The self-assembly of a mini-fibril with axial periodicity from a designed collagen-mimetic triple helix.

ABSTRACT: In this work we describe the self-assembly of a collagen-like periodic mini-fibril from a recombinant triple helix. The triple helix, designated Col108, is expressed in Escherichia coli using an artificial gene and consists of a 378-residue triple helix domain organized into three pseudo-repeating sequence units. The peptide forms a stable triple helix with a melting temperature of 41 °C. Upon increases of pH and temperature, Col108 self-assembles in solution into smooth mini-fibrils with the cross-striated banding pattern typical of fibrillar collagens. The banding pattern is characterized by an axially repeating feature of ∼35 nm as observed by transmission electron microscopy and atomic force microscopy. Both the negatively stained and the positively stained transmission electron micros

SUBMITTER: Kaur PJ 

PROVIDER: S-EPMC4423709 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature