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1.
RSC Adv ; 13(46): 32223-32265, 2023 Oct 31.
Article in English | MEDLINE | ID: mdl-37928851

ABSTRACT

The optical features of gold nanorods (GNR) may be precisely controlled by manipulating their size, shape, and aspect ratio. This review explores the impact of these parameters on the optical tuning of (GNR). By altering the experimental conditions, like the addition of silver ions during the seed-mediated growth process, the aspect ratio of (GNR) may be regulated. The shape is trans from spherical to rod-like structures resulting in noticeable changes in the nanoparticles surface plasmons resonance (SPR) bands. The longitudinal SPR band, associated with electron oscillations along the long axis, exhibits a pronounced red shift into the (NIR) region as the aspect ratio increases. In contrast, the transverse SPR band remains relate unchanged. Using computational methods like the discrete dipole approximation (DDA) allows for analyzing absorption, scattering, and total extinction features of gold (G) nanoparticles. Studies have shown that increasing the aspect ratio enhances the scattering efficiency, indicating a higher scattering quantum yield (QY). These findings highlight the importance of size, shape, and aspect ratio in controlling the optical features of (GNR) providing valuable insights for various uses in nanophotonics and plasmonic-dependent fluorescence in cancer treatment and developing new photonic compound NRs.

2.
Sci Rep ; 13(1): 3926, 2023 03 09.
Article in English | MEDLINE | ID: mdl-36894576

ABSTRACT

A putative virulence exoprotease designated as UcB5 was successfully purified from the bacterium Salmonella typhimurium to the electrophoretic homogeneity with 13.2-fold and 17.1% recovery by hydrophobic, ion-exchange, and gel permeation chromatography using Phenyl-Sepharose 6FF, DEAE-Sepharose CL-6B, and Sephadex G-75, respectively. By applying SDS-PAGE, the molecular weight was confirmed at 35 kDa. The optimal temperature, pH, and isoelectric point were 35 °C, 8.0, 5.6 ± 0.2, respectively. UcB5 was found to have a broad substrate specificity against almost all the tested chromogenic substrates with maximal affinity against N-Succ-Ala-Ala-Pro-Phe-pNA achieving Km of 0.16 mM, Kcat/Km of 3.01 × 105 S-1 M-1, and amidolytic activity of 28.9 µmol min-1 L-1. It was drastically inhibited by TLCK, PMSF, SBTI, and aprotinin while, DTT, ß-mercaptoethanol, 2,2'-bipyridine, o-phenanthroline, EDTA, and EGTA had no effect, which suggested a serine protease-type. Also, it has shown a broad substrate specificity against a broad range of natural proteins including serum proteins. A cytotoxicity and electron microscopy study revealed that UcB5 could cause subcellular proteolysis that finally led to liver necrosis. For this, future research should focus on using a combination of external antiproteases and antimicrobial agents for the treatment of microbial diseases instead of using drugs alone.


Subject(s)
Salmonella typhimurium , Serine Proteases , Serine Proteases/metabolism , Salmonella typhimurium/metabolism , Hydrogen-Ion Concentration , Serine Endopeptidases/metabolism , Isoelectric Point , Temperature , Substrate Specificity , Molecular Weight
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