A generic approach to engineer antibody pH-switches using combinatorial histidine scanning libraries and yeast display-Reference-Cited by-同舟云学术

A generic approach to engineer antibody pH-switches using combinatorial histidine scanning libraries and yeast display

Published:2015-01-02 Issue:1 Volume:7 Page:138-151
ISSN:1942-0862
Container-title:mAbs
language:en
Short-container-title:mAbs

Author:

Schröter Christian¹²,Günther Ralf²,Rhiel Laura²,Becker Stefan²,Toleikis Lars²,Doerner Achim²,Becker Janine¹,Schönemann Andreas²,Nasu Daichi¹,Neuteboom Berend³,Kolmar Harald¹,Hock Björn²

Affiliation:

1. Institute for Organic Chemistry and Biochemistry; Technische Universität Darmstadt; Darmstadt, Germany

2. Protein Engineering and Antibody Technologies; Merck-Serono; Merck KGaA; Darmstadt, Germany

3. EMD Serono Research Center, Inc.; Billerica, MA USA

Publisher

Informa UK Limited

Subject

Immunology,Immunology and Allergy

Link

https://www.tandfonline.com/doi/pdf/10.4161/19420862.2014.985993

Reference51 articles.

1. Increasing Serum Half-life and Extending Cholesterol Lowering in Vivo by Engineering Antibody with pH-sensitive Binding to PCSK9

2. Design of pH Sensitive Binding Proteins from the Hyperthermophilic Sso7d Scaffold

3. Antibody recycling by engineered pH-dependent antigen binding improves the duration of antigen neutralization

4. Rational cytokine design for increased lifetime and enhanced potency using pH-activated “histidine switching”

5. Engineered protein A ligands, derived from a histidine-scanning library, facilitate the affinity purification of IgG under mild acidic conditions

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