Ocimum sanctum mediated green synthesis of silver nanoparticles: A biophysical study towards lysozyme binding and anti-bacterial activity

Baruah, Kakali; Haque, Mahabul; Langbang, Leader; Das, Sourav; Aguan, Kripamoy; Roy, Atanu Singha

doi:10.1016/j.molliq.2021.116422

Cited by 16 publications

(1 citation statement)

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“…[20] Baruah et al reported the interaction between silver nanoparticles and Lysozyme. [21] The primary objective of this study is to synthesize CuO NPs using a green, convenient, economical, and ecofriendly method and to characterize their interaction with ct-DNA and the major blood proteins (HSA, HHb, and Lys) under simulative physiological conditions (pH = 7.40) using a variety of physicochemical analyses. Such research is necessary to gain insight into the molecular mechanism underlying the interactions of CuO NPs with proteins and CuO NPs with DNA.…”

Section: Introductionmentioning

confidence: 99%

Green Synthesis, in vitro Cytotoxicity, Antioxidant Activity and Interaction Studies of CuO Nanoparticles with DNA, Serum Albumin, Hemoglobin and Lysozyme

2022

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The present study reports an environmentally safe synthesis of CuO NPs employing Echinophora platyloba DC extract. The production of CuO NPs was authenticated using various analytical characterization techniques such as FT-IR, TEM, XRD, SEM-EDX, DLS, zeta potential, and UV-Vis. The DPPH assay was employed to assess the scavenging efficacy of synthesized CuO NPs. The results of the MTT assay exhibited that CuO NPs have efficient anticancer potential on two used cancer cell lines (MCF-7 and Burkitt's lymphoma). Thus, it tempts us to study the synthesized CuO NPs biocompatible aspects by interactions with several biologically significant molecules. The present experimental evidence demonstrates the direct interaction of CuO NPs with DNA, which might be one of the credible highways elevating its anticancer potential. Moreover, we investigated the interaction of CuO NPs with the most important blood proteins (HSA, HHb, and Lys) in simulated physiological conditions using spectroscopic methods. The interaction findings suggest that the native conformation of the above proteins was preserved at the level of secondary structure in spite of complex formations with CuO NPs. The binding constant values revealed the greater binding affinity of CuO NPs with HSA, HHb, and Lys as compared to ct-DNA; the binding affinity was found in the order HSA > HHb > Lys > ct-DNA.

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Section: Introductionmentioning

confidence: 99%