Development of a new approach for screening combinatorial libraries using XXXX .

@entity1522 @entity2101 @entity563 @entity15 @entity264
Mass spectrometric techniques play a prominent role in the rapidly expanding field of @entity2101 ( @entity2101 ). In this paper, the authors present a novel qualitative approach for the screening of a small library of compounds using @entity15 . Chymotrypsin (CT), a @entity563 protease, was selected as the target protein. A well-known inhibitor of CT is chymostatin (CS), a naturally occurring peptide @entity264 , which is reported to be a mixture of 3 components-A, B, and C-differing only in one of the @entity1522 . The authors report that native CS mixture consists of 3 additional ring hydroxylated components and that each compound exists in 2 epimeric forms. In case of protein-binding compounds, only 1 of the epimers was found to be active. A unique feature of this study is the generation of a combinatorial library of CS derivatives applying a one-pot strategy followed by identification and structural elucidation of the library components. Analytical investigation of the library resulted in the identification of 22 compounds. After incubation with CT and centrifugal ultrafiltration, 10 compounds were detected as protein-binding ligands. Finally, the complementary potentials of @entity15 in the screening of complex ligand mixtures have been discussed.
