The complete chirospectroscopic signature of the peptide 310‐helix in aqueous solution

• DOI: 10.1002/bip.20109
• Publication Date: 2004-06-23T22:01:11Z
• Authors: Claudio Toniolo; Fernando Formaggio; Sabrina Tognon; Quirinus B. Broxt...; Bernard Kaptein; Rong Huang; Vladimir Setnicka; Timothy A. Keider...; Iain H. McColl; Lutz Hecht; Laurence D. Barron
• Keywords: Propanoic acid; Helix (gastropod); Raman optical activity; Side chain

Abstract We synthesized by solution methods a water‐soluble, terminally blocked heptapeptide based on five markedly helicogenic, C α ‐tetrasubstituted α‐amino acids ‐methyl‐ L ‐norvalines and two strongly hydrophilic 2‐amino‐3‐[1‐(1,4,7‐triazacyclononane)]‐ ‐propanoic acid residues at positions 2 5. A Fourier transform infrared absorption NMR analysis in deuterated chloroform aqueous solutions of the side‐chain protected synthetic precursors confirmed our working hypothesis that all oligomers are folded 3 10 ‐helical conformation. Based these findings, we exploited this as chiral reference compound for detailed electronic CD, vibrational Raman optical activity characterizations ‐helix solution. © 2004 Wiley Periodicals, Inc. Biopolymers,