Circular permutation directs orthogonal assembly in complex collagen peptide mixtures.

ABSTRACT: Multiple types of natural collagens specifically assemble and co-exist in the extracellular matrix. Although noncollagenous trimerization domains facilitate the folding of triple-helical regions, it is intriguing to ask whether collagen sequences are also capable of controlling heterospecific association. In this study, we designed a model system mimicking simultaneous specific assembly of two collagen heterotrimers using a genetically inspired operation, circular permutation. Previously, surface charge-pair interactions were optimized on three collagen peptides to promote the formation of an abc-type heterotrimer. Circular permutation of these sequences retained networks of stabilizing interactions, preserving both triple-helical structure and heterospecificity of assembly. Combining orig

SUBMITTER: Xu F 

PROVIDER: S-EPMC3814757 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature