Yang Li - Template-tethered collagen mimetic peptides for studying heterotrimeric triple-helical interactions.

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  Li, Y.; Mo, X.; Kim, D.; Yu, S. M., Biopolymers 2011, 95, (2),   94-104. doi: 10.1002/bip.21536. Epub 2010 Aug 24.


  Collagen mimetic peptides (CMPs) have been used to elucidate the   structure and stability of the triple helical conformation of   collagen molecules. Although CMP homotrimers have been widely   studied, very little work has been reported regarding CMP   heterotrimers because of synthetic difficulties. Here, we present   the synthesis and characterization of homotrimers and ABB type   heterotrimers comprising natural and synthetic CMP sequences that   are covalently tethered to a template, a tris(2-aminoethyl) amine   (TREN) succinic acid derivative. Various tethered heterotrimers   comprising synthetic CMPs [(ProHypGly)6,   (ProProGly)6] and CMPs representing specific domains   of type I collagen were synthesized and characterized in terms of   triple helical structure, thermal melting behavior, and refolding   kinetics. The results indicated that CMPs derived from natural   type I collagen sequence can form stable heterotrimeric helical   complexes with artificial CMPs and that the thermal stability and   the folding rate increase with the increasing number of helical   stabilizing amino acids (e.g. Hyp) in the peptide chains.   Covalent tethering enhanced the thermal stability and refolding   kinetics of all CMPs; however, their relative values were not   affected suggesting that the tethered system can be used for   comparative study of heterotrimeric CMP's folding behavior in   regards to chain composition and for characterization of   thermally unstable CMPs. © 2010 Wiley Periodicals, Inc.   Biopolymers 95: 94–104, 2011.

  Address (URL): http://http://onlinelibrary.wiley.com/doi/10.1002/bip.21536/full