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NAAS Journal
International Journal of Advanced Chemistry Research
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Vol. 7, Issue 1, Part A (2025)

Conformational analysis of pipecolic acid substituted collagen model peptides

Author(s):

Sonu Ram Shankar and Bhavesh Shandilya

Abstract:

Collagen model peptides, (Xaa-Yaa-Gly)10 have been used to understand the propensity of the amino acid in Xaa nad Yaa positions. Five membered cyclic imino acid, proline (Pro), have found to be most investigated model. In this investigation Pipecolic acid (Pip), a six member cyclic imino acid and a higher homologue of Pro has been used for sysnthesis of (Pro-Pip-Gly)10, (Pip-Pro-Gly)10, and (Pip-Pip-Gly)10 have been synthesized, characterised and compared with (Pro-Pro-Gly)10 for their physical property such as solubility. Their triple helix formation characteristics at 4 °C has been investigated by circular dichroism (CD) spectroscopy. It has been found that Pip has higher propensity for Yaa position compared to Xaa position in triple helix conformations.

Pages: 67-74  |  116 Views  48 Downloads


International Journal of Advanced Chemistry Research
How to cite this article:
Sonu Ram Shankar and Bhavesh Shandilya. Conformational analysis of pipecolic acid substituted collagen model peptides. Int. J. Adv. Chem. Res. 2025;7(1):67-74. DOI: 10.33545/26646781.2025.v7.i1a.316
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