02415nas a2200301   4500008004100000020001400041022001400055245012000069210006900189260000800258300001600266490000700282520145200289653001501741653001201756653001901768653000601787653001901793653002201812100002401834700001601858700002401874700001701898700002401915700002301939700002201962856012901984       2020                        eng d  a1572-8862  a1040-727800aInhibition of quorum sensing, motility and biofilm formation ofpseudomonas aeruginosaby copper oxide nanostructures0 aInhibition of quorum sensing motility and biofilm formation ofps  cOCT  a1531 - 15410 v323 a<p>Quorum sensing (QS) is the communication between bacterial cells governed by their population density and regulated by the genes controlling virulence factors and biofilm formation. Multiple mechanisms of biofilms are resistive to antimicrobial chemotherapy; therefore novel strategies are required to overcome its limitations. Here, we report the effect of various copper oxide nanostructures (CuO-NSs) on quorum sensing inhibition. The two-dimensional CuO-NSs such as interlaced nanodiscs, nanodiscs and leaf-shaped nanosheets are prepared via a simple chemical method. The Quorum sensing inhibition (QSI) activity of all the CuO-NS are examined using reporter strainChromobacterium violaceumCV026 andEscherichia colipSB1142. We found that the CuO-interlaced nanodisc structures exhibit better QSI activity than nanodiscs and leaf-shaped sheets. The interlaced nanodisc structures are inhibited various long-chainN-acyl homoserine lactones (AHLs) mediated QS individually and confirmed by other QS-associated phenomena forPseudomonas aeruginosa, including biofilm inhibition, inhibition of virulence factors such as pyocyanin, protease production and swarming motility. Thus QSI activity of CuO-NSs is solely dependent on specific shape offering large surface area and more active sites. The CuO-NS is effective quorum sensing inhibitors, which has potential clinical applications in the management ofP. aeruginosaassociated infections.</p>
10aaeruginosa10aBiofilm10aNanostructures10aP10aquorum sensing10aVirulence factors1 aDesai, Dnyanada, G.1 aSwarali, H.1 aNavale, Govinda, R.1 aPrabhune, A.1 aLate, Dattatray, J.1 aDharne, Mahesh, S.1 aWalke, Pravin, S.  uhttp://library.ncl.res.in/content/inhibition-quorum-sensing-motility-and-biofilm-formation-ofpseudomonas-aeruginosaby-copper02378nas a2200277   4500008004100000022001400041245010700055210007000162260000900232300001100241490000800252520144600260653002501706653003801731653002201769100001701791700002401808700001601832700002501848700001901873700001901892700001901911700002201930700001901952856012901971       2023                        eng d  a0141-813000aInhibition of amyloid β1-42 peptide aggregation by newly designed cyclometallated palladium complexes0 aInhibition of amyloid β142 peptide aggregation by newly designed  cSEP   a1258470 v2483 a<p>
	Uncontrolled amyloid aggregation is a frequent cause of neurodegenerative disorders such as prions and Alzheimer's disease (AD). As a result, many drug development approaches focus on evaluating novel molecules that can alter self-recognition pathways. Herein, we designed and synthesized the cyclometallated pyrene (Pd-1 and Pd-3) and anthracene (Pd-2) based palladium complexes ([Pd((L-1)Cl] Pd-1, [Pd(L-2)Cl](Pd-2), and [Pd(L-3)Cl] (Pd-3)). This study explores the effect of these complexes on the aggregation, fibrillation, and amyloid formation of bovine serum albumin (BSA) and A beta(1-42) peptide. Several spectroscopic methods were used to characterize all the Pd-complexes, and the molecular structure of Pd -3 was determined by X-ray crystallography. The secondary structures were studied using circular dichroism (CD) and transmission electron microscopy (TEM), while am-yloid aggregation and inhibitory activities were investigated using the Thioflavin-T (ThT) fluorescence assay. Molecular docking of the Pd-complex (Pd-3) was done using fibril (PDB: 2BEG) and monomeric (PDB: 1IYT) peptides using Auto-dock Vina. As a result, the hydrogen bonding and hydrophobic interaction between the aromatic rings of the Pd-complexes and the amino acids of amyloid-beta peptides significantly reduced the pro-duction of ordered beta-sheets of amyloid fibrils and protein aggregation in the presence of Pd-2 and Pd-3 complexes.</p>
10aA beta(1-42) peptide10aAggregation and molecular docking10aPalladium complex1 aSaini, Rahul1 aNavale, Govinda, R.1 aSingh, Sain1 aSingh, Haobam, Kisan1 aChauhan, Rahul1 aAgrawal, Sonia1 aSarkar, Dhiman1 aSarma, Manabendra1 aGhosh, Kaushik  uhttp://library.ncl.res.in/content/inhibition-amyloid-%CE%B21-42-peptide-aggregation-newly-designed-cyclometallated-palladium