期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 134, 期 9, 页码 4057-4059出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja211931f
关键词
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资金
- NIH [T32 GM008688, R01 GM044783]
- American Heart Association [09PRE2260125]
Dithiothreitol (DTT) is the standard reagent for reducing disulfide bonds between and within biological molecules. At neutral pH, however, >99% of DTT thiol groups are protonated and thus unreactive. Herein, we report on (2S)-2-amino-1,4-dimercaptobutane (dithiobutylamine or DTBA), a dithiol that can be synthesized from L-aspartic acid in a few high-yielding steps that are amenable to a large-scale process. DTBA has thiol pK(a) values that are similar to 1 unit lower than those of DTT and forms a disulfide with a similar E degrees' value. DTBA reduces disulfide bonds in both small molecules and proteins faster than does DTT. The amino group of DTBA enables its isolation by cation-exchange and facilitates its conjugation. These attributes indicate that DTBA is a superior reagent for reducing disulfide bonds in aqueous solution.
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