We performed a comparative analysis of biological activity of Lys-Glu peptide and its amino acid constituents. It was established that Lys-Glu stimulated proliferation of splenic cells in organotypic culture, while the mixture of glutamic acid and lysine inhibited culture growth. Using the method of molecular docking, we showed that glutamic acid, lysine, and Lys-Glu peptide can interact with different DNA sequences. The energy of interaction and the most beneficial localization of glutamic acid, lysine, and Lys-Glu peptide in DNA molecule was calculated. We demonstrated the interaction of the peptide and amino acids with DNA along the minor groove. The energy of DNA interaction with the peptide is higher than with individual amino acids. The peptide bonds increase the interaction of Lys-Glu peptide with DNA, which potentiates the biological effect on cell proliferation in organotypic culture of splenic cells.
Similar content being viewed by others
References
P. R. Gerber and K. Muller, J. Comput. Aided. Mol. Des., 9, No. 3, 251–268 (1995).
V. Kh. Khavinson, S. I. Tarnovskaya, N. S. Linkova, et al., Bull. Exp. Biol. Med., 154, No. 3, 403–410 (2013).
V. Khavinson, L. Shataeva, and A. Chernova, Neurosci. Endocrinol. Lett., 26, No. 3, 237–241 (2005).
V. Kh. Khavinson and V. N. Anisimov, Bull. Exp. Biol. Med., 148, No. 1, 94–98 (2009).
V. Kh. Khavinson, N. S. Linkova, V. E. Pronyaeva, et al., Bull. Exp. Biol. Med., 153, No. 5, 795–799 (2012).
V. Kh. Khavinson, I. S. Nikolsky, V. V. Nikolskaya, et al., Bull. Exp. Biol. Med., 151, No. 6, 722–725 (2011).
V. Kh. Khavinson, S. V. Serv, and V. G. Morozov, Pharmaceutical Dipeptide Compositions and Methods of Use Thereof, Patent US No. 6,139,862 from October 31, 2000.
V. Kh. Khavinson, N. M. Timofeeva, V. V. Malinin, et al., Bull. Exp. Biol. Med., 131, No. 6, 583–585 (2001).
V. Kh. Khavinson and V. V. Malinin, Gerontological Aspects of Genome Peptide Regulation, Basel (2005).
V. Kh. Khavinson, V. G. Morozov, V. V. Malinin, S. V. Sery, Use of a Dipeptide for Stimulating Repair Processes, European Patent No. 1089753 from June 23, 2003.
E. A. Koncevaya, N. S. Linkova, N. I. Chalizova, et al., Bull. Exp. Biol. Med., 153, No. 4, 573–576 (2012).
N. S. Lin’kova, V. O. Polyakova, A. V. Trofimov, et al., Bull. Exp. Biol. Med., 151, No. 2, 239–242 (2011).
Molecular Operating Environment; Chemical Computing Group Inc (2012) 1010 Sherbooke St. West, Suite #910, Montreal, QC, Canada, H3A 2R7, 2012.
T. Ya. Vakhitov, N. I. Chalisova, E. V. Polevaya, et al., Bull. Exp. Biol. Med., 3, No. 6, 596–600 (2013).
Author information
Authors and Affiliations
Corresponding author
Additional information
Translated from Kletochnye Tekhnologii v Biologii i Meditsine, No. 4, pp. 237–241, October, 2014
Rights and permissions
About this article
Cite this article
Khavinson, V.K., Tarnovskaya, S.I., Lin’kova, N.S. et al. Role of Peptide Bond in the Realization of Biological Activity of Short Peptides. Bull Exp Biol Med 158, 551–554 (2015). https://doi.org/10.1007/s10517-015-2805-0
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10517-015-2805-0