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- W2034981725 abstract "Renin inhibition was evaluated for a series of peptide analogues of angiotensinogen with different chain lengths. Systematic deletion of amino acid residues from the hexapeptide BocPheHisLeu-ValIleHisOCH3 showed that the presence of residues at the N-terminal Phe and His positions was essential for efficient enzyme-inhibitor binding whereas the C-terminal Ile and His residues were much less important. Synthesis of a tetrapeptide analogue shortened at the C-terminus and containing modified side chains produced a potent inhibitor of renin which demonstrated hypotensive activity in a salt depleted monkey." @default.
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- W2034981725 date "1986-09-01" @default.
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- W2034981725 title "Peptide analogues of angiotensinogen effect of peptide chain length on renin inhibition" @default.
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- W2034981725 doi "https://doi.org/10.1016/s0006-291x(86)80274-1" @default.
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