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Size of the aliphatic chain of sodium houttuyfonate analogs determines their affinity for renin and angiotensin I converting enzyme.

Abstract：

: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 and 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 of SHAs. Ability of SHAs to inhibit enzyme activities and quench protein fluorescence was greater with renin than with ACE. The presence of an ACE substrate (angiotensin I) did not reduce quenching ability of SHAs, suggesting that enzyme-inhibitor interactions did not involve the active site or the substrate was displaced by inhibitor molecules. The results showed that renin is a more sensitive target than ACE for the potential antihypertensive ability of SHAs.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Yuan L,Wu J,Aluko RE

doi

10.1016/j.ijbiomac.2007.03.004

subject

Has Abstract

pub_date

2007-08-01 00:00:00

pages

274-80

issue

3

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(07)00097-9

journal_volume

41

pub_type

杂志文章

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