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Vibrational Raman optical activity of alanyl peptide oligomers: A new perspective on aqueous solution conformation


Vibrational Raman optical activity of alanyl peptide oligomers: A new perspective on aqueous solution conformation



Biopolymers 34(3): 303-313



ISSN/ISBN: 0006-3525

DOI: 10.1002/bip.360340302

The vibrational Raman optical activity (ROA) spectra of di- and tri-L-alanine in the range 650-1750 cm-1 have been measured in H-2O and D-2O solution at high, neutral, and low pH and pD. Corresponding ROA spectra for tetra- and penta-L-alanine have also been obtained, but over a more restricted set of pH and pD conditions. There are similarities with the ROA spectrum of L-alanine below apprx 1200 cm-1, but the spectra are very different above this wavenumber due to the influence of the vibrational coordinates of the peptide group. The similar overall appearance of the di-, tri-, and tetrapeptide ROA under selected conditions of pH and pD, and of all four peptide ROA spectra in DCl and HCl solutions, in the backbone skeletal stretch region apprx 1050-1200 cm-1 and the extended amide III region apprx 1250-1350 cm-1, suggests that the backbone conformation is approximately the same in all four structures. One difference, however, is a shift of a large positive ROA band in H-2O at apprx 1341 cm-1 in the dipeptide, assigned to C-alpha-H and in-plane N-H deformations, down to apprx 1331 cm-1 in the tripeptide and to apprx 1315 cm-1 in the tetrapeptide and pentapeptide (the last in HCl due to insufficient solubility in H-2O), which indicates increasing delocalization of the corresponding normal mode with increasing chain length. Our results do not support the suggestion that stabilizing interactions of the zwitterionic end groups in tri-L-alanine at neutral pH leads to a different solution structure to that at high pH.

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Accession: 009723834

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