title: The interaction of beta-lactoglobulin with ciprofloxacin and kanamycin; a spectroscopic and molecular modeling approach.
abstract: A vast research has been conducted to find suitable and safe carriers for vital and pH-sensitive drugs including antibiotics. This article reports the use of easily accessible and abundant purified beta-lactoglobulin (β-LG) protein as the potential carrier of widely used Kanamycin (Kana) and Ciprofloxacin (Cip) antibiotics. Spectroscopic techniques (Fluorescence, UV-vis, Circular Dichroism) combined with molecular docking were used to determine the binding mechanism of these drugs. Fluorescence studies showed moderate binding affinity with the calculated binding constants KCip= 60.1 (±0.2) × 103M-1and Kkana= 2.5 (±0.6) × 103M-1with the order of Cip > Kana. Results of UV-vis were consistent with fluorescence measurements and demonstrated a stronger complexation for Cip rather than Kana. The secondary structure of β-LG was preserved upon interaction with Kana; however, a reduction in β-sheet content from 39.1 to 31.9% was convoyed with an increase in α-helix from 12.8 to 20.5% due to complexation of Cip. Molecular docking studies demonstrated that preferred binding sites of these drugs are not the same and several amino acids are involved in stabilizing the interaction. Based on the achieved results, Kana and Cip can spontaneously bind to β-LG and this protein may serve as their transport vehicle.
authors: a Pharmaceutical Sciences Research Center, School of Pharmacy , Shiraz University of Medical Sciences , Shiraz , Iran.|b Genetics Division, Biology Department , Faculty of Sciences , University of Isfahan , Isfahan , Iran.
authors: Mohammad Hossein
authors: MH
authors: Mehraban
authors: a Pharmaceutical Sciences Research Center, School of Pharmacy , Shiraz University of Medical Sciences , Shiraz , Iran.|c Department of Biology, Faculty of Sciences , University of Isfahan , Isfahan , Iran.
authors: Salman
authors: S
authors: Odooli
authors: d Protein Chemistry Laboratory (PCL), Department of Biology , College of Sciences, Shiraz University , Shiraz , Iran.
authors: Reza
authors: R
authors: Yousefi
authors: c Department of Biology, Faculty of Sciences , University of Isfahan , Isfahan , Iran.
authors: Rasoul
authors: R
authors: Roghanian
authors: b Genetics Division, Biology Department , Faculty of Sciences , University of Isfahan , Isfahan , Iran.
authors: Majid
authors: M
authors: Motovali-Bashi
authors: e Institute of Biochemistry and Biophysics (IBB) , University of Tehran , Tehran , Iran.
authors: Ali-Akbar
authors: AA
authors: Moosavi-Movahedi
authors: a Pharmaceutical Sciences Research Center, School of Pharmacy , Shiraz University of Medical Sciences , Shiraz , Iran.|f Department of Pharmaceutical Biotechnology , School of Pharmacy, Shiraz University of Medical Sciences , Shiraz , Iran.
authors: Younes
authors: Y
authors: Ghasemi
mesh_terms: D001665:Binding Sites / Q000187:drug effects; D002939:Ciprofloxacin / Q000737:chemistry* / Q000627:therapeutic use; D016503:Drug Delivery Systems; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007612:Kanamycin / Q000737:chemistry* / Q000627:therapeutic use; D007782:Lactoglobulins / Q000737:chemistry* / Q000627:therapeutic use; D062105:Molecular Docking Simulation; D011485:Protein Binding / Q000187:drug effects
chemical_list: D007782:Lactoglobulins; D007612:Kanamycin; D002939:Ciprofloxacin
keywords: CD; UV–vis spectroscopy; antibiotics delivery; fluorescence quenching; β-lactoglobulin