2. Coupled Conformational Equilibria in Peptide-Dendron Conjugates
Jon R. Parquette, Department of Chemistry, The Ohio State University, Columbus, OH 43210
Dendrons
Sequence A
i, i+11
Ac-AAD*AKAAAAKAAAD*YA-NH2 B
i, i+10
Ac-AAD*AKAAAAKAAD*AYA-NH2 C
i, i+9
Ac-AAD*AKAAAAKAD*AAYA-NH2 D
i, i+8
Ac-AAD*AKAAAAKD*AAAYA-NH2 E
i, i+7
Ac-AAD*AAKAAAD*KAAAYA-NH2 F
i, i+6
Ac-AAD*AKAAAD*AKAAAYA-NH2 G
i, i+5
Ac-AAD*AKAAD*AAKAAAYA-NH2 H
i, i+4
Ac-AAD*AKAD*AAKAAAAYA-NH2 I
Control
Ac-AAAAKAAAAKAAAAYA-NH2
In this work, we are attempting to understand how multiple elements of secondary structure cooperate in determining the conformational properties of synthetic, folded macromolecules. These studies will facilitate the design of materials with novel functions not present in biological materials. Specifically, we have prepared peptide-dendron conjugates based on a polyalanine sequence having a strong tendency to adopt the -helical conformation. Preliminary studies indicate that when the dendrons are incorporated at the i, i+10 (B) or i, i+6 (F) positions the peptides actually adopt a -sheet conformation that further assembles into fibrils. These -sheet structures exhibit a strong capacity for chirality transfer to the dendrons whereas the chirality transfer does not take place when the peptide is in the -helical form. D*
Circular Dichroism
Atomic Force Microscopy
M Bias of Dendron