The effect of N-terminal substitutions on the biological activity of MSH fragments. |
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Authors: | H Sü li-Vargha J B di H Medzihradszky-Schweiger and K Medzihradszky |
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Institution: | Research Group of Peptide Chemistry, Hungarian Academy of Sciences, H-1518, Budapest 112, P.O. Box 32, Hungary |
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Abstract: | In order to study the role of N-terminal substitutions of peptide sequences related to the active site of -melanotropin, Glp5] -MSH(5–10), Glp5,
-Phe7] -MSH(5–10), Sar5,
-Phe7] -MSH(5–10), Nle4,
-Phe7] -MSH(4–10), N-carbamoyl] -MSH(5–10), and formyl and acetyl derivatives of -MSH(5–10), Gly5] -MSH(5–10) and Gly5,
-Phe7] -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. |
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Keywords: | Melanotropin fragments Synthesis Biological activity N-acyl peptides N-alkyl peptide |
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