Conformation of human calcitonin gene-related peptide (8-37) in aqueous solution as determined by circular dichroism spectroscopy

J Pharm Biomed Anal. 1993 Feb;11(2):89-93. doi: 10.1016/0731-7085(93)80128-n.

Abstract

Circular dichroism (CD) studies on CGRP(8-37) indicate that there is some latent alpha-helical structure in aqueous solution. However, the amount is quite small (approximately 10% at 5 degrees C), which is substantially less than for CGRP itself (approximately 15-20%). Upon addition of helix-promoting materials, such as trifluoroethanol and sodium dodecyl sulphate, the helix content increases dramatically. No evidence for helix stabilization upon the addition of zinc was observed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Calcitonin
  • Calcitonin Gene-Related Peptide / chemistry*
  • Circular Dichroism
  • Humans
  • Peptide Fragments / chemistry*
  • Protein Conformation
  • Protein Structure, Secondary / drug effects
  • Sodium Dodecyl Sulfate / pharmacology
  • Solutions
  • Trifluoroethanol / pharmacology
  • Water
  • Zinc / metabolism

Substances

  • Peptide Fragments
  • Solutions
  • Water
  • calcitonin gene-related peptide (8-37)
  • Sodium Dodecyl Sulfate
  • Trifluoroethanol
  • Calcitonin
  • Zinc
  • Calcitonin Gene-Related Peptide