ISSN:
0020-7608
Schlagwort(e):
Computational Chemistry and Molecular Modeling
;
Atomic, Molecular and Optical Physics
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Chemie und Pharmazie
Notizen:
Based on previous research from these laboratories various structural analogs of 3-hydroxyflavone were tested for inhibition of glyoxalse I (S-lactoyl-glutathione methylglyoxal lyase, isomerizing; EC 4.4.1.5). The substrate of glyoxalse I (Glo I), methylglyoxal, has growth inhibitory properties. Glo I was purified 7000-fold from human red blood cells, and the concentration of various flavones was determined for 50% inhibition (I50) of enzyme activity. These compounds resemble the transition state of the methylglyoxal hemimercaptal as previously reported [Int. J. Quantum Chem. Quantum Biol. Symp., 10, 357 (1983)]. The I50 in μM varies from 5 to 330 for the flavones tested, with the parent compound 3-hydroxyflavone having an I50 of 10 μM. The most inhibitory compound in vitro was myricetin (5 μM), which has a 3′,4′,5′-trihydroxyphenolic ring at the 2 position of the pyrone ring.
Zusätzliches Material:
4 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/qua.560260720
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