Fibrous long spacing type collagen fibrils have a hierarchical internal structure.
Nanodissection of single fibrous long spacing (FLS) type collagen fibrils by atomic force microscopy (AFM) reveals hierarchical internal structure: Fibrillar subcomponents with diameters of approximately 10 to 20 nm were observed to be running parallel to the long axis of the fibril in which they are found. The fibrillar subcomponent displayed protrusions with characteristic approximately 270 nm periodicity, such that protrusions on neighboring subfibrils were aligned in register. Hence, the banding pattern of mature FLS-type collagen fibrils arises from the in-register alignment of these fibrillar subcomponents. This hierarchical organization observed in FLS-type collagen fibrils is different from that previously reported for native-type collagen fibrils, displaying no supercoiling at the level of organization observed.
Wen
Chuck K
CK
Department of Chemistry, University of Toronto, Toronto, Ontario, Canada.
Goh
M Cynthia
MC
D000818:Animals; D002417:Cattle; D003094:Collagen / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D036103:Nanotechnology / Q000379:methods; D011487:Protein Conformation; D012867:Skin / Q000737:chemistry
D003094:Collagen