Caught in action: selecting peptide aptamers against intrinsically disordered proteins in live cells.

ABSTRACT: Intrinsically disordered proteins (IDPs) or unstructured segments within proteins play an important role in cellular physiology and pathology. Low cellular concentration, multiple binding partners, frequent post-translational modifications and the presence of multiple conformations make it difficult to characterize IDP interactions in intact cells. We used peptide aptamers selected by using the yeast-two-hybrid scheme and in-cell NMR to identify high affinity binders to transiently structured IDP and unstructured segments at atomic resolution. Since both the selection and characterization of peptide aptamers take place inside the cell, only physiologically relevant conformations of IDPs are targeted. The method is validated by using peptide aptamers selected against the prokaryotic ubiquit

SUBMITTER: Cobbert JD 

PROVIDER: S-EPMC4371151 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature