Publications by authors named "Imocha Rajkumar Singh"

The interaction of protein with nanoparticles (NPs) of varying shape and/or size boosts our understanding on their bioreactivity and establishes a comprehensive database for use in medicine, diagnosis, and therapeutic applications. The present study explores the interaction between lysozyme (LYZ) and different NPs like graphene oxide (GO) and zinc oxide (ZnO) having various shapes (spherical, 's', and rod-shaped, 'r') and sizes, focusing on their binding dynamics and subsequent effects on both the protein fibrillation and antimicrobial properties. Typically, GO is considered a promising medium due to its apparent inhibition and prolonged lag phase for LYZ fibrillation.

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Advanced methodologies, such as hyperthermia and modulation of reactive oxygen species (ROS), exhibit considerable promise in the therapeutic landscape of cancer. These strategies offer a targeted paradigm for combating malignant cells while mitigating damage to healthy tissue. Noteworthy among these approaches is the utilization of superparamagnetic iron oxide nanoparticles, which are renowned for their ability to enhance both hyperthermia and ROS generation specifically within tumor microenvironments.

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Developing nano-biomaterials with tunable topology, size, and surface characteristics has shown tremendously favorable benefits in various biologic and clinical applications. Among various nano-biomaterials, peptide-based drug delivery systems offer multiple merits over other synthetic systems due to their enhanced bio- and cytocompatibility and desirable biochemical and biophysical properties. Currently, around 100 peptide-based drugs are clinically available for numerous therapeutic purposes.

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Nanotherapeutics are gaining traction in the modern scenario because of their unique and distinct properties which separate them from macro materials. Among the nanoparticles, metal NPs (MNPs) have gained importance due to their distinct physicochemical and biological characteristics. Peptides also exhibit several important functions in humans.

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The mode of interaction of polyphenolic compounds like genistein (GTN) and ellagic acid (EGA) with human and bovine serum albumin (HSA and BSA, respectively) was found to differ significantly. Stern-Volmer (SV) analysis of the fluorescence quenching data revealed that the binding strength of EGA (1.9 ± 0.

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Binding strength of the anti-diabetic drugs chlorpropamide (CPM) and tolbutamide (TBM) with model protein bovine serum albumin (BSA) shows strong modulation in presence of colloidal gold nanoparticles (AuNP). Intrinsic tryptophan fluorescence of both the native BSA and BSA-AuNP conjugate quenched in presence of the drugs. Stern-Volmer quenching constant (K) of CPM binding to BSA-AuNP conjugate at different temperatures is almost twice (6.

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Carrier proteins like bovine or human serum albumin (BSA and HSA, respectively) are prone to glycation as compared to the other available proteins. In this study, reducing sugars such as l-arabinose (ara), d-(-) galactose (gal) and d-(-) fructose (fru) were used to create model glycated serum albumins and binding ability of these with well-known antidiabetic drug chlorpropamide (CPM) was monitored. Fluorescence quenching experiment revealed that interaction of CPM with native as well as glycated albumins undergoes through a ground state complex formation.

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