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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
Published on: March 27, 2017
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Inhibition of amyloid β1-42 peptide aggregation by newly designed cyclometallated palladium complexes
Rahul Saini1, Govinda R Navale1, Sain Singh1
1Department of Chemistry, Indian Institute of Technology, Roorkee 247667, India.
International Journal of Biological Macromolecules
|July 17, 2023
Summary
New palladium complexes show promise in preventing amyloid aggregation, a key factor in neurodegenerative diseases like Alzheimer's. These compounds interfere with protein self-recognition pathways, reducing harmful fibril formation.
Area of Science:
- Medicinal Chemistry
- Biochemistry
- Materials Science
Background:
- Uncontrolled amyloid aggregation is implicated in neurodegenerative disorders like Alzheimer's disease (AD).
- Developing molecules to inhibit protein self-recognition and aggregation is a key therapeutic strategy.
Purpose of the Study:
- To design and synthesize novel cyclometallated palladium complexes.
- To investigate the effect of these complexes on the aggregation and fibrillation of bovine serum albumin (BSA) and amyloid-beta (Aβ) peptides.
Main Methods:
- Synthesis and characterization of palladium complexes (Pd-1, Pd-2, Pd-3) using spectroscopic methods and X-ray crystallography.
- Assessment of secondary structures via circular dichroism (CD) and transmission electron microscopy (TEM).
- Investigation of amyloid aggregation inhibition using Thioflavin-T (ThT) assay and molecular docking studies.
Main Results:
- Pd-2 and Pd-3 complexes significantly reduced amyloid fibril formation and protein aggregation.
- Spectroscopic and crystallographic analyses confirmed the structure of the synthesized palladium complexes.
- Molecular docking revealed hydrogen bonding and hydrophobic interactions between complexes and Aβ peptides, inhibiting β-sheet formation.
Conclusions:
- The synthesized palladium complexes, particularly Pd-2 and Pd-3, demonstrate potent inhibitory activity against amyloid aggregation.
- These findings suggest potential therapeutic applications for these complexes in combating neurodegenerative diseases associated with amyloid pathology.
