首页 | 本学科首页   官方微博 | 高级检索  
     


Antibodies as specific chaperones
Authors:D.?N.?Ermolenko,A.?V.?Zherdev,B.?B.?Dzantiev  author-information"  >  author-information__contact u-icon-before"  >  mailto:dzantiev@inbi.ras.ru"   title="  dzantiev@inbi.ras.ru"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author
Affiliation:(1) Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071 Moscow, 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 Alzheimerrsquos and prion-related diseases. Antibody-assisted folding may enhance renaturation of recombinant proteins from inclusion bodies.Translated from Biokhimiya, Vol. 69, No. 11, 2004, pp. 1515–1521.Original Russian Text Copyright © 2004 by Ermolenko, Zherdev, Dzantiev.
Keywords:antibodies  protein aggregation  folding  chaperones  inclusion bodies
本文献已被 PubMed SpringerLink 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号