Premium
Functional Antibody CDR3 Fusion Proteins with Enhanced Pharmacological Properties
Author(s) -
Zhang Yong,
Wang Danling,
de Lichtervelde Lorenzo,
Sun Sophie B.,
Smider Vaughn V.,
Schultz Peter G.,
Wang Feng
Publication year - 2013
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.201303656
Subject(s) - antiparallel (mathematics) , computational biology , computer science , fusion protein , immunoglobulin domain , disulfide bond , antibody , chemistry , biology , biochemistry , gene , genetics , recombinant dna , physics , quantum mechanics , magnetic field
Real staying power : A subset of bovine antibodies (blue, see scheme) feature an ultralong CDR3 loop that forms an antiparallel β‐sheet stalk, terminating in a folded, disulfide cross‐linked knob domain. Fusion of a polypeptide (red) into this unique CDR3 motif provides a novel strategy for generating polypeptide therapeutics with enhanced pharmacokinetics and pharmacodynamics.