文摘
Posttranslational modification (PTM) of proteins is likelyto be the most common mechanism of altering theexpression of genetic information. It is essential to characterize PTMs to establish a complete understanding ofthe activities of proteins. Here, we present a sensitivedetection method using surface-enhanced Raman spectroscopy (SERS) that can detect PTMs from as little aszeptomoles of peptide. We demonstrate, using modelpeptides, the ability of SERS to detect a variety of proteinmodifications, such as acetylation, trimethylation, phosphorylation, and ubiquitination. In addition, we show thecapability to obtain positional information for modifications such as trimethylation and phosphorylation usingSERS and wavelet decomposition data analysis techniques. We further show that it is possible to apply SERSto detect PTMs from biological samples such as histones.We envision that this detection method might be avaluable technique that is complementary to mass spectrometry in obtaining orthogonal chemical and modification-specific information from biological samples at sensitive levels.