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Application of Combinatorial Procedures in the Search for Serine‐Protease‐Like Activity with Focus on the Acyl Transfer Step
Author(s) -
De Muynck Hilde,
Madder Annemieke,
Farcy Nadia,
De Clercq Pierre J.,
PérezPayán M. Nieves,
Öhberg Liselotte M.,
Davis Anthony P.
Publication year - 2000
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/(sici)1521-3773(20000103)39:1<145::aid-anie145>3.0.co;2-j
Subject(s) - serine protease , protease , serine , cleavage (geology) , chemistry , combinatorial chemistry , peptide , proteases , stereochemistry , focus (optics) , biochemistry , computational biology , enzyme , biology , physics , paleontology , fracture (geology) , optics
Recursive deconvolution of a 729‐membered peptide library has identified three active sequences, in which both Ser and His are present in one of the two tripeptidic chains generated on a steroidal scaffold (see structural formula), for the cleavage of an activated p ‐nitrophenyl ester. This combinatorial approach aims at searching for serine‐protease‐like activity.