Acetyl-Terminated and Template-Assembled Collagen-Based Polypeptides Composed of Gly-Pro-Hyp Sequences. 2. Synthesis and Conformational Analysis by Circular Dichroism, Ultraviolet Absorbance, and Optical Rotation

Abstract

Template-assembled collagen-based polypeptides KTA-[Gly-(Gly-Pro-Hyp)n-NH2]3 (n = 1, 3, 5, 6; KTA is cis,cis-1,3,5-trimethylcyclohexane-1,3,5-tricarboxylic acid, also known as the Kemp triacid) and acetyl-terminated single-chain collagen-based analogs Ac-(Gly-Pro-Hyp)n-NH2 (n = 1, 3, 5, 6, 9) were synthesized by solid phase segment condensation methods. The triple-helical propensities of these collagen analogs were investigated using circular dichroism, ultraviolet absorbance, optical rotation, and nuclear magnetic resonance measurements. The acetyl analogs, Ac-(Gly-Pro-Hyp)n-NH2 (n = 6, 9), assume a stable triple-helical conformation in H2O (0.2 mg/mL) at room temperature. By contrast, Ac-(Gly-Pro-Hyp)5-NH2 adopts a triple-helical conformation in H2O only below 18 °C at a concentration of 0.2 mg/mL. For the template-assembled collagen analogs, results show that KTA-[Gly-(Gly-Pro-Hyp)n-NH2]3 (n = 5, 6) peptides form triple-helical structures which have melting temperatures above 70 °C in H2O. These meltin...