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Molbank 2009, 2009(4), M642; doi:10.3390/M642
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1 and 1,2,*
1 Department of Biochemistry, University of Wisconsin–Madison, 433 Babcock Drive, Madison, WI 53706-1544, USA 2 Department of Chemistry, University of Wisconsin–Madison, 1101 University Avenue, Madison, WI 53706-1322, USA
* Author to whom correspondence should be addressed.
Received: 21 October 2009 / Accepted: 16 November 2009 / Published: 17 November 2009
Download PDF [144 KB, uploaded 17 November 2009]


Disulfide crosslinking of proteins is typically performed by treating proteins bearing cysteine residues with small-molecule disulfide reagents. The process results in the formation of a mixed disulfide intermediate, which then reacts with the cysteine residue of another protein molecule to form the crosslinked product. This second step requires the intimate association of two large reactants. The ensuing steric hindrance can result in poor crosslinking yields. Here, we introduce a bis(disulfide) reagent in which activated disulfides are separated by linkers that can alleviate steric hindrance and thereby potentially increase the efficiency of crosslinking.
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Kalia, J.; Raines, R.T. 1,9-Bis(2-pyridyl)-1,2,8,9-tetrathia-5-oxanonane. Molbank 2009, 2009, M642.

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