title: Antibodies as specific chaperones.
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.
authors.affiliation: Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia.
authors.forename: D N
authors.initials: DN
authors.lastname: Ermolenko
authors.forename: A V
authors.initials: AV
authors.lastname: Zherdev
authors.forename: B B
authors.initials: BB
authors.lastname: Dzantiev
mesh_terms: D000818:Animals; D000906:Antibodies / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D002384:Catalysis; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D009113:Muramidase / Q000378:metabolism; D017510:Protein Folding
chemical_list: D000906:Antibodies; D018832:Molecular Chaperones; D009113:Muramidase