Comparative Binding Analysis of N-Acetylneuraminic Acid in Bovine Serum Albumin and Human α-1 Acid Glycoprotein

The present study focuses on the determination of the biologically significant N-acetylneuraminic acid (NANA) drug binding interaction mechanism between bovine serum albumin (BSA) and human α-1 acid glycoprotein (HAG) using various optical spectroscopy and computational methods. The steady state fluorescence spectroscopy result suggests that the fluorescence intensity of BSA and HAG was quenched by NANA in a static mode of quenching. Further time-resolved emission spectroscopy measurements confirm that mode of quenching mechanism of NANA in the BSA and HAG system. The FT-IR, excitation-emission matrix and circular dichroism (CD) analysis confirms the presence of NANA in the HAG, BSA system, and fluorescence resonance energy transfer analysis shows that NANA transfers energy between the HAG and BSA system. The molecular docking result shows good binding affinity in both protein complexes, and further molecular dynamics simulations and charge distribution analysis were performed to gain more insight into the binding interaction mechanism of NANA in the HAG and BSA complex. © 2018 American Chemical Society.

Karthikeyan S. 1, 2 , Bharanidharan G.1 , Ragavan S.3 , Kandasamy S.4 , Chinnathambi S.5 , Udayakumar K.6 , Mangaiyarkarasi R.1 , Sundaramoorthy A.1 , Aruna P.1 , Ganesan S.1
American Chemical Society
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  • 1 Department of Medical Physics, Anna University, Chennai, 600 025, India
  • 2 Department of Organic Chemistry, Science Faculty, Peoples' Friendship University of Russia, RUDN University, MikluhoMaklaya St., 6, Moscow, 117198, Russian Federation
  • 3 Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Chennai, 600 025, India
  • 4 Department of Physics, Periyar University, Salem, 636 011, India
  • 5 International Center for Young Scientists, National Institute for Materials Science (NIMS), 1-2-1 Sengen, Tsukuba, Ibaraki, 305-0047, Japan
  • 6 Postdoctoral Research Fellow, University of Montreal, Saint, Justine Hospital University Center, 3175 Cote Sainte-Catherine, Montreal, QC H3T1C5, Canada
Body fluids; Dichroism; Emission spectroscopy; Energy transfer; Fluorescence; Fluorescence spectroscopy; Glycoproteins; Mammals; Molecular dynamics; Quenching; Spectrum analysis; Surface plasmon resonance; Alpha-1-acid glycoprotein; Excitation emission matrices; Fluorescence intensities; Fluorescence resonance energy transfer analysis; Molecular dynamics simulations; N-acetylneuraminic acid; Steady state fluorescences; Time-resolved emission spectroscopy; Binding energy
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