02593nas a2200229 4500008004100000022001400041245012400055210006900179260000900248300001600257490000700273520179100280100002002071700001602091700001902107700002302126700003002149700001602179700001902195700001902214856013002233 2022 eng d a1477-922600aDNA binding, antitubercular, antibacterial and anticancer studies of newly designed piano-stool ruthenium(ii) complexes0 aDNA binding antitubercular antibacterial and anticancer studies  cNOV  a16371-163820 v513 a

The chemotherapeutic potential of ruthenium(ii) complexes has recently attracted researchers' interest as antibacterial and anticancer agents. In this study, two novel half-sandwich imine-based Ru complexes ([Ru(p-cymene)Cl(L-1)][PF6] (Ru-1) and [Ru(p-cymene)Cl(L-2)][PF6] (Ru-2)) were reported for their deoxyribonucleic acid (DNA) binding and antitubercular, antibacterial, and anticancer activities. The molecular structure of Ru-2 was obtained by single-crystal X-ray crystallography. DNA interaction studies were conducted by UV-Vis absorbance and fluorescence spectral titration which gave rise to DNA binding constants (K-b) of 1.32 x 10(6) and 1.82 x 10(6) for Ru-1 and Ru-2, respectively and the Stern-Volmer binding constant (K-SV) values for Ru-1 and Ru-2 were 1.7763 x 10(4) M-1 and 7.6 x 10(3) M-1, respectively. The in vitro antitubercular activity was evaluated against Mycobacterium tuberculosis H37Ra. The antibacterial potential of both the Ru-complexes was examined against Gram-negative (Escherichia coli and Pseudomonas aeruginosa) and Gram-positive (Staphylococcus aureus and Bacillus subtilis) bacteria. The half-maximal inhibitory concentration (IC50) values for the antitubercular activity of Ru-1 and Ru-2 were 4.87 +/- 1.32 mu M and 5.78 +/- 0.54 mu M, respectively. A cytotoxic study of these complexes was performed against the human breast cancer cell line (MCF-7) and the human embryonic kidney cell line (HEK293) (normal cells). The study revealed meaningful activity of the Ru-1 complex against (cancer) MCF-7 cells, while the viability of HEK293 (normal) cells in the presence of Ru-2 was higher as compared to a reference drug 5FU. We suggest that these kinds of Ru-complexes could have potential for application in metallopharmaceuticals.

1 aNavale, Govinda1 aSingh, Sain1 aAgrawal, Sonia1 aGhosh, Chandrachur1 aChoudhury, Angshuman, Roy1 aRoy, Partha1 aSarkar, Dhiman1 aGhosh, Kaushik uhttps://library.ncl.res.in/content/dna-binding-antitubercular-antibacterial-and-anticancer-studies-newly-designed-piano-stool02255nas a2200277 4500008004100000022001400041245011700055210006900172260000900241300001100250490000800261520133500269653001201604653002701616653002901643653002001672653002301692100001701715700002201732700001801754700002001772700001901792700001901811700002101830856012601851 2022 eng d a0167-732200aElliptically birefringent chemically tuned liquid crystalline nanocellulose composites for photonic applications0 aElliptically birefringent chemically tuned liquid crystalline na cNOV  a1203260 v3663 a

Cellulose nanocrystals (CNCs) based photonic materials are one of the promising materials in the recent trends. The liquid crystalline behavior of the CNCs can be tailored to different advanced applications. The proposed research investigates the potential of CNCs as an optically active material. CNCs were tuned to hydroxypropyl nano cellulose (HPNC) with the degree of substitution 1.39. The prepared liquid crystalline HPNC were dispersed in various concentrations of monomethyl ether of polyethylene glycol to get waterborne materials with specific optical anisotropy. The extraction, modification, and morphology of the CNCs were investigated using NMR (Nuclear Magnetic Resonance), TEM (Transmission Electron Microscopy), XRD (X-ray Powder Diffraction), and FESEM (Field Emission Scanning Electron Microscopy) analysis. The prepared HPNC was analyzed using a hot stage POM (Polarized Optical Microscope) for optical anisotropy. The thermal stability of prepared CNCs and HPNC was also investigated. Upon optimization using rheology and POM, it was found that at the ratio of 1:1, HPNC (5 wt%) and mPEG (40 wt%) had the most distinct optical properties. The potential of the prepared materials can be further explored in sensing, smart coating, and security materials. (C) 2022 Elsevier B.V. All rights reserved.

10abagasse10aCellulose nanocrystals10aElliptical birefringence10aliquid crystals10aoptical anisotropy1 aSingh, Shiva1 aBhardwaj, Shakshi1 aVerma, Chhavi1 aChhajed, Monika1 aBalayan, Kajal1 aGhosh, Kaushik1 aMaji, Pradip, K. uhttps://library.ncl.res.in/content/elliptically-birefringent-chemically-tuned-liquid-crystalline-nanocellulose-composites03072nas 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

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.

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-amyloid02379nas a2200277 4500008004100000022001400041245010700055210007000162260000900232300001100241490000800252520144600260653002501706653003801731653002201769100001701791700002401808700001601832700002501848700001901873700001901892700001901911700002201930700001901952856013001971 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

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.

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 uhttps://library.ncl.res.in/content/inhibition-amyloid-%CE%B21-42-peptide-aggregation-newly-designed-cyclometallated-palladium