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First Interchain Peptide Interaction Detected by ESR in Fully Synthetic, Template-Assisted, Two-Helix Bundles

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journal contribution
posted on 18.11.1999 by Alessandra Polese, D. Joe Anderson, Glenn Millhauser, Fernando Formaggio, Marco Crisma, Fernando Marchiori, Claudio Toniolo
We have designed and synthesized by solution methods two simple two-helix bundles based on a conformationally constrained cyclo-dipeptide template to the side chains of which two short, 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid spin-monolabeled, 310-helical peptides are covalently tethered. The preferred conformation of the appended chains has been assessed by FTIR absorption. The conclusions are corroborated by an X-ray diffraction analysis of one of the terminally blocked pentapeptide tails. For the first time, a solvent-dependent, inter-helix interaction has been monitored by conventional ESR spectroscopy on fully synthetic peptide systems. Half-field ESR measurements of these side-chain-substituted templates provided an experimental average distance between the two labels that is in good accord with that determined in a molecular modeling study.

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