Interaction of AMOT@CS NPs and AMOT drug with bovine serum albumin: Insights from spectroscopic and molecular docking techniques
2021; Elsevier BV; Volume: 546; Linguagem: Inglês
10.1016/j.chemphys.2021.111139
ISSN1873-4421
AutoresYahiya Kadaf Manea, Afreen Banu, Mohsen T.A. Qashqoosh, Amjad Mumtaz Khan, Faiza M.A. Alahdal, Ajaz Ahmad Wani, Mansour A.S. Salem, Saeeda Naqvi,
Tópico(s)Surfactants and Colloidal Systems
ResumoThe drug binding to serum protein (SP) is an area of intense research in evaluating drug candidates. Thus, composite material based on chitosan (CS), and amoxicillin tri hydrate (AMOT) were designed in order to evaluate the release of [email protected] NPs and it’s binding with BSA under physiological condition. The inclusion of 2% v/v T80 in the CS NPs enabled in vitro release of AMOT, at 298 K and pH 7.4 up to 68.03%. This study also was undertaken to compare and explore the binding of potential chemotherapeutic antibacterial drug Amoxicillin trihydrate (AMOT) and [email protected] nanoparticles ([email protected] NPs) with a model protein bovine serum albumin (BSA) by fluorescence spectroscopy, synchronous fluorescence spectroscopy, Ultraviolet–visible (UV–vis) absorption, and CD spectroscopic techniques. Experimental results indicated that AMOT and [email protected] NPs could bind with BSA and quench the fluorescence of BSA via static mechanism. The interactions among BSA with AMOT, AMOT/T80 and [email protected] NPs were evidenced by substantial changes in the BSA secondary structure, as revealed by circular dichroism. The findings of thermodynamic parameters revealed that the binding reaction in both systems was exothermic and spontaneous, enthalpically driven and that the hydrogen bonding and Vander Waals forces played a vital role to achieve optimal interaction between AMOT/ [email protected] NPs and BSA.
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