Studies on the conformation and interactions of elastin secondary structure of synthetic repeat hexapeptides.

Repeat hexapeptides of elastin have been synthesized and studied with nuclear magnetic resonance methods. The deuterium substituted hexapeptide HCO-Ala1-Pro2-(2H2) Gly3-Val4-Gly5-Val6-OMe allowed completion of the proton assignments and specifically the definitive assignments of the Gly3 and Gly5 resonances. Solvent titrations followed by carbon-13 magnetic resonances are reported which delineate the Ala1 C-O and Gly5 C-O as intramolecularly hydrogen bonded. This coupled with the proton magnetic resonance data which delineated the Gly3 NH and VAL4 NH as candidates for intramolecular hydrogen bonding lead to the proposal of two hydrogen bonds, one between the Ala1 C-O and the Val4NH and the second between the Gly5C-O and the Gly3NH. The probability, or mol fraction, of occurrence of these secondary structural features is demonstrated to be high.