Abstract
Molecular chaperones serve to prevent protein misfolding and aggregation in the cell. Chaperones act by binding transiently to exposed hydrophobic surfaces in target proteins in a manner that is regulated by ATP-induced conformational changes. Some molecular chaperones(heat-shock proteins, HSP) are peptide-binding proteins such as antigenic peptides that are generated within cells. Molecular chaperons play very important role in antigen presentation and cross-presentation. The immunological properties enable them to be used in new immunotherapies of cancers and infections. Chaperone can prevent the deposition of amyloid aggregates that induce Alzheimer's or Huntington disease. In biotechnology, there is much interest in producing large amounts of biologically active recombinant proteins. In many cases, however, problems such as formation of insoluble inclusion bodies are encountered. To overcome this problem, molecular chaperon and artificial molecular chaperone are used in vitro as refolding aids of proteins. In this paper, we summarized the function of molecular chaperones and application to biotechnology and medicine. Artificial molecular chaperones are also discussed.
