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Updated: Aug 20, 2026

Studying Protein Function and the Role of Altered Protein Expression by Antibody Interference and Three-dimensional Reconstructions
Published on: April 21, 2016
Antibodies as specific chaperones
D N Ermolenko1, A V Zherdev, B B Dzantiev
1Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia.
Abstract:
Protein folding is often accompanied by formation of non-native conformations leading to protein aggregation. A number of reports indicate that antibodies can facilitate folding and prevent aggregation of protein antigens. The influence of antibodies on folding is strictly antigen specific. Chaperone-like antibody activity may be due to the stabilization of native antigen conformations or folding transition states, or screening of aggregating hydrophobic surfaces. Taking advantage of chaperone-like activity of antibodies for immunotherapy may prove to be a promising approach to the treatment of Alzheimer's and prion-related diseases. Antibody-assisted folding may enhance renaturation of recombinant proteins from inclusion bodies.
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