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Article

Aggregation-resistant domain antibodies engineered with charged mutations near the edges of the complementarity-determining regions.

Protein engineering, design & selection : PEDS - 1 Oct 2012

Perchiacca Joseph M, Ladiwala Ali Reza A, Bhattacharya Moumita, Tessier Peter M

Abstract excerpt

Antibodies commonly contain hydrophobic residues within their complementarity-determining regions (CDRs) that mediate binding to target antigens. Unfortunately, hydrophobic CDRs can also promote antibody aggregation, which is especially concerning for therapeutic antibodies due to the immunogenicity of antibody aggregates. Here we investigate how the sequences of CDRs within single-domain (V(H)) antibodies...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22843678
DOI: 10.1093/protein/gzs042

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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