Bioactive compounds of Hemidesmis indices inhibit the acyl-homoserine lactone synthase

Authors

  • Clara Preethi Rodrigo Dept. of Microbiology, Kamaraj Women’s College, Thoothukudi. Tamil Nadu, India.
  • Kasi Murugan Dept. of Biotechnology, Manomaniam Sundarnar University, Tirunelveli, Tamil Nadu, India.

Abstract

AHL (acyl homoserine lactone) is a signaling molecule responsible for communication in gram negative bacteria, which is responsible for bacterial virulence as well as biofilm formation. The speedy growing in the number of resistant pathogenic bacteria takes controlled to a decrease in the efficacy of the existing antimicrobial agents. Acyl-homoserine lactone synthase plays an important role in the key molecules responsible for the formation of antibiotic resistance of gram-negative bacteria. The molecular docking studies performed by using molecular docking server online respectively in which the oral biofilm target namely N-acyl homoserine (ESAI) (PDB id: 1kzf) have a potential interaction with vanillin and Hexadeconoic acid. In this study, the protein N-acyl homoserine (ESAI) was used from its structure perspectives. The primary and secondary structures were calculated using online tools. Its role in oral biofilm was assessed by molecular docking the compounds present in the root extract of Hemidesmis indices assayed by GC-MS analysis. This in-silico study results throw light on how these active components of Hemidesmis indices are effective in oral biofilm. 

Keywords: Hemidesmis indices, Docking studies.  

Keywords:

Hemidesmis indices, Docking studies, acyl-homoserine lactone synthase

DOI

https://doi.org/10.22270/jddt.v15i4.7072

Author Biographies

Clara Preethi Rodrigo, Dept. of Microbiology, Kamaraj Women’s College, Thoothukudi. Tamil Nadu, India.

Dept. of Microbiology, Kamaraj Women’s College, Thoothukudi. Tamil Nadu, India.

Kasi Murugan , Dept. of Biotechnology, Manomaniam Sundarnar University, Tirunelveli, Tamil Nadu, India.

Dept. of Biotechnology, Manomaniam Sundarnar University, Tirunelveli, Tamil Nadu, India.

References

1. Lopez D, Vlamakis H & Kolter R, Biofilms, Cold Spring Harbor: Perspectives in Biology, 2009; 2 (3):370-378 https://doi.org/10.1101/cshperspect.a000398 PMid:20519345 PMCid:PMC2890205

2. Archer NK, Mazaitis MJ, Costerton JW, Leid JG, Powers ME, Shirtliff ME, Staphylococcus aureus biofilms: properties, regulation, and roles in human disease, Virulence, 2011; 2:445-459 https://doi.org/10.4161/viru.2.5.17724 PMid:21921685 PMCid:PMC3322633

3. Shweta N, Prakash SK, Dental abscess: A microbiological review, Dent Res J (Isfahan) 2013; 10:585-591

4.Joshi A, Lad H, Sharma H, Bhatnagar D, Evaluation of phytochemical composition and ant oxidative, hypoglycemic and hypolipodaemic properties of methanolic extract of Hemidesmus indicus roots in streptozotocin-induced diabetic mice, Clin PhytoSci, 2018; 4:7 https://doi.org/10.1186/s40816-018-0064-0

5. Nagarajan S, Rao LJ. Determination of 2-hydroxy-4-methoxybenzaldehyde in roots of Decalepis hamiltonii (Wight and arn) and Hemidesmus indicus R. Br, J AOAC Int, 2003; 86:564-567. https://doi.org/10.1093/jaoac/86.3.564 PMid:12852577

6. Arnold K, Boardoli L, Schwede T, The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling, Bioinformatics, 2006; 22:195-201 https://doi.org/10.1093/bioinformatics/bti770 PMid:16301204

7. Gill SC, Von Hippel PHH, Calculation of protein extinction coefficients from amino acid sequence data, Anal Biochem, 1989; 182: 319-326 https://doi.org/10.1016/0003-2697(89)90602-7 PMid:2610349

8. Bachmair A, Finley D, Varshavsky A, In-vivo-half-life of a protein is a function of its amino terminal residue, Science, 1986; 234:179-186 https://doi.org/10.1126/science.3018930 PMid:3018930

9. Gonad DK, Bachmir A, Wuning I, Tobias JW, Lane WS, Varshavsky AJ, University and structure of the N-end rule, J Biol Chem, 1989; 264:16700 16712 https://doi.org/10.1016/S0021-9258(19)84762-2 PMid:2506181

10. Tobias JW, Shrader TE, Rocap, Varshavsky A, The N-end rule in bacteria, Science 1991; 254:1374-1377 https://doi.org/10.1126/science.1962196 PMid:1962196

