Local orientational disorder in peptide fibrils probed by a combination of residue-specific 13C–18O labelling, polarised infrared spectroscopy and molecular combing

José C. Rodríguez-Pérez; Ian W. Hamley; Sally L. Gras; Adam M. Squires

doi:10.1039/C2CC35586H

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Local orientational disorder in peptide fibrils probed by a combination of residue-specific ¹³C–¹⁸O labelling, polarised infrared spectroscopy and molecular combing†

José C. Rodríguez-Pérez,^a Ian W. Hamley,^a Sally L. Gras^b and Adam M. Squires*^a

Author affiliations

* Corresponding authors

^a Department of Chemistry, University of Reading, Whiteknights Campus, Reading RG6 6AD, UK
E-mail: a.m.squires@reading.ac.uk
Tel: +44 118 378 4736

^b Department of Chemical and Biomolecular Engineering and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria 3010, Australia

Abstract

A novel combination of site-specific isotope labelling, polarised infrared spectroscopy and molecular combing reveals local orientational ordering in the fibril-forming peptide YTIAALLSPYSGGRADS. Use of ¹³C–¹⁸O labelled alanine residues demonstrates that the N-terminal end of the peptide is incorporated into the cross-beta structure, while the C-terminal end shows orientational disorder.

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Article information

DOI: https://doi.org/10.1039/C2CC35586H
Article type: Communication
Submitted: 01 Aug 2012
Accepted: 22 Aug 2012
First published: 23 Aug 2012

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Chem. Commun., 2012,48, 11835-11837

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Local orientational disorder in peptide fibrils probed by a combination of residue-specific ¹³C–¹⁸O labelling, polarised infrared spectroscopy and molecular combing

J. C. Rodríguez-Pérez, I. W. Hamley, S. L. Gras and A. M. Squires, Chem. Commun., 2012, 48, 11835 DOI: 10.1039/C2CC35586H

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Chemical Communications