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

Yang Li, Xiao Mo, Daniel Kim, S. Michael Yu

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)94-104
Number of pages11
Issue number2
StatePublished - Feb 2011


  • collagen
  • collagen mimetic peptide
  • triple helix

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry


Dive into the research topics of 'Template-tethered collagen mimetic peptides for studying heterotrimeric triple-helical interactions'. Together they form a unique fingerprint.

Cite this