neuropeptide-y and acetonitrile

The reversed-phase high-performance liquid chromatographic (RP-HPLC) gradient elution behaviour of a series of peptides related to Neuropeptide Y (NPY) has been investigated. The peptides studied included NPY, NPY[13-36], NPY[18-36] and a series of 16 analogues of NPY[18-36], each with a single D-amino acid substitution. Chromatographic parameters which relate to the interactive contact area and the binding affinity have been evaluated with two different stationary phase ligands and two organic modifiers. The results demonstrate that D-amino acid substitutions in the sequence region encompassing amino acid residues NPY[27-31] of these NPY[18-36] peptides significantly influence the interactive behaviour of these peptides relative to the unsubstituted NPY[18-36] molecule, while substitutions in the N- and C-terminal regions had little effect. Further, these results indicate that, in hydrophobic environments, NPY[18-36] adopts a significant degree of secondary structure which is severely disrupted by the presence of the D-amino acids in the central portion of the molecule.

Topics: Acetonitriles; Amino Acid Sequence; Amino Acids; Chemical Phenomena; Chemistry, Physical; Chromatography, High Pressure Liquid; Circular Dichroism; Indicators and Reagents; Ligands; Molecular Sequence Data; Neuropeptide Y; Peptide Fragments; Stereoisomerism; Temperature