Analysis of complex formation of human recombinant hsp70 with tumor-associated peptides

Chernikov V.A.1 , Gorokhovets N.V.2, Savvateeva L.V.2, Severin S.E.3

1. Research Institute of Uronephrology and Reproductive Health care, I.M. Sechenov First Moscow State Medical University
2. National Research Centre "Kurchatov Institute" Research Institute of Molecular Medicine of the I. M. Sechenov First MSMU
3. National Research Centre "Kurchatov Institute" Moscow, Russia Biochemisry Department, I.M. Sechenov First Moscow State Medical University
Section: Experimental/Clinical Study
DOI: 10.18097/pbmc20125806651      PubMed Id: 23350197
Year: 2012  Volume: 58  Issue: 6  Pages: 651-661
Molecular chaperones of HSP70 family assists presentation of exogenous antigenic peptides by antigen-presenting cells (APC). HSP70-peptide complexes are powerful immunotherapeutic agents, which enhance cross-presentation of captured antigen in dendritic cells and macrophages. Several clinical trials have shown that HSP-based cancer vaccines possess good efficacy and safety. However, sometime it is impossible to isolate sufficient amount of vaccine. These make us to pay attention for recombinant HSP70-based vaccines and to optimize in vitro complex formation mechanism. Here we have investigated two human recombinant proteins HSP70HYB and HSC70. Optimal values of ADP concentration, pH, temperature and peptides excess are determined in this work. We have also shown that proposed complex formation method enriches eluted from HSP70-complexes peptide repertoire compared to in vivo assembled ones.
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Keywords: heat shock proteins, HSP70, tumor-associated antigenic peptide, peptide binding

Chernikov, V. A., Gorokhovets, N. V., Savvateeva, L. V., Severin, S. E. (2012). Analysis of complex formation of human recombinant hsp70 with tumor-associated peptides. Biomeditsinskaya khimiya, 58(6), 651-661.
This paper is also available as the English translation: 10.1134/S1990750813020054
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