α-proton Chemical Shift Index and Amide Proton Chemical Shift Temperature Coefficient of Melittin in Methanol:...

The methods of the α-proton chemical shift index (CSI) and the amide proton (NH) chemical shift temperature coefficient (Δδ/ΔT) were found experimentally by a number of studies on proton NMR chemical shifts of peptides and proteins in an aqueous solution, and have been widely accepted. They provide an insight into secondary structures and intra-molecular hydrogen bonds in peptides and proteins without complex calculation. Our question is whether the methods are applicable to helical peptides in methanol. Melittin, a peptide of 26 amino acid residues found in bee venom, has been known to consist of two helices (the residues 2-11 and 13-26) connected by a kink section (the residues 11-13). Employing the methods for melittin in methanol, we have shown that most of the CSI's for the residues 3-10 and 14-26 are - 1, and the Δδ/ΔT's for the residues 5-26 except 6 and 14 are more positive than - 6 ppb/℃. If the methods are applicable to melittin in methanol, these results indicate that helix structures are formed in the regions of the residues 3-10 and 14-26 and NH's in the residues 5-26 except 6 and 14 are involved in intra-molecular hydrogen bonds. The helical structure evaluated from the methods, hence, agrees nearly with the known helix structure. We also apply the methods to D-Pro14 melittin (synthetic melittin) and alamethicin (a peptide of 20 amino acid residues) in methanol, and show that they virtually work well.