02050nas a2200253   4500008004100000022001400041245012500055210006900180260000800249300001100257490000800268520116800276653001601444653003201460653002201492653002901514100002301543700002401566700001701590700001901607700002301626700001601649856013101665       2020                        eng d  a0301-462200aEffect of tert-alcohol functional imidazolium salts on oligomerization and fibrillization of amyloid beta (1-42) peptide0 aEffect of tertalcohol functional imidazolium salts on oligomeriz  cDEC  a1064800 v2673 a<p>Imidazolium based IL's has gained vast interest in developing biological applications. Oligomerization and fibrillization of amyloid beta (1-42) peptide are mainly responsible for the extra-neuronal deposition of amyloid fibrils in neurodegenerative disorders like Alzheimer's disease (AD). Here, we report an effect of tert-BuOH-functional imidazolium ILs on oligomerization and fibrillization of amyloid beta (1-42) Peptide in vitro. In this study, a series of these [alkyl-(t)OHim][OMs] ILs with methyl sulphonate counter anion by varying alkyl chains were used. Among the seven protic ILs, four showed strong binding and inhibition activity for the formation of amyloid beta (1-42) aggregation by using Thioflavin T fluorescence binding assay. The secondary structural analysis of the peptide, pre-incubated with active ILs shows the loss of ordered beta-sheet amyloid structure. The longer alkyl chain ILs showed that an increased in amyloid binding and hence an inhibition effect on amyloid aggregation was enhanced. Thus, we propose that ILs could be presented as potential candidates for therapeutic intervention against Alzheimer's disease (AD).</p>
10aAggregation10aAmyloid beta (1-42) peptide10aBiofilm inhibitor10aImidazolium ionic liquid1 aSaid, Madhukar, S.1 aNavale, Govinda, R.1 aYadav, Ashok1 aKhonde, Nilesh1 aShinde, Sandip, S.1 aJha, Anjali  uhttps://library.ncl.res.in/content/effect-tert-alcohol-functional-imidazolium-salts-oligomerization-and-fibrillization-amyloid03072nas a2200313   4500008004100000022001400041245014000055210006900195260000900264300001100273490000800284520201300292653001602305653002802321653002002349653001902369653002202388653002402410100001602434700002402450700001902474700002502493700002002518700001902538700002202557700002902579700001902608856013102627       2023                        eng d  a0141-813000aDesign and synthesis of piano-stool ruthenium(II) complexes and their studies on the inhibition of amyloid ? (1-42) peptide aggregation0 aDesign and synthesis of pianostool rutheniumII complexes and the  cJUN   a1241970 v2393 a<p>
	Misfolding , protein aggregation have been linked to numerous human neurodegenerative disorders such as Alzheimer's, prion , Parkinson's diseases. Ruthenium (Ru) complexes have received considerable attention in studying protein aggregation due to their interesting photophysical and photo properties. In this study, we have synthesized the novel Ru complexes ([Ru(p-cymene)Cl(L-1)][PF6](Ru-1), and [Ru(p-cymene)Cl(L-2)][PF6](Ru-2)) and investigated their inhibitory activity against the bovine serum albumin (BSA) aggregation and the A beta 1-42 peptides amyloid formation. Several spectroscopic methods were used to characterize these complexes, and the molecular structure of the complex was determined by X-ray crystallography. Amyloid aggregation and inhi-bition activities were examined using the Thioflavin-T (ThT) assay, and the secondary structures of the protein were analyzed by circular dichroism (CD) spectroscopy and transmission electron microscopy (TEM). The cell viability assay was carried out on the neuroblastoma cell line, revealing that the complex Ru-2 showed better protective effects against A beta 1-42 peptide toxicity on neuro-2a cells than the complex Ru-1. Molecular docking studies elucidate the binding sites and interactions between the Ru-complexes and A beta 1-42 peptides. The exper-imental studies revealed that these complexes significantly inhibited the BSA aggregation and A beta 1-42 amyloid fibril formation at 1:3 and 1:1 molar concentrations, respectively. Antioxidant assays demonstrated that these complexes act as antioxidants, protecting from amyloid-induced oxidative stress. Molecular docking studies with the monomeric A beta 1-42 (PDB: 1IYT) show hydrophobic interaction, and both complexes bind preferably in the central region of the peptide and coordinate with two binding sites of the peptide. Hence, we suggest that the Ru-based complexes could be applied as a potential agent in metallopharmaceutical research against Alzheimer's disease.</p>
10aAggregation10aAmyloid ?(1-42) peptide10aDFT computation10aFibrillization10aMolecular docking10aRuthenium complexes1 aSingh, Sain1 aNavale, Govinda, R.1 aAgrawal, Sonia1 aSingh, Haobam, Kisan1 aSingla, Labhini1 aSarkar, Dhiman1 aSarma, Manabendra1 aChoudhury, Anghuman, Roy1 aGhosh, Kaushik  uhttps://library.ncl.res.in/content/design-and-synthesis-piano-stool-rutheniumii-complexes-and-their-studies-inhibition-amyloid