Screening protein-ligand interactions using 1H NMR techniques for detecting the ligand

被引：12

作者：

Figueiredo, Isis Martins ^{[1
]}

Marsaioli, Anita Jocelyne ^{[1
]}

机构：

[1] Univ Estadual Campinas, Inst Quim, Dept Quim Organ, BR-13083970 Campinas, SP, Brazil

来源：

QUIMICA NOVA | 2007年 / 30卷 / 07期

关键词：

NMR; protein-ligand interactions; bovine serum albumin;

D O I：

10.1590/S0100-40422007000700019

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

NMR is a valuable screening tool for the binding of ligands to proteins providing structural information on both protein and ligands and is thus largely applied to drug-discovery. Among the recent NMR techniques to probe weak binding protein-ligand complexes we have critically evaluated the advantages and disadvantages of STD (Saturation Transfer Difference), WaterLOGSY (Water Ligand Observation with Gradient Spectroscopy), NOE pumping and DOSY-NOESY (Diffusion-Ordered NOESY) using a mixture of BSA (bovine serum albumin) plus salicylic acid, caffeine, citric acid, adipic acid and D-glucose.

引用

页码：1597 / 1605

页数：9

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