Assembly of collagen into microribbons: effects of pH and electrolytes

F Jiang, JKH Hoerber, J Howard, DJ Müller

Research output: Contribution to journalArticle (Academic Journal)

175 Citations (Scopus)

Abstract

Collagen represents the major structural protein of the extracellular matrix. Elucidating the mechanism of its assembly is important for understanding many cell biological and medical processes as well as for tissue engineering and biotechnological approaches. In this work, conditions for the self-assembly of collagen type I molecules on a supporting surface were characterized. By applying hydrodynamic flow, collagen assembled into ultrathin (3 nm) highly anisotropic ribbon-like structures coating the entire support. We call these novel collagen structures microribbons. High-resolution atomic force microscopy topographs show that subunits of these microribbons are built by fibrillar structures. The smallest units of these fibrillar structures have cross-sections of 3 × 5 nm, consistent with current models of collagen microfibril formation. By varying the pH and electrolyte of the buffer solution during the self-assembly process, the microfibril density and contacts formed within this network could be controlled. Under certain electrolyte compositions the microribbons and microfibers display the characteristic D-periodicity of 65 nm observed for much thicker collagen fibrils. In addition to providing insight into the mechanism of collagen assembly, the ultraflat collagen matrices may also offer novel ways to bio-functionalize surfaces.
Original languageEnglish
Pages (from-to)268 - 278
Number of pages10
JournalJournal of Structural Biology
Volume148(3)
Publication statusPublished - Dec 2004

Bibliographical note

Publisher: Academic Press

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    Jiang, F., Hoerber, JKH., Howard, J., & Müller, DJ. (2004). Assembly of collagen into microribbons: effects of pH and electrolytes. Journal of Structural Biology, 148(3), 268 - 278.