Simple approach to assign disulfide connectivity using extracted ion chromatograms of electron transfer dissociation spectra.

ABSTRACT: Increasing interest in production of protein-based pharmaceuticals (biotherapeutics) is accompanied by an increased need for verification of protein folding and correct disulfide bonding. Recombinant protein expression may produce aberrant disulfide bonds and could result in safety concerns or decreased efficacy. Thus, the thorough analysis of disulfide bonding is a necessity for protein therapeutics. The use of electron transfer dissociation (ETD) facilitates this analysis because disulfide bonds are preferentially cleaved when subjected to ETD. Here, we make use of this well-characterized reaction to assign disulfide bonding networks by coupling the use of extracted ion chromatograms (XICs) of cysteine-containing peptides with ETD analysis to produce an efficient assignment approach for

SUBMITTER: Clark DF 

PROVIDER: S-EPMC3607449 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature