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Mix to Validate: A Facile, Reversible PEGylation for Fast Screening of Potential Therapeutic Proteins In Vivo
Author(s) -
Kim Tae Hyung,
Swierczewska Magdalena,
Oh Yumin,
Kim AeRyon,
Jo Dong Gyu,
Park Jae Hyung,
Byun Youngro,
SadeghNasseri Scheherazade,
Pomper Martin G.,
Lee Kang Choon,
Lee Seulki
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.201302181
Subject(s) - pegylation , nitrilotriacetic acid , in vivo , computer science , computational biology , chemistry , world wide web , biology , microbiology and biotechnology , organic chemistry , chelation
Happy TRAILs to you : PEGylation of proteins through complementary interactions between a His‐tag and a Ni 2+ complex of nitrilotriacetic acid (NTA, see picture), a well‐established practice in protein research, was used to improve the half‐life of therapeutic proteins in the blood following systemic administration in vivo. Animal models show that this site‐specific modification improves the efficacy of modified TRAIL proteins.