Comparative EPR and fluorescence conformational studies of fully active spin-labeled melanotropic peptides

FEBS Lett. 2001 May 25;497(2-3):103-7. doi: 10.1016/s0014-5793(01)02449-8.

Abstract

Similar to melanocyte stimulating hormone (alpha-MSH), its potent and long-acting analogue, [Nle(4), D-Phe(7)]alpha-MSH, when labeled with the paramagnetic amino acid probe 2,2,6,6-tetramethylpiperidine-N-oxyl-4-amino-4-carboxylic acid (Toac), maintains its full biological potency, thus validating any comparative structural investigations between the two labeled peptides. Correlation times, calculated from the electron paramagnetic resonance signal of Toac bound to the peptides, and Toac-Trp distances, estimated from the Toac fluorescence quenching of the Trp residue present in the peptides, indicate a more rigid and folded structure for the potent analogue as compared to the hormone, in aqueous medium.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Assay
  • Cyclic N-Oxides / chemistry*
  • Dose-Response Relationship, Drug
  • Electron Spin Resonance Spectroscopy
  • Hydrogen-Ion Concentration
  • In Vitro Techniques
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Tertiary / physiology
  • Rana catesbeiana
  • Skin Pigmentation / drug effects
  • Spectrometry, Fluorescence
  • Spectrophotometry
  • Tryptophan / chemistry
  • alpha-MSH / analogs & derivatives
  • alpha-MSH / chemistry*
  • alpha-MSH / pharmacology

Substances

  • Cyclic N-Oxides
  • alpha-MSH
  • MSH, 4-Nle-7-Phe-alpha-
  • Tryptophan
  • 2,2,6,6-tetramethylpiperidine-N-oxide-4-amino-4-carboxylic acid