Erkmen, Cem and Bozal-Palabiyik, Burcin and Tayyab, Hafsa and Kabir, Md. Zahirul and Mohamad, Saharuddin and Uslu, Bengi (2023) Exploring molecular interaction of cefpirome with human serum albumin: In vitro and in silico approaches. Journal of Molecular Structure, 1275. ISSN 0022-2860, DOI https://doi.org/10.1016/j.molstruc.2022.134723.
Full text not available from this repository.Abstract
Cefpirome (CFP), a fourth-generation cephalosporin for parenteral administration, is highly influential against gram-negative and gram-positive bacteria. Multiple approaches, such as fluorescence, absorption, voltammetric, and molecular docking were applied to assess the binding of CFP to the primary carrier protein, human serum albumin (HSA). The CFP-triggered quenching of HSA fluorescence reported the CFP -HSA complex formation, which was accomplished by a static quenching mechanism. A moderate binding affinity (Kf = 1.78 x 10 4 M -1 at 298 K) was found in the CFP -HSA interaction. The complex was anticipated to be stabilized by the presence of van der Waals interactions and hydrogen bonds. Upon CFP binding, microenvironmental alterations surrounding Trp and Tyr residues of HSA were observed. To establish the location of the CFP binding site in HSA, molecular docking studies were conducted, and the results indicated that CFP attaches to site I of HSA mostly through hydrophobic interactions and hy-drogen bonding. The results of fluorescence spectroscopy and molecular docking supported one another quite well.(c) 2022 Elsevier B.V. All rights reserved.
| Item Type: | Article |
|---|---|
| Funders: | Ankara University (Grant No: 18B0237001), Ministry of National Education - Turkey, Turkiye Bilimsel ve Teknolojik Arastirma Kurumu (TUBITAK) |
| Uncontrolled Keywords: | Cefpirome; Human serum albumin; Fluorescence spectroscopy; Binding mechanism; Molecular docking |
| Subjects: | Q Science > QD Chemistry |
| Divisions: | Faculty of Science > Institute of Biological Sciences |
| Depositing User: | Ms Zaharah Ramly |
| Date Deposited: | 29 Nov 2023 04:50 |
| Last Modified: | 29 Nov 2023 04:50 |
| URI: | http://eprints.um.edu.my/id/eprint/39233 |
Actions (login required)
 |
View Item |
