1981
DOI: 10.1016/0014-5793(81)80236-0
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The space structures of α‐melanotropin

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Cited by 13 publications
(5 citation statements)
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“…The cyclic amide analogues reported here were designed to test a hypothesis recently proposed (Sugg et al, 1986) for a bioactive conformation of the melanotropins. The 5 to 8 cyclization was suggested by computer modeling studies which predicted a salt bridge between the Glu5 and Arg8 side chains (Nikiforovich et al, 1981(Nikiforovich et al, , 1984. In order to promote cyclization and to stabilize the backbone to a left-handed turn, D stereochemistry is required at position 5.…”
Section: Discussionmentioning
confidence: 99%
“…The cyclic amide analogues reported here were designed to test a hypothesis recently proposed (Sugg et al, 1986) for a bioactive conformation of the melanotropins. The 5 to 8 cyclization was suggested by computer modeling studies which predicted a salt bridge between the Glu5 and Arg8 side chains (Nikiforovich et al, 1981(Nikiforovich et al, , 1984. In order to promote cyclization and to stabilize the backbone to a left-handed turn, D stereochemistry is required at position 5.…”
Section: Discussionmentioning
confidence: 99%
“…Several computational studies have led to the hypothesis of a bioactive turn conformation in melanocortin peptides localized in the conserved message sequence His‐Phe‐Arg‐Trp (22–25). In support of the bioactive turn hypothesis, cyclic analogs of α ‐MSH (Ac‐Ser‐Tyr‐Ser‐Met‐Glu‐His‐Phe‐Arg‐Trp‐Gly‐Lys‐Pro‐Val‐NH 2 ) and NDP‐MSH (Ac‐Ser‐Tyr‐Ser‐Nle‐Glu‐His‐ d ‐Phe‐Arg‐Trp‐Gly‐Lys‐Pro‐Val‐NH 2 ), such as MTII (Ac‐Nle‐c[Asp‐His‐ d ‐Phe‐Arg‐Trp‐Lys]‐NH 2 ; 26,27) and related compounds (Ac‐Nle‐c[Asp‐Pro‐ d ‐Phe‐Arg‐Trp‐Lys]‐NH 2 ), have exhibited enhanced potency, selectivity, and/or prolonged duration of action (28–31).…”
Section: Analytical Data For the Peptides Tested In This Studyamentioning
confidence: 99%
“…54,55,58,59 The time histories of the distances between all pairs of the positively charged nitrogens on the end of the Arg 8 side chain, and the negatively charged oxygens on the end of the Glu 5 side chain were monitored and one pair is displayed in Figure 5e. From initial distances of 16 -19 Å for the various pairs, these distances fall to less that 3 Å within the first 5 ns of the simulation, indicating a close contact between these two side chains.…”
Section: Figurementioning
confidence: 99%
“…66 Another interesting question about the conformation of ␣-MSH is whether the biologically active structure is stabilized by a salt bridge. Two possible salt bridges have been proposed, one 54,55,58,59 involving the electrostatically charged side chains of Glu 5 and Arg 8 and the other 1,44 involving Glu 5 and Lys 11 . Experiments based on structure-activity studies have not been conclusive, first on whether a salt bridge does exist and second on the importance of these charged moieties for the potency of this peptide.…”
mentioning
confidence: 99%