Browsing by Author "Al Bratty, Mohammed"

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    Rapid Screening and Estimation of Binding Constants for Interactions of Fe3+ with Two Metalloproteins, Apotransferrin and Transferrin, Using Affinity Mode of Capillary Electrophoresis
    (Hindawi, 19/11/2021) Al Bratty, Mohammed; Alhazmi, Hassan A; Javed, Sadique A; Rehman, Zia Ur; Najmi, Asim; El-Sharkawy, Karam A
    e interaction behavior of Fe 3+ with transferrin and apotransferrin (iron-free form) was investigated in this study using affinity capillary electrophoresis. Change in the mass and charge of protein upon binding to the metal ion in the capillary tube led to variation in its migration time and was used to measure the noncovalent binding interactions by fast screening method. Acetanilide was used as the electroosmotic
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    Spectroscopic and in silico Approach to Probe the Binding Interactions of Irbesartan and Human Serum Albumin
    (Elsevier, 01/02/2022) Najmi, Asim; Al Bratty, Mohammed; Alhazmi, Hassan Ahmad; Thangavel, Neelaveni; Alam, Md Shamsher; Ahsan, Waquar; Javed, Sadique Akhtar; Arbab, Ismail Adam; El-Sharkawy, Karam Ahmed
    Objective: The free and active concentration of drugs and thereby their pharmacokinetic properties are controlled by their binding to human serum albumin (HSA) protein. Irbesartan (IRB), an antihypertensive drug was aimed to be investigated in terms of its binding interactions with the different sites of HSA using in silico molecular docking technique along with the commonly employed spectroscopic techniques. Methods: Using FT-IR spectroscopy, the spectral shifting and intensity variations before and after complexation with IRB were studied for amide A, amide-I as well as amide-II of HSA. The absorbance of HSA with and without increasing concentrations of IRB was studied at 280 nm and the binding constant was determined using UV-spectroscopy. Molecular docking study was performed, and the types of interactions were predicted. Results: The IR spectra of IRB-HSA complex showed reductions in the intensities of amide-I and II bands as well as marked reduction in the α-helix content of HSA. The absorbance of HSA protein increased with increasing concentrations of drug. A binding constant value of 5.64 × 104 M-1 was calculated indicating good interaction. Molecular docking studies showed that IRB interacts more effectively with site-I of HSA through greater number of hydrogen bonds and strong π–charge (electrostatic) interactions than with site-II. Conclusions: The spectroscopic and molecular docking techniques proved to be effective tools to study the drug-protein interaction which provided accurate results as evident from these studies. Studying drug-albumin interaction is of utmost importance as it directly influences the overall pharmacokinetics of the drugs including its distribution, metabolism and therefore the duration of action.