Synthesis, characterization, anticancer activity, optical spectroscopic and docking studies of novel thiophene-2-carboxaldehyde derivatives

Shareef, Mohamed Ahadu; Musthafa, Mohamed Saiyad; Velmurugan, D.; Karthikeyan, S.; Ganesan, Singaravelu; Padusha, Syed Ali; Musthafa, Saiyad; Mohamed, J.Madhavan M. Gulam

doi:10.5155/eurjchem.7.4.454-462.1505

Cited by 1 publication

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“… Where, F 0 and F are the initial and final fluorescence intensities of the BSA– and HAG–NANA complexes, K b is the binding constant, and n is the binding sites of the protein–drug complex. Also, the free energy changes Δ G ° for the protein–drug complex were calculated using eq . Where, T is the temperature (298, 300, and 304 K), R is the gas constant (1.987 cal mol –1 K –1 ), enthalpy is Δ H °, entropy is Δ S °, free energy is Δ G °, and K b is the binding constant of BSA– and HAG–NANA complexes. − …”

Section: Methodsmentioning

confidence: 99%

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

Karthikeyan

Bharanidharan

Ragavan

et al. 2018

J. Chem. Inf. Model.

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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.

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