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• W2020563796 abstract "To investigate the roles of the hydrophobic residues in the ANP molecule on biological activities, we synthesized a series of analogs containing various phenylalanine-homologs in position 8 or methionine-homologs in position 12. Among the analogs [pCl-Phe8]-alpha-hANP(7-28) was 4.8 times as potent as alpha-hANP(7-28) in cGMP accumulation and 3.5 times as potent in vasorelaxant activity. All the analogs showed nanomolar affinity to the receptor. In contrast, vasorelaxation and cGMP accumulation activity of the analogs ranged widely. These results suggest that these hydrophobic residues in the cyclic core are critical for vasorelaxant activity rather than for the apparent receptor binding, and that these residues may possibly discriminate the bioactive receptor which is coupled to guanylate cyclase from the non-coupled receptor." @default.
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• W2020563796 date "1990-11-01" @default.
• W2020563796 modified "2023-09-27" @default.
• W2020563796 title "Importance of hydrophobic residues in α-human atrial natriuretic peptide (α-hANP) for vasorelaxant activity" @default.
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• W2020563796 doi "https://doi.org/10.1016/0006-291x(90)91541-y" @default.
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