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Pseudodynamic Combinatorial Libraries: A Receptor‐Assisted Approach for Drug Discovery
Author(s) -
Corbett Andrew D.,
Cheeseman Jeremy D.,
Kazlauskas Romas J.,
Gleason James L.
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200453769
Subject(s) - dipeptide , combinatorial chemistry , protease , chemistry , yield (engineering) , hydrolysis , peptide synthesis , peptide , carbonic anhydrase , enzyme , peptide library , stereochemistry , biochemistry , computational biology , biology , peptide sequence , materials science , metallurgy , gene
Enzyme protection : An irreversible solid‐phase, aqueous peptide coupling resulted in the formation of a library of eight dipeptides, while an irreversible protease‐catalyzed hydrolysis destroyed them. Those dipeptides that bound to carbonic anhydrase were protected from destructions. Six cycles of active ester addition produced only the best‐binding dipeptide (>100:1) in 29 % yield.