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Anal Chem. 2010 Sep 15;82(18):7736-43. doi: 10.1021/ac101586z.

Novel amidinating cross-linker for facilitating analyses of protein structures and interactions.

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  • 1Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.


A novel bifunctional thioimidate cross-linking reagent (diethyl suberthioimidate) that modifies amines without sacrificing their native basicity is developed. Intermolecular cross-linking of neurotensin and intramolecular cross-linking of cytochrome c under physiological conditions is investigated with this reagent. Because it does not perturb the electrostatic properties of a protein, it is unlikely to lead to artifactual conclusions about native protein structure. The interpeptide cross-links formed with this reagent are easily separated from other tryptic fragments using strong cation exchange chromatography, and they have a readily identified mass spectrometric signature. The use of this novel amidinating protein cross-linking reagent holds great promise for efficient, large-scale structural analysis of complex systems.

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