Premium
all‐ D ‐Polypeptides: Novel Targets for Semisynthesis
Author(s) -
Wehofsky Nicole,
Thust Sven,
Burmeister Jens,
Klussmann Sven,
Bordusa Frank
Publication year - 2003
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.200390187
Subject(s) - semisynthesis , chemistry , proteases , cleavage (geology) , biocatalysis , biochemistry , enzyme , thermostability , stereochemistry , combinatorial chemistry , biology , catalysis , reaction mechanism , paleontology , fracture (geology)
The chemoenzymatic synthesis of all‐ D ‐polypeptides such as the all‐ D version of the WW domain of hPin1 ( 1 ) was achieved by applying the substrate mimetics strategy and clostripain as the biocatalyst. Ironically all‐ D ‐peptides are better synthesis targets for proteases than their all‐ L analogues, although nature designed these enzymes for the cleavage of all‐ L ‐peptides.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom