Allosteric modulation of anti-HIV drug and ferric heme binding to human serum albumin
β Scribed by Alessio Bocedi; Stefania Notari; Enea Menegatti; Gabriella Fanali; Mauro Fasano; Paolo Ascenzi
- Book ID
- 111310310
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 278 KB
- Volume
- 272
- Category
- Article
- ISSN
- 1432-1327
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Binding of drugs to plasma proteins is an important determinant for their efficacy because it modulates drug availability to the intended target. Co-administered drugs may bind to the same protein site or to different functionally linked clefts following competitive and allosteric mechanisms. Here,
Heme endows human serum albumin (HSA) with globin-like reactivity and spectroscopic properties. Here, the effect of chlorpropamide, digitoxin, furosemide, indomethacin, phenylbutazone, sulfisoxazole, tolbutamide, and warfarin on peroxynitrite isomerization to NO 3 -by ferric HSA-heme (HSA-heme-Fe(II