Mix to validate: A facile, reversible pegylation for fast screening of potential therapeutic proteins in vivo

Tae Hyung Kim; Magdalena Swierczewska; Yumin Oh; Aeryon Kim; Dong Gyu Jo; Jae Hyung Park; Youngro Byun; Scheherazade Sadegh-Nasseri; Martin G. Pomper; Kang Choon Lee; Seulki Lee

doi:10.1002/anie.201302181

Mix to validate: A facile, reversible pegylation for fast screening of potential therapeutic proteins in vivo

Tae Hyung Kim
, Magdalena Swierczewska
, Yumin Oh
, Aeryon Kim
, Dong Gyu Jo
, Jae Hyung Park
, Youngro Byun
, Scheherazade Sadegh-Nasseri
, Martin G. Pomper
, Kang Choon Lee
, Seulki Lee

School of Medicine

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Happy TRAILs to you: PEGylation of proteins through complementary interactions between a His-tag and a Ni²⁺ 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.

Original language	English (US)
Pages (from-to)	6880-6884
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	52
Issue number	27
DOIs	https://doi.org/10.1002/anie.201302181
State	Published - Jul 1 2013

Keywords

PEGylation
drug screening
histidine tags
protein design
protein modifications

ASJC Scopus subject areas

Catalysis
General Chemistry

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10.1002/anie.201302181

Cite this

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title = "Mix to validate: A facile, reversible pegylation for fast screening of potential therapeutic proteins in vivo",

abstract = "Happy TRAILs to you: PEGylation of proteins through complementary interactions between a His-tag and a Ni2+ 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.",

keywords = "PEGylation, drug screening, histidine tags, protein design, protein modifications",

author = "Kim, \{Tae Hyung\} and Magdalena Swierczewska and Yumin Oh and Aeryon Kim and Jo, \{Dong Gyu\} and Park, \{Jae Hyung\} and Youngro Byun and Scheherazade Sadegh-Nasseri and Pomper, \{Martin G.\} and Lee, \{Kang Choon\} and Seulki Lee",

year = "2013",

month = jul,

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doi = "10.1002/anie.201302181",

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journal = "Angewandte Chemie - International Edition",

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T2 - A facile, reversible pegylation for fast screening of potential therapeutic proteins in vivo

AU - Kim, Tae Hyung

AU - Swierczewska, Magdalena

AU - Oh, Yumin

AU - Kim, Aeryon

AU - Jo, Dong Gyu

AU - Park, Jae Hyung

AU - Byun, Youngro

AU - Sadegh-Nasseri, Scheherazade

AU - Pomper, Martin G.

AU - Lee, Kang Choon

AU - Lee, Seulki

PY - 2013/7/1

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N2 - Happy TRAILs to you: PEGylation of proteins through complementary interactions between a His-tag and a Ni2+ 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.

AB - Happy TRAILs to you: PEGylation of proteins through complementary interactions between a His-tag and a Ni2+ 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.

KW - PEGylation

KW - drug screening

KW - histidine tags

KW - protein design

KW - protein modifications

UR - https://www.scopus.com/pages/publications/84879329492

UR - https://www.scopus.com/pages/publications/84879329492#tab=citedBy

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VL - 52

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 27

ER -

Mix to validate: A facile, reversible pegylation for fast screening of potential therapeutic proteins in vivo

Abstract

Keywords

ASJC Scopus subject areas

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