A mass spectrometry screening method for antiaggregatory activity of proteins covalently modified by combinatorial library members: application to sickle hemoglobin.
A mass spectrometry screening method for antiaggregatory activity of proteins covalently modified by combinatorial library members: application to sickle hemoglobin.
复制标题
组合文库成员共价修饰的蛋白质抗聚集活性的质谱筛选方法：应用于镰状血红蛋白。
DOI：
10.1021/cc9900798
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
Venton,DL
中科院分区：
文献类型：
--
作者：
Park,S;Wanna,L;Johnson,ME;Venton,DL
A homogeneous assay, based on electrospray mass spectrometry, is described for identifying compounds in a combinatorial library that covalently modify a protein and thereby enhance its solubility. The technique is based on measuring the distribution of modified proteins in the supernatant versus aggregate. Compounds having the greatest anti-aggregatory activity are those with the highest supernatant/aggregate ratio. Mass is used as a marker to identify which covalent modifier in the library is involved. An exploratory study is presented which demonstrates that the antisickling activity of a family of isothiocyanates, as measured by the standard Csatassay, correlates well (r2= 0.98) with the mass spectrometry analysis of the supernatant/aggregate distribution. The technique has potential for screening libraries capable of covalently modifying other proteins of clinical interest, e.g., Alzheimer's, Huntington's, and various prion related diseases.
