| Research Abstract |
Since there is no strict linear relationship between genome and proteome, proteomics is desirable to address protein networks. Until recently, proteomics was almost synonymous with the mapping of denatured proteins by two-dimensional gel electrophoresis. However, the major question about protein functions is how they interact with their partners. Thus, affinity-based methods have become increasingly appreciated as the approach of chemical genomics for sorting proteins based on their functions.
Photoaffinity methods introduces a cross-link between a ligand and its specific receptor for probing their affinity correlation through a covalent bond, which enables the direct identification of target proteins as well as ligand binding domains. ^<1)>Because the proteomics of is the extensive study of proteins, it is clear that conventional photoaffinity methods are required to increase in the throughput throughout the analytical steps. We firstly developed efficient methods for tethering photoreactive diazirine to various biological ligands. The method significantly increases the synthetic routine in the preparation of various photoreactive derivatives of important biological ligands such as DNA,RNA,carbohydretes, peptides, and proteins. Analogous to DNA technologies, protein chips and protein arrays serve an efficient device for the Screening of samples in a massively parallel fashion. Thus, we secondly developed a rapid and sensitive photoaffinity device for capturing ligand-receptor pair on a solid matrix. The technique based on surface plasmon resonance spectroscopy was developed for the real-time analysis of ligand-receptor interaction. In contrast to this, the photoaffinity device provides a rapid method for the isolation of target proteins, which enables the high-throughput mass spectrometric analysis for the identification of targets as well as their functional sites.
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