@article {48808,
	title = {Inhibition of amyloid β1-42 peptide aggregation by newly designed cyclometallated palladium complexes},
	journal = {International Journal of Biological Macromolecules},
	volume = {248},
	year = {2023},
	month = {SEP },
	pages = {125847},
	type = {Article},
	abstract = {<p>
	Uncontrolled amyloid aggregation is a frequent cause of neurodegenerative disorders such as prions and Alzheimer{\textquoteright}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>
},
	keywords = {A beta(1-42) peptide, Aggregation and molecular docking, Palladium complex},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2023.125847},
	author = {Saini, Rahul and Navale, Govinda R. and Singh, Sain and Singh, Haobam Kisan and Chauhan, Rahul and Agrawal, Sonia and Sarkar, Dhiman and Sarma, Manabendra and Ghosh, Kaushik}
}
