ArticleMolecules (Basel, Switzerland)2022
Insight into the Interaction Mechanism of HSA with Aztreonam: A Multispectroscopic and Computational Approach.
Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 16 citations in OpenAlex.
- Evaluation of the antimicrobial and antibiofilm activities of aztreonam-avibactam against the Burkholderia cepacia complex.Folia microbiologica · 2026Article
- Unravelling the Interaction Mechanism Between Oryzanol and Human Serum Albumin: An Integrated Approach Using Multispectral Analysis and Molecular Simulations.Foods (Basel, Switzerland) · 2026Article
- Binding and transport functions of human serum albumin and its clinical implications in liver disease: a narrative review.Translational gastroenterology and hepatology · 2026Review
- Unveiling the binding details and esterase-like activity effect of methyl yellow on human serum albumin: spectroscopic and simulation study.RSC advances · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Aztreonam is a Gram-negative bacteria-targeting synthetic monobactam antibiotic. Human serum albumin (HSA) plays an important role in the transference of pharmaceuticals, hormones, and fatty acids, along with other compounds, determining their biodistribution and physiological fate. Using several biophysical and in silico approaches, we studied the interaction of aztreonam with HSA under physiological environments in this study. Results confirm the formation of HSA-aztreonam complex where aztreonam showed moderate affinity towards HSA. A static mode of quenching was confirmed from the steady state fluorescence data. FRET findings also showed that there was a significant feasibility of energy transfer between HSA and aztreonam. Site marker displacement experimental conclusion suggested the binding site of aztreonam was the sub-domain IB of HSA. Circular dichroic spectroscopic analysis suggested that aztreonam interaction decreases the α-helical content of HSA. Changes in microenvironment were studied through synchronous fluorescence data. According to molecular docking results, the HSA-aztreonam complex is mostly maintained by non-covalent forces, with a binding energy of 7.7 kcal mol
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Registered trials
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