC11331128 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature