2,3-Benzodiazepines containing a centre of asymmetry at C-5 possess both central and helical chiralities, and the solution of their racemates contains four molecular species. The binding of these compounds to human serum albumin (HSA) was studied by affinity chromatography. The binding strength depe
Exploring the Drug-Binding Site Sudlow I of Human Serum Albumin: The Role of Water and Trp214 in Molecular Recognition and Ligand Binding
β Scribed by Dr. Osama K. Abou-Zied; Najla Al-Lawatia
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 492 KB
- Volume
- 12
- Category
- Article
- ISSN
- 1439-4235
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The binding of drugs known to interact with area I on human serum albumin (HSA) was investigated using a chiral stationary phase obtained by anchoring HSA to a silica matrix. In particular, this high-pressure affinity chromatography selector was employed to study the binding properties of the indivi
The Cu(I1) binding site of human serum albumin is located on the N-terminal sequence Asp-Ala-His.l-4 It has been shown that the synthetic tripeptide Asp-Ala-His N-methylamide exhibits an affinity towards Cu(I1) ions even higher than that of serum albumin itself.5 In general, i t has been observed th
The high-affinity monoclonal anti-estradiol antibody 9D3 presents a specificity defect towards estradiol-3sulphate and 3-glucuronide conjugates incompatible with use in direct immunoassays. The corresponding single-chain variable fragment (scFv), cloned and produced in E. coli, exhibited a 10-fold l