11. Ciechanover A, Schwartz AL, how are substrates recognized by the ubiquitin mediated proteolytic system, Trends Biochem, Sci, 1989; 14:483-488 https://doi.org/10.1016/0968-0004(89)90180-1 PMid:2696178

12. Ikai A, Thermostability and aliphatic index of globular proteins, J Biochem, 1980; 88: 1895-1898

13. Kyte J, Doolittle RF, a simple method for displaying the hydropathic character of a protein, J Mol Biol 1982; 157:105-132 https://doi.org/10.1016/0022-2836(82)90515-0 PMid:7108955

14. Comber C, Blanchet C, Geourijon C, Deleage G, NPS @ Network protein sequence Analysis, Trends Biochem Sci 2000; 25:147-150 https://doi.org/10.1016/S0968-0004(99)01540-6 PMid:10694887

15. Hirokawa T, Boon-chieng S, Mitaku S, SOSUI classification and secondary structure prediction system for membrane proteins, Bioinformatics, 1998; 14:378-379 https://doi.org/10.1093/bioinformatics/14.4.378 PMid:9632836

16. Ramachandran GN, Sasikharan V, Conformation of polypeptides and proteins, Adv Prot Chem, 1968; 23:283-437 https://doi.org/10.1016/S0065-3233(08)60402-7 PMid:4882249

17. Kiefer F, Arnold K, Kunzli M, Bordoli L, Schwede T, The SWISS-MODEL repository and associated resources, Nucleic Acids Res, 2009; 37: D387-D392 https://doi.org/10.1093/nar/gkn750 PMid:18931379 PMCid:PMC2686475

18. Lovell SC, Davis IW, Arendall B, De Bakker PIW, Word M, et al., Structure validation by Cά geometry: φ, ψ and Cβ deviation, Proteins: Struct Funct, Gen, 2002; 50:437-450 https://doi.org/10.1002/prot.10286 PMid:12557186

19. Laskowski FA, Fullmannn JA, Mac Arthur MW, Kaptein R, Thornton JM, AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR, J Biomol, NMR, 1996; 8:477-486 https://doi.org/10.1007/BF00228148 PMid:9008363

20. Vriend G, WHAT IF: A molecular modelling and drug design program, J Mol Graph, 1990; 8:52-56 https://doi.org/10.1016/0263-7855(90)80070-V PMid:2268628

21. Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, et al., Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function, J Comput Chem, 1998; 19(14):1639-1662 https://doi.org/10.1002/(SICI)1096-987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B

22.Mickymaray S, AI Aboody MS, Rath PK, Annamalai P, Nooruddin T, Screening and antibacterial efficacy of selected Indian medicinal plants, Asian Pac J Trop Biomed, 2016; 6:185-191 https://doi.org/10.1016/j.apjtb.2015.12.005

23. Bikadi Z, Demmko L, and Hazai E, Functional and structural characterization of a protein based on analysis of its hydrogen bonding plot, Arch. Biochem, Biophys, 2007; 461: 225-234 https://doi.org/10.1016/j.abb.2007.02.020 PMid:17391641

24. Garrett M. Morris, David S, Goodsell, Robert S. Halliday, Ruth Huey, William E. Hart, Richard K, Belew, Arthur J, Olson, Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. Journal of Computational Chemistry, 1998; 19(14):1639-1662 https://doi.org/10.1002/(SICI)1096-987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B

25. Solis FJ, and Wets RJB, Minimization of Random Search Techniques. Mathematics of Operations Research, 1981; 6(1): 19-30 https://doi.org/10.1287/moor.6.1.19

26. Inbathamizh L, Padmini E, In-Silico studies on the inhibitory effects of calcitriol and 5,5'-dithiobis-2-nitrobenzoic acid on human glucosaminyl n-acetyl transferase 1 activity, Asian J Exp, Biol Sci, 2021; 3(1):4-21

Published

15-04-2025
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How to Cite

1.
Rodrigo CP, Murugan K. Bioactive compounds of Hemidesmis indices inhibit the acyl-homoserine lactone synthase. J. Drug Delivery Ther. [Internet]. 2025 Apr. 15 [cited 2025 Apr. 26];15(4):72-9. Available from: https://jddtonline.info/index.php/jddt/article/view/7072

How to Cite

1.
Rodrigo CP, Murugan K. Bioactive compounds of Hemidesmis indices inhibit the acyl-homoserine lactone synthase. J. Drug Delivery Ther. [Internet]. 2025 Apr. 15 [cited 2025 Apr. 26];15(4):72-9. Available from: https://jddtonline.info/index.php/jddt/article/view/7072