Vibrational Raman Optical Activity Characterization of Poly(L-proline) II Helix in Alanine Oligopeptides

Iain H. McColl, Ewan W. Blanch, Lutz Hecht, Neville R. Kallenbach, Laurence D. Barron

Research output: Contribution to journalArticle

Abstract

A vibrational Raman optical activity (ROA) study of a series of alanine peptides in aqueous solution is presented. The seven-alanine peptide Acetyl-OOAAAAAAAOO-Amide (OAO), recently shown by NMR and UVCD to adopt a predominantly poly(l-proline II) (PPII) helical conformation in aqueous solution, gave an ROA spectrum very similar to that of disordered poly(l-glutamic acid) which has long been considered to adopt the PPII conformation, both being dominated by a strong positive extended amide III ROA band at ∼1319 cm-1 together with weak positive amide I ROA intensity at ∼1675 cm-1. A series of alanine peptides Ala2-Ala6 studied in their cationic states in aqueous solution at low pH displayed ROA spectra which steadily evolved toward that of OAO with increasing chain length. As well as confirming that alanine peptides can support the PPII conformation in aqueous solution, our results also confirm the previous ROA band assignments for PPII structure, thereby reinforcing the foundation for ongoing ROA studies of unfolded and partially folded proteins.

Original languageEnglish (US)
Pages (from-to)5076-5077
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number16
DOIs
StatePublished - Apr 28 2004

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Optical Rotation
Oligopeptides
Amides
Proline
Alanine
Peptides
Conformations
Chain length
Glutamic Acid
Nuclear magnetic resonance
Proteins
Acids
polyproline

ASJC Scopus subject areas

  • Chemistry(all)

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Vibrational Raman Optical Activity Characterization of Poly(L-proline) II Helix in Alanine Oligopeptides. / McColl, Iain H.; Blanch, Ewan W.; Hecht, Lutz; Kallenbach, Neville R.; Barron, Laurence D.

In: Journal of the American Chemical Society, Vol. 126, No. 16, 28.04.2004, p. 5076-5077.

Research output: Contribution to journalArticle

McColl, Iain H. ; Blanch, Ewan W. ; Hecht, Lutz ; Kallenbach, Neville R. ; Barron, Laurence D. / Vibrational Raman Optical Activity Characterization of Poly(L-proline) II Helix in Alanine Oligopeptides. In: Journal of the American Chemical Society. 2004 ; Vol. 126, No. 16. pp. 5076-5077.
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AU - Barron, Laurence D.

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N2 - A vibrational Raman optical activity (ROA) study of a series of alanine peptides in aqueous solution is presented. The seven-alanine peptide Acetyl-OOAAAAAAAOO-Amide (OAO), recently shown by NMR and UVCD to adopt a predominantly poly(l-proline II) (PPII) helical conformation in aqueous solution, gave an ROA spectrum very similar to that of disordered poly(l-glutamic acid) which has long been considered to adopt the PPII conformation, both being dominated by a strong positive extended amide III ROA band at ∼1319 cm-1 together with weak positive amide I ROA intensity at ∼1675 cm-1. A series of alanine peptides Ala2-Ala6 studied in their cationic states in aqueous solution at low pH displayed ROA spectra which steadily evolved toward that of OAO with increasing chain length. As well as confirming that alanine peptides can support the PPII conformation in aqueous solution, our results also confirm the previous ROA band assignments for PPII structure, thereby reinforcing the foundation for ongoing ROA studies of unfolded and partially folded proteins.

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