Streptavidin-mediated enrichment is a powerful strategy to identify biotinylated biomolecules and their interaction partners; however, intense streptavidin-derived peptides impede protein identification by mass spectrometry. Here, we present an approach to chemically modify streptavidin, thus rendering it resistant to proteolysis by trypsin and LysC. This modification results in over 100-fold reduction of streptavidin contamination and in better coverage of proteins interacting with various biotinylated bait molecules (DNA, protein, and lipid) in an overall simplified workflow.

中文翻译：

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耐蛋白酶的链霉亲和素，用于相互作用蛋白质组学。

链霉亲和素介导的富集是鉴定生物素化生物分子及其相互作用伙伴的有力策略。但是，强烈的链霉亲和素衍生肽会阻碍质谱鉴定蛋白质。在这里，我们提出一种化学修饰链霉亲和素的方法，从而使其对胰蛋白酶和LysC的蛋白水解具有抗性。这种修饰可以在整个简化的工作流程中将链霉亲和素污染减少100倍以上，并更好地覆盖与各种生物素化诱饵分子（DNA，蛋白质和脂质）相互作用的蛋白质。