Anti-browning and antibacterial dual functions of novel hydroxypyranone-thiosemicarbazone derivatives as shrimp preservative agents: Synthesis, bio-evaluation, mechanism, and application

Synthesis, structural characterization, density functional theory, anticancer, and antimicrobic studies of Ni2+ and Cu2+ complexes encompassing tridentate ONS‐donor azo‐thiosemicarbazone

“…They have attracted a lot of study interest because of their therapeutic applications for the treatment of feared diseases like tuberculosis and leprosy in the 1950s 5–8 . Additional investigation on TSCs has demonstrated advantageous biological uses in various areas, incorporating bactericidal, 9,10 antiviral, 11 anti‐spermatogenic, antifungal, 12,13 anti‐inflammatory, 14,15 antioxidant, 15,16 anticancer, 17–19 antimicrobial, 20 anti‐neurotoxic, 21 antimalarial, 15 anti‐proliferative, 22 and anti‐HIV‐TB co‐infection 23 and to an limit anti‐HIV 24 as well as in therapy for Alzheimer's disease 25 . As well as act as cruzipain, urease, α‐glucosidase, acetylcholinesterase, butyrylcholinesterase, and mushroom tyrosinase inhibitors 26–29 .…”

Translocation of Pyrimidine Derivative-Capped Gold Nanoparticles via Membrane Ion Channels Induce Pseudomonas aeruginosa and Staphylococcus aureus Cell Death

“…It has been shown that AuNPs can induce conformational changes in adsorbed proteins. , Therefore, the bacterial membrane protein conformational variations caused by MP-AuNPs were further investigated. Phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp) are the dominant amino acid residues of membrane proteins, and as fluorescent chromophores, they emit fluorescence at the excitation wavelengths of 258, 280, and 296 nm, respectively . Water-soluble fluorescence quenching agent potassium iodide (KI) can only quench the fluorescence of membrane proteins located at the cell exterior.…”

“…Phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp) are the dominant amino acid residues of membrane proteins, and as fluorescent chromophores, they emit fluorescence at the excitation wavelengths of 258, 280, and 296 nm, respectively. 36 Water-soluble fluorescence quenching agent potassium iodide (KI) can only quench the fluorescence of membrane proteins located at the cell exterior. The decreased fluorescence intensity of three amino acid residues was representative of the conformation change of the protein.…”