The effect of N-terminal substitutions on the biological activity of MSH fragments.
In order to study the role of N-terminal substitutions of peptide sequences related to the active site of alpha-melanotropin, [Glp5]alpha-MSH(5-10), [Glp5,D-Phe7]alpha-MSH(5-10), [Sar5,D-Phe7]alpha-MSH(5-10), [Nle4,D-Phe7]alpha-MSH(4-10), [N-carbamoyl]alpha-MSH(5-10), and formyl and acetyl derivatives of alpha-MSH(5-10), [Gly5]alpha-MSH(5-10) and [Gly5,D-Phe7]alpha-MSH(5-10), were synthesized in solution. The N-terminal acylations enhance by 2 to 10 times the melanin-dispersing activity of the unsubstituted sequences. Alkylation of the N-terminus does not change the biological activity of the parent peptide, suggesting the necessity of a carbonyl group for increasing the hormonal effect.
Süli-Vargha
H
H
Research Group of Peptide Chemistry, Hungarian Academy of Sciences, Budapest.
Bódi
J
J
Medzihradszky-Schweiger
H
H
Medzihradszky
K
K
D000595:Amino Acid Sequence; D000818:Animals; D009074:Melanocyte-Stimulating Hormones / Q000737:chemistry* / Q000494:pharmacology*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000494:pharmacology*; D011895:Rana ridibunda; D013329:Structure-Activity Relationship
D010446:Peptide Fragments; D009074:Melanocyte-Stimulating Hormones