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https://doi.org/10.14300/mnnc.2017.12086

The prognosis and investigation of α-defensin-1 (HNP-1) influence on morphological changes of staphylococcus aureus cells by the atomic-force microscopy data

[Experimental medicine]
Vladimir Baturin; M. Selimov; Albert Bolatchiev; Vladimir Sadovoy; Roman Budkevich; Mariya Baturina;

Methods of computer chemistry were used to model the spatial structures of α-defensin-1 (human neutrophil peptide-1, HNP-1) and peptidoglycan molecules. Geometric optimization has been carried out, quantum-chemical characteristics and charge density distribution of the molecules have been studied, molecular docking has been car­ried out. Using high-resolution atomic-force microscopy, the influence of HNP-1 on the character of morphological changes in the cell wall of gram-positive microorganisms (Staphylococcus aureus) was studied. A pronounced dif­ference in the morphological features of bacterial populations is shown by the nature of the response to the action of HNP-1. Positively charged sites of HNP-1, binding to the negatively charged lipopolysaccharides (LPS) of the outer bacterial membrane, either create cracks in the LPS layer, or bind to sites in LPS that are responsible for interaction with the Ca2+ and Mg2+, cations necessary for stabilizing the cell surface.

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References:
1. Baturin V. A., Selimov M. A., Bolatchiev A. D., Budkevich R. O., Sadovoy V. V. [et al.] Study of cefotaxime influence on morphological changes in the cells of Staphylococcus aureus by atomic force microscopy. Medical news North Caucasus. 2017;12(1):36-40. doi: 10.14300/mnnc.2017.12010
2. Baturin V. A., Shchetinin Ye. V., Demidenko I. F., Korableva O. A. Byulleten antibiotikorezistentnosti respiratornykh patogenov v OITAR g. Stavropolya. Stavropol: StGMU, 2014.
3. Binnig G., Quate C. F. Atomic Force Microscope. Phys. Rev. Lett. 1986;56(9):930-933. doi: 10.1103/PhysRevLett.56.930
4. Finberg R. W., Moellering R. C., Tally F. P. [et al.] The Importance of Bactericidal Drugs: Future Directions in Infectious Disease. Clin. Infect. Dis. 2004;39(9):1314-1320. doi: 10.1086/425009
5. Kagan B. L., Selsted M. E., Ganz T., Lehrer R. I. Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes. Proc. Natl. Acad. Sci USA. 1990;87:210–214. doi:10.1073/pnas.87.1.210
6. Leeuw E. de, Li C., Zeng P., Li C., de Buin M. D., Lu W. Y., Breukink E., Lu W. Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II. FEBS Lett. 2010;584(8):1543-1548. doi:10.1016/j.febslet.2010.03.004
7. Leikina E., Delanoe-Ayari H., Melikov K., Cho M.-S., Chen A. [et al.] Carbohydrate-binding molecules inhibit viral fusion and entry by crosslinking membrane glycoproteins. Nat. Immunol. 2005;6(10):995-1001. doi:10.1038/ni1248
8. Martínez J. L., Baquero F. Emergence and spread of antibiotic resistance: setting a parameter space. Ups. J. Med. Sci. 2014;119(2):68-77. doi:10.3109/03009734.2014.901444
9. Mironov V. L. Osnovy skaniruyushchey zondovoy mikroskopii. N. Novgorod; 2004.
10. Nikiyan H., Vasilchenko A., Deryabin D. Humidity-Dependent Bacterial Cells Functional Morphometry Investigations Using Atomic Force Microscope. Int. J. Microbiol. 2010;2010:1-5. doi: 10.1155/2010/704170
11. Pazgier M., Li X., Lu W., Lubkowski J. Human Defensins: Synthesis and Structural Properties. Curr. Pharm. Des. 2007;13(30):3096-3118. doi: 10.2174/138161207782110381
12. Peters B. M., Shirtliff M. E., Jabra-Rizk M. A. Antimicrobial Peptides: Primeval Molecules or Future Drugs? PLoS Pathog. 2010;6(10):e1001067. doi: 10.1371/journal. ppat.1001067
13. Prakticheskoye rukovodstvo po antiinfektsionnoy khimioterapiii. pod red. L. S. Strachunskogo, Yu. B. Belousova, S. N. Kozlova. Smolensk: «MAKMAKh»; 2007.
14. Ratsionalnaya antimikrobnaya terapiya. pod red. S. V. Yakovleva. 2-e izd., pererab. i dop. M.: «Litterra»; 2015.
15. Sengupta D., Leontiadou H., Mark A. E., Marrink S. J. Toroidal pores formed by antimicrobial peptides show significant disorder. Biochim. Biophys. Acta –Biomembr. 2008;1778(10):2308-2317. doi: 10.1016/j.bbamem.2008.06.007
16. Sullivan C. J., Venkataraman S., Retterer S. T., Allison D. P., Doktycz M. J. Comparison of the indentation and elasticity of E. coli and its spheroplasts by AFM. Ultramicroscopy. 2007;107(10-11):934-942. doi:10.1016/j.ultramic.2007.04.017
17. Wang G. Human Antimicrobial Peptides and Proteins. Pharmaceuticals. 2014;7(5):545-594. doi: 10.3390/ph7050545

Keywords: defensin, HNP-1, antimicrobial peptide, antimicrobial resistance, molecular docking, atomic-force microscopy, Staphylococcus aureus