Comparative Binding Analysis of N-Acetylneuraminic Acid in Bovine Serum Albumin and Human α-1 Acid Glycoprotein
| Autor: | Ganesan Bharanidharan, Rajendiran Mangaiyarkarasi, Singaravelu Ganesan, Shanmugavel Chinnathambi, Saravanan Kandasamy, Subramani Karthikeyan, Prakasarao Aruna, Anandh Sundaramoorthy, Sriram Ragavan, Kanniyappan Udayakumar |
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| Rok vydání: | 2018 |
| Předmět: |
Circular dichroism
Protein Conformation General Chemical Engineering Static Electricity Serum albumin Plasma protein binding Library and Information Sciences 01 natural sciences chemistry.chemical_compound Protein structure 0103 physical sciences Static electricity Animals Humans Bovine serum albumin Density Functional Theory 010304 chemical physics biology Serum Albumin Bovine Orosomucoid General Chemistry N-Acetylneuraminic Acid 0104 chemical sciences Computer Science Applications Molecular Docking Simulation 010404 medicinal & biomolecular chemistry Förster resonance energy transfer chemistry biology.protein Biophysics Cattle N-Acetylneuraminic acid Protein Binding |
| Zdroj: | Journal of Chemical Information and Modeling. 59:326-338 |
| ISSN: | 1549-960X 1549-9596 |
| DOI: | 10.1021/acs.jcim.8b00558 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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