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High-performance liquid chromatography of amino acids, peptides and proteins CXXVIII. Effect of d-amino acid substitutions on the reversed-phase high-performance liquid chromatography retention behaviour of neuropeptide Y[18–36] analogues by M.I. Aguilar; S. Mougos; J. Boublik; J. Rivier; M.T.W. Hearn is a Chemistry article available to read on EtoBox.

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The reversed-phase high-performance liquid shromatographic (RP-HPLC) gradient elution behaviour of a series of peptides related to Neuropeptide Y (NPY) has been investigated. The peptides studied included NPY, NPY[13-361, NPY[l8-361 and a series of 16 analogues of NPY [18-361, each with a single D-anhO 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-aIIIin0 acid substitutions in the sequence region encompassing amino acid residues NPY [27-311 of these NPY [l&36] peptides significantly influence the interactive behaviour of these peptides relative to the unsubstituted NPY [18-361 molecule, while substitutions in the N-and C-terminal regions had little effect. Further, these results indicate that, in hydrophobic environments, NPY[18-361 adopts a significant degree of secondary structure which is severely disrupted by the presence of the ~-amino acids in the central portion of the molecule.

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Author

M.I. Aguilar; S. Mougos; J. Boublik; J. Rivier; M.T.W. Hearn

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1873-3778)

Published

1993

Language

EN

Field

Chemistry (Physical Sciences)