02343nas a2200253   4500008004100000022001400041245009300055210006900148260000800217300001400225490000700239520147400246653003501720653002401755653002501779653002801804653003001832653002301862100002501885700002301910700001801933700001501951856012301966       2022                        eng d  a1948-719300aScan-find-scan-model: discrete site-targeted suppressor design strategy for amyloid-beta0 aScanfindscanmodel discrete sitetargeted suppressor design strate  cJUL  a2191-22080 v133 a<p>
	Alzheimer's disease is undoubtedly the most well-studied ranks at the top in terms of getting attention from the scientific community for structural property-based characterization. Even after decades of extensive research, there is existing volatility in terms of understanding and hence the effective tackling procedures against the disease that arises due to the lack of knowledge of both specific targetand site-specific drugs. Here, we develop a multidimensional approach based on the characterization of the common static-dynamic-thermodynamic trait of the monomeric protein, which efficiently identifies a small target sequence that contains an inherent tendency to misfold and consequently aggregate. The robustness of the identification of the target sequence comes with an abundance of a priori knowledge about the length and sequence of the target and hence guides toward effective designing of the target-specific drug with a very low probability of bottleneck and failure. Based on the target sequence information, we further identified a specific mutant that showed the maximum potential to act as a destabilizer of the monomeric protein as well as enormous success as an aggregation suppressor. We eventually tested the drug efficacy by estimating the extent of modulation of binding affinity existing within the fibrillar form of the A beta protein due to a single-point mutation and hence provided a proof of concept of the entire protocol.</p>
10aconfigurational misfoldability10adrug developability10ainherent frustration10apotential aggregability10asequence-based mutability10atarget specificity1 aBhagavatula, Hasathi1 aSarkar, Archishman1 aSantra, Binit1 aDas, Atanu  uhttps://library.ncl.res.in/content/scan-find-scan-model-discrete-site-targeted-suppressor-design-strategy-amyloid-beta01619nas a2200241   4500008004100000022001400041245007800055210006900133260000800202300001100210490000800221520084700229100002201076700002501098700001801123700002301141700002101164700002701185700002201212700002301234700001801257856010201275       2023                        eng d  a1010-603000aSolvation structure and dynamics of a small ion in an organic electrolyte0 aSolvation structure and dynamics of a small ion in an organic el  cJUN  a1146660 v4403 a<p>
	Organic carbonates are commonly used as electrolytes in commercial lithium-ion batteries. A detailed interpretation of the solvation structure and dynamics of the electrolyte around ions is necessary to understand the charge/discharge process in batteries. This work combines infrared absorption spectroscopy with quantum chemical calculations and molecular dynamics simulations to decipher the solvation structure of propylene carbonate, a cyclic carbonate, around the dissolved thiocyanate ion. Two dimensional infrared spectroscopy and polarization-selective pump probe spectroscopies have been utilized to extract the timescales of solvent fluctuation and the solute reorientational dynamics. The similarity in the slow timescales for the solute and the solvent dynamics signifies that similar processes control both dynamics.</p>
1 aKore, Shivshankar1 aSahoo, Rudhi, Ranjan1 aSantra, Binit1 aSarkar, Archishman1 aChowdhury, Tubai1 aDeshmukh, Samadhan, H.1 aHazarika, Sulagna1 aChatterjee, Srijan1 aBagchi, Sayan  uhttps://library.ncl.res.in/content/solvation-structure-and-dynamics-small-ion-organic-electrolyte