NMR and quenched molecular dynamics studies of superpotent linear and cyclic α-melanotropins

Fahad Al-Obeidi, Steven D. O'Connor, Constantin Job, Victor J. Hruby, B. Montgomery Pettitt

Research output: Contribution to journalArticle

37 Scopus citations


Conformational searching, computer simulations, synthesis and NMR are used on a variety of α melanocyte-stimulating hormone (α-MSH) analogues to understand the physical characteristics required for biological potency. Peptides I (Ac-[Nle4,Asp5,D-Phe7,Lys10]α-MSH(4-10)-NH2), II (Ac- c[Nle4,Asp5,D-Phe7,Lys10]α-MSH(4-10)-NH2) and III (Ac-[Nle4,Asp5,D- Phe7,Dap10]α-MSH(4-10)-NH2 all show very similar conformational properties (backbone and side-chain torsional angles), and all-display high biological potencies. The modeling results for these compounds are supported by the NMR data. Peptide IV (Ac-c[Nle4,Asp5,D-Phe7,Dap10]α-MSH(4-10)- NH2) appears to have a markedly different conformation and has decreased biological potency.

Original languageEnglish (US)
Pages (from-to)420-431
Number of pages12
JournalJournal of Peptide Research
Issue number6
StatePublished - Jun 8 1998



  • Cyclic melanotropins
  • NMR
  • Quenched molecular dynamics
  • α-melanotropin

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

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