Collagen degradation and denaturation are associated with various pathologic conditions (e.g. tumor, fibrosis, arthritis) and muscular skeletal injuries. Therefore, the ability to specifically target denatured collagens could lead to new diagnostics and therapeutics, as well as applications in regenerative medicine. Our research group has developed collagen hybridizing peptide (CHP), a rationally designed synthetic peptide that has a strong propensity to fold into triple helical structure of collagen and is able to bind to denatured collagen strands both in vitro and in vivo, in a manner similar to primer binding to single strand DNA during PCR. In this talk, I will summarize three recent developments: i) new results of using CHP to target collagen remodeling activities in normal and pathologic conditions, ii) CHP medicated assembly of high order structures, and iii) molecular level detection of mechanical damage in collagen. The results demonstrate CHP’s striking ability to hybridize to collagen denatured by both enzymatic activity (e.g. MMP) and by mechanical overload (e.g. tendon injury). I will discuss how CHP can be used in specific biomedical applications, including theranostics, tissue regeneration, and understanding the mechanism of mechanical injury.

Collagen hybridizing peptide: Targeted binding, self-assembly, and biomedical application

253rd National Meeting (2017)

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