Substrate-dependent morphology of supramolecular assemblies: fibrillin and type-VI collagen microfibrils.

ABSTRACT: Substrate hydrophobicity/hydrophilicity has previously been shown to affect the morphology and biological function of isolated proteins. We have employed atomic force microscopy to investigate substrate dependent morphologies of two biochemically distinct native supramolecular assemblies: fibrillin and type-VI collagen microfibrils. These morphologically heterogeneous microfibrillar systems are found in many vertebrate tissues where they perform structural and cell-signaling roles. Fibrillin microfibrils adsorbed to a hydrophilic mica substrate adopted a diffuse morphology. Fibrillin microfibrils adsorbed to mica coated with poly-L-lysine or to borosilicate glass substrates had a more compact morphology and a directional asymmetry to the bead, which was not present on mica alone. Intermedi

SUBMITTER: Sherratt MJ 

PROVIDER: S-EPMC1304186 | biostudies-literature | 2004 May

REPOSITORIES: biostudies-literature