Quantitative Analysis of Allosteric Drug - Protein Binding by Biointeraction Chromatography  

Oleh:

Jianzhong Chen ; Hage, David S.

Jenis: Article from Journal - ilmiah internasional
Dalam koleksi: Nature Biotechnology: The Science and Business of Biotechnology vol. 22 no. 11 (Nov. 2004), page 1445-1448.
Topik: PROTEIN; quantitative analysis; allosteric drug proteion; biointeraction; chromatography

Ketersediaan

Perpustakaan Pusat (Semanggi) Nomor Panggil: NN9.3 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada

Lihat Detail Induk

Isi artikel

Allosteric interactions are important in many biological processes. They occur when the interactions of one substance with a binding agent changes the interactions of a second substance with the same agent at a separate site. Such interactions are often observed during the binding of drugs to blood proteins such as human serum albumin (HSA). Most previous studies of allosteric interactions have involved only qualitative observations of increased or decreased binding. In this study, we present an approach for quantitatively characterizing such allosteric effects using protein columns. The method is used to examine the interactions of ibuprofen / s-lorazepam acetate. S-oxazepam hemisuccinate / R-oxazepam hemisuccinate, and L-tryptophan / phenytoin during their binding to HSA. This approach can be applied to other receptors of biopolymers and can be used to independently examine the effects of two competing agents during an allosteric interaction.

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