NMR and quenched molecular dynamics studies of superpotent linear and cyclic alpha-melanotropins |
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Authors: | F Al-Obeidi SD O'Connor C Job VJ Hruby BM Pettitt |
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Affiliation: | Department of Chemistry, University of Arizona, Tucson, USA. |
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Abstract: | Conformational searching, computer simulations, synthesis and NMR are used on a variety of alpha melanocyte-stimulating hormone (alpha-MSH) analogues to understand the physical characteristics required for biological potency. Peptides I (Ac-Nle4,Asp5,D-Phe7,Lys10]alpha-MSH(4-10)-NH2), II (Ac-cNle4,Asp5,D-Phe7,Lys10]alpha-MSH(4-10)-NH2) and III (Ac-Nle4,Asp5,D-Phe7,Dap10]alpha-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-cNle4,Asp5,D-Phe7,Dap10]alpha-MSH(4-10)-NH2) appears to have a markedly different conformation and has decreased biological potency. |
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