Author(s):
Sambath Rajesh, Mani Akshaya, Babu Chandraja, Chandrasekar Anand, Gunasekaran Shoba, Rajendran Kumaran
Email(s):
kumaranwau@rediffmail.com
DOI:
10.52711/0974-360X.2026.00178 
Address:
Sambath Rajesh1, Mani Akshaya1, Babu Chandraja1, Chandrasekar Anand1, Gunasekaran Shoba2, Rajendran Kumaran1*
1Post Graduate and Research Department of Chemistry, Dwaraka Doss Goverdhan Doss Vaishnav College (Autonomous), Affiliated to University of Madras, E.V.R. Periyar Road, Arumbakkam, Chennai 600106, Tamil Nadu, India.
2Department of Biotechnology, Dwaraka Doss Goverdhan Doss Vaishnav College (Autonomous), Affiliated to University of Madras, E.V.R. Periyar Road, Arumbakkam, Chennai 600106, Tamil Nadu, India.
*Corresponding Author
Published In:
Volume - 19,
Issue - 3,
Year - 2026
ABSTRACT:
Binding studies of a globular protein, ßeta-Lactoglobin (ßlg) as the host with select antibiotics (guest) were explored by molecular docking methodology. The energetics of ßlg-antibiotics complexes were established from their free energy change (docking score) upon complex formation. The forces governing the relative stability of ßlg-guest complex were ascertained from the bimolecular interactions. The drugs employed were based on their inhibiting action on ßlg. Amoxicillin (AMX), cycloserine (CYC) metronidazole (MET) prontosil (PRO) and sulfanidazole (SUL) were docked with ßlg and their energetics were explored with highly competing guest molecule, dicyanomethylene (DCM) dye. The binding efficiency of ßlg-antibiotics complex is as AMX > PRO> SUL > MET > CYC. Interestingly, the docking score of ßlg-dye complex was energetically more favoured than drug-protein complex. Moreover, the simultaneous docking of the antibiotics destabilizes the ßlg-dye complex resulting in a lesser binding affinity. AMX and PRO drastically destabilises the ßlg-dye complex by 85% whereas MET and CYC results in decrease of 60%. However, when dye docked to protein bound to the drugs, an enhancement in the binding stability more than two-fold resulted. On the contrary, this phenomenon was not observed when antibiotics docked to dye-protein complex. The study explores the concept of binding stability of ßlg -guest versus ßlg-competing guest complexes through docking methods. Further, the role of polar / non-polar amino acids influencing the molecular interactions were analysed and explored in depth.
Cite this article:
Sambath Rajesh, Mani Akshaya, Babu Chandraja, Chandrasekar Anand, Gunasekaran Shoba, Rajendran Kumaran. Exploring the Energetics and Binding Stability of βeta-Lactoglobin(βlg)-Antibiotics Complexes with Competing Guest Molecule. Research Journal Pharmacy and Technology. 2026;19(3):1245-0. doi: 10.52711/0974-360X.2026.00178
Cite(Electronic):
Sambath Rajesh, Mani Akshaya, Babu Chandraja, Chandrasekar Anand, Gunasekaran Shoba, Rajendran Kumaran. Exploring the Energetics and Binding Stability of βeta-Lactoglobin(βlg)-Antibiotics Complexes with Competing Guest Molecule. Research Journal Pharmacy and Technology. 2026;19(3):1245-0. doi: 10.52711/0974-360X.2026.00178 Available on: https://www.rjptonline.org/AbstractView.aspx?PID=2026-19-3-39
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