Template-assembled collagen-based polypeptidesKTA-[Gly-(Gly-Pro-Hyp)
n-NH
2]
3(
n = 1, 3, 5, 6; KTAis
cis,
cis-1,3,5-trimethylcyclohexane-1,3,5-tricar
boxylicacid, also known as the Kemp triacid) andacetyl-terminatedsingle-chain collagen-based analogsAc-(Gly-Pro-Hyp)
n-NH
2 (
n= 1, 3, 5, 6, 9) were synthesized by solid phasesegment condensation methods. The triple-helical propensities ofthese collagen analogs were investigated usingcircular dichroism, ultraviolet absorbance, optical rotation, andnuclear magnetic resonance measurements. The acetylanalogs, Ac-(Gly-Pro-Hyp)
n-NH
2(
n = 6, 9), assume a stable triple-helical conformation inH
2O (0.2 mg/mL) atroom temperature. By contrast,Ac-(Gly-Pro-Hyp)
5-NH
2 adopts a triple-helicalconformation in H
2O only below 18
C at a concentration of 0.2 mg/mL. For the template-assembledcollagen analogs, results show that KTA-[Gly-(Gly-Pro-Hyp)
n-NH
2]
3(
n = 5, 6) peptides form triple-helical structures whichhave melting temperatures a
bove 70
C in H
2O. These melting temperatures are muchhigher than those of the corresponding acetyl analogs,demonstratingthe significant triple-helix-stabilizing effects of the KTA template.In addition, the KTA template facilitates triple-helical structures by dramatically accelerating triple-helixformation.