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. Previously, my research group introduced 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 primers binding to single strand DNAs during PCR. We demonstrated CHP’s striking ability to hybridize to collagen denatured by both enzymatic activity (e.g. MMP) and by mechanical overload (e.g. tendon injury). In this talk, I will present our recent efforts in developing the next generation CHPs: i) CHPs comprised of fluoroprolines which have low propensity to fold into homotrimers but are able to hybridize to collagen strands, allowing reproducible <i>in vivo</i> experiments, ii) CHPs based on peptoids with expanded side chain architectures that can be used to produce diverse CHP library, and iii) dimeric CHPs that can efficiently capture collagen fragments from biological fluid.  We believe that these new CHPs will not only facilitate mechanistic study of collagen degradation associated with pathology, but also bring us one step closer to realizing CHP-based diagnostics and therapeutics.

Next-generation collagen hybridizing peptides

2019 Spring National Meeting

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