Size of the aliphatic chain of sodium houttuyfonate analogs determines their affinity for renin and angiotensin I converting enzyme.
作者： Lujiang Yuan , Jianping Wu , Rotimi E. Aluko
DOI: 10.1016/J.IJBIOMAC.2007.03.004
关键词:
摘要: Sodium houttuyfonate analogs (SHAs), CH(3)-(CH(2))(n)-CO-CH(2)-CH(OH)SO(3)Na, (n=6-14) were synthesized and their molecular interactions with renin angiotensin I converting enzyme (ACE) studied using fluorescence quenching techniques. Unlike renin, inhibition of ACE activity was not directly proportional to the aliphatic chain length SHAs. Ability SHAs inhibit activities quench protein greater than ACE. The presence an substrate (angiotensin I) did reduce ability SHAs, suggesting that enzyme-inhibitor involve active site or displaced by inhibitor molecules. results showed is a more sensitive target for potential antihypertensive
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