Functional Antibody CDR3 Fusion Proteins with Enhanced Pharmacological Properties | Zendy

Zhang Yong | Zendy; Wang Danling | Zendy; de Lichtervelde Lorenzo | Zendy; Sun Sophie B. | Zendy; Smider Vaughn V. | Zendy; Schultz Peter G. | Zendy; Wang Feng | Zendy

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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.

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