Publication:
Binding interaction of potent HIV-1 NNRTIs, amino-oxy-diarylquinoline with the transport protein using spectroscopic and molecular docking

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Issued Date

2020

Resource Type

Article

File Type

application/pdf

ISSN

13861425

DOI

10.1016/j.saa.2020.118159

Other identifier(s)

2-s2.0-85080072589

Rights Holder(s)

Scopus

Bibliographic Citation

Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. Vol 233, (2020)

Suggested Citation

Patnin S., Makarasen A., Kuno M., Deeyohe S., Techasakul S., Chaivisuthangkura A. Binding interaction of potent HIV-1 NNRTIs, amino-oxy-diarylquinoline with the transport protein using spectroscopic and molecular docking. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. Vol 233, (2020). doi:10.1016/j.saa.2020.118159 Retrieved from: https://hdl.handle.net/20.500.14740/4528

Title

Binding interaction of potent HIV-1 NNRTIs, amino-oxy-diarylquinoline with the transport protein using spectroscopic and molecular docking

Author(s)

Patnin S.
 Makarasen A.
 Kuno M.
 Deeyohe S.
 Techasakul S.
 Chaivisuthangkura A.

Abstract

In the present investigation, the intermolecular interaction of 4-(4′-cyanophenoxy)-2-(4′′-cyanophenyl)-aminoquinoline (1), a potent non-nucleoside HIV-1 reverse transcriptase inhibitors, with the transport proteins, namely bovine serum albumin (BSA) and human serum albumin (HSA), has been investigated under physiological conditions employing UV–Vis, fluorescence spectrophotometry, competitive binding experiments and molecular docking methods. The results indicated that binding of (1) to the transport proteins caused fluorescence quenching though a static quenching mechanism. The number of binding site (n) and the apparent binding constant (Kb) between (1) and the transport proteins were determined to be about 1 and 104–105 L·mol−1 (at three different temperatures; 298, 308, 318 K), respectively. The interaction of (1) upon binding to the transport proteins was spontaneous. The enthalpic change (ΔH°) and the entropic change (ΔS°) were calculated to be −56.50 kJ·mol−1, −72.31 J·mol−1 K−1 for (1)/BSA, respectively and computed to be −49.35 kJ·mol−1, −58.64 J·mol−1 K−1, respectively for (1)/HSA, respectively. The results implied that the process of interaction force of (1) with the transport protein were Vander Waals force and/or hydrogen bonding interactions. The site maker competitive experiments revealed that the binding site of (1) with the transport proteins were mainly located within site I (sub-domain IIA) in both proteins. Additionally, the molecular docking experiment supported the above results which confirmed the binding interaction between (1) and the transport proteins. This study will come up with basic data for explicating the binding mechanisms of (1) with the transport protein and can be great significance in the opening to clarify the transport process of (1) in vivo. © 2020 Elsevier B.V.

Subject(s)

Binding energy
 Diseases
 Fluorescence
 Fluorescence spectroscopy
 Hydrogen bonds
 Mammals
 Molecular modeling
 Quenching
 Spectrophotometry
 Fluorescence spectrophotometry
 HIV-1 reverse transcriptase
 Hydrogen bonding interactions
 Intermolecular interactions
 Molecular docking
 NNRTIs
 Serum albumin
 VIS spectrophotometry
 Proteins
 Bovine serum albumin
 Human serum albumin
 RNA directed DNA polymerase inhibitor
 Animal
 Binding site
 Bovine
 Chemistry
 Human
 Human immunodeficiency virus 1
 Molecular docking
 Ultraviolet spectrophotometry
 Animals
 Binding Sites
 Cattle
 HIV-1
 Humans
 Molecular Docking Simulation
 Reverse Transcriptase Inhibitors
 Serum Albumin, Bovine
 Serum Albumin, Human
 Spectrophotometry, Ultraviolet

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URI

https://hdl.handle.net/20.500.14740/4528

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Scopus: Year 1983-2021

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