Alternative Affinity Ligands for Immunoglobulins

The demand for recombinant therapeutic antibodies and Fc-fusion proteins is expected to increase in the years to come. Hence, extensive efforts are concentrated on improving the downstream processing. In particular, the development of better-affinity chromatography matrices, supporting robust time-...

Full description

Saved in:
Bibliographic Details
Published in:Bioconjugate chemistry 2017-08, Vol.28 (8), p.2009-2030
Main Authors: Kruljec, Nika, Bratkovič, Tomaž
Format: Article
Language:English
Subjects:
Affinity
Affinity chromatography
Amino Acid Sequence
Animals
Antibodies
Aptamers
Bacteria
Binding
Chromatography
Combinatorial analysis
Combinatorial libraries
Drug Design
Fc receptors
High-throughput screening
Humans
Immunoglobulins
Immunoglobulins - chemistry
Immunoglobulins - immunology
Immunoglobulins - metabolism
Libraries
Ligands
Peptides
Protein Engineering
Proteins
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The demand for recombinant therapeutic antibodies and Fc-fusion proteins is expected to increase in the years to come. Hence, extensive efforts are concentrated on improving the downstream processing. In particular, the development of better-affinity chromatography matrices, supporting robust time- and cost-effective antibody purification, is warranted. With the advances in molecular design and high-throughput screening approaches from chemical and biological combinatorial libraries, novel affinity ligands representing alternatives to bacterial immunoglobulin (Ig)-binding proteins have entered the scene. Here, we review the design, development, and properties of diverse classes of alternative antibody-binding ligands, ranging from engineered versions of Ig-binding proteins, to artificial binding proteins, peptides, aptamers, and synthetic small-molecular-weight compounds. We also provide examples of applications for the novel affinity matrices in chromatography and beyond.
ISSN:1043-1802
1520-4812
DOI:10.1021/acs.bioconjchem.7b00335