Identification of aggregation inhibitors of the human antibody light chain repertoire by phage display.

Publication Type:
Journal Article
Citation:
Protein engineering, design & selection : PEDS, 2014, 27 (10), pp. 405 - 409
Issue Date:
2014-10
Full metadata record
Files in This Item:
Filename Description Size
Identification_of_aggregation_inhibitors_of_the_hu.pdfPublished Version574.74 kB
Adobe PDF
Protein aggregation hinders the development of biologics and underpins the molecular basis of many human diseases. Considerable variation of aggregation propensity exists not only between different proteins, but also within a single homologous family, which complicates analyses. A classic example is observed among human antibody light chains, which aggregate in a clonally specific manner, driven by sequence diversity within their variable domains. Here, we utilise a library versus library strategy, based on phage display and a chemical library of FDA approved drugs, to overcome this limitation. Our approach allowed the identification of small molecule drugs that inhibit the aggregation of the human light chain repertoire. It also provides a general template for the small molecule targeting of diverse protein families.
Please use this identifier to cite or link to this item: