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Template-assembled collagen-based polypeptides KTA-Gly-(Gly-Pro-Hyp) n -NH 2 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 -NH 2 ( 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 -NH 2 ( n = 6, 9), assume a stable triple-helical conformation in H 2 O (0.2 mg/mL) at room temperature. By contrast, Ac-(Gly-Pro-Hyp) 5 -NH 2 adopts a triple-helical conformation in H 2 O 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 -NH 2 3 ( n = 5, 6) peptides form triple-helical structures which have melting temperatures above 70 °C in H 2 O. These melting temperatures are much higher than those of the corresponding acetyl analogs, demonstrating the significant triple-helix-stabilizing effects of the KTA template. In addition, the KTA template facilitates triple-helical structures by dramatically accelerating triple-helix formation.
Feng et al. (Mon,) studied this question.