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Institution

Bharathiar University

EducationCoimbatore, Tamil Nadu, India
About: Bharathiar University is a education organization based out in Coimbatore, Tamil Nadu, India. It is known for research contribution in the topics: Thin film & Adsorption. The organization has 5812 authors who have published 8628 publications receiving 143934 citations. The organization is also known as: BU.


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Journal ArticleDOI
TL;DR: The synthesis of PEG functionalized SeNPs (PEG-SeNPs) is described and its use as a cancer-targeted delivery vehicle to achieve enhanced anticancer efficacy and opens a new path for synergistic treating of cancer with higher efficacy and decreased side effects.
Abstract: Selenium nanoparticles (SeNPs) have garnered a great deal of attention as potential cancer therapeutic payloads. However, the in vivo targeting drug delivery has been challenging. Herein, we describe the synthesis of PEG functionalized SeNPs (PEG-SeNPs) and its use as a cancer-targeted delivery vehicle to achieve enhanced anticancer efficacy. Crocin, a major active product of saffron (dried stigmas of Crocus sativus), having many therapeutic properties was conjugated to PEG-SeNPs. PEG-SeNPs showed pH-mediated crocin release for potential cancer therapy. Crocin conjugated PEG-SeNPs exhibits unprecedented enhanced cytotoxicity toward lung cancer cells through induction of apoptosis. Furthermore, crocin conjugated PEG-SeNPs significantly inhibited in vivo tumor growth in nude mice model. This cancer-targeted design of SeNPs opens a new path for synergistic treating of cancer with higher efficacy and decreased side effects.

51 citations

Journal ArticleDOI
TL;DR: In this paper, the authors studied buoyancy driven convection in a square cavity induced by two mutually orthogonal and arbitrarily located baffles and found that buoyancy force plays a key role and overall heat transfer in the cavity is enhanced for higher values of both baffle-cavity ratios.

51 citations

Journal ArticleDOI
01 Sep 2016-Proteins
TL;DR: Fe2+ promotes the oligomerization by enhancing the peptide‐peptide interaction in the Aβ1‐42‐Zn2+ system, which suggested, Fe2+ promote the oligomersization by enhances the peptides' interaction.
Abstract: The metal ions Zn(2+) , Cu(2+) , and Fe(2+) play a significant role in the aggregation mechanism of Aβ peptides. However, the nature of binding between metal and peptide has remained elusive; the detailed information on this from the experimental study is very difficult. Density functional theory (dft) (M06-2X/6-311++G (2df,2pd) +LANL2DZ) has employed to determine the force field resulting due to metal and histidine interaction. We performed 200 ns molecular dynamics (MD) simulation on Aβ1-42 -Zn(2+) , Aβ1-42 -Cu(2+) , and Aβ1-42 -Fe(2+) systems in explicit water with different combination of coordinating residues including the three Histidine residues in the N-terminal. The present investigation, the Aβ1-42 -Zn(2+) system possess three turn conformations separated by coil structure. Zn(2+) binding caused the loss of the helical structure of N-terminal residues which transformed into the S-shaped conformation. Zn(2+) has reduced the coil and increases the turn content of the peptide compared with experimental study. On the other hand, the Cu(2+) binds with peptide, β sheet formation is observed at the N-terminal residues of the peptide. Fe(2+) binding is to promote the formation of Glu22-Lys28 salt-bridge which stabilized the turn conformation in the Phe19-Gly25 residues, subsequently β sheets were observed at His13-Lys18 and Gly29-Gly37 residues. The turn conformation facilitates the β sheets are arranged in parallel by enhancing the hydrophobic contact between Gly25 and Met35, Lys16 and Met35, Leu17 and Leu34, Val18 and Leu34 residues. The Fe(2+) binding reduced the helix structure and increases the β sheet content in the peptide, which suggested, Fe(2+) promotes the oligomerization by enhancing the peptide-peptide interaction. Proteins 2016; 84:1257-1274. © 2016 Wiley Periodicals, Inc.

51 citations

Journal ArticleDOI
TL;DR: In this paper, BaTiO3:Eu3+@SiO2 superstructures (SS) using CTAB as a surfactant were used for visualizing dormant fingerprints.
Abstract: Nanoparticles (NPs) synthesized via a facile sonochemical route showed excellent assembly of BaTiO3:Eu3+@SiO2 superstructures (SS) using CTAB as a surfactant. Crystallite size, phase, surface science, and core–shell confirmation were determined through advanced characterization techniques. Experimental parameters like pH, temperature, and surfactant concentration were varied and resulted in SS with high surface modifications, and the possible mechanisms for the same are reported. Scanning electron microscopy images revealed broomlike structures, and various experimental parameters resulting in them dissolving into freestanding sticks are discussed. CIE chromaticity coordinates were in the range of the orange-red to pure red. Drawbacks associated with the commercial powder dusting method for visualizing dormant fingerprint (DFP), namely, high background scattering and high autofluorescence of the substrate material, were improved with the help of the prepared SS as a dusting powder. Visualization of DFPs a...

51 citations

Journal ArticleDOI
TL;DR: It is concluded that ketoprofen could have an impact on the development and biological endpoints of the zebra fish at above concentrations and the malformation in the development of the embryo and changes in the biological end points may provide integrated evaluation of the toxic effect of ketoprafen on zebrafish in a new perspective.

51 citations


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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
202321
2022113
2021807
2020694
2019792
2018813