Finding Universal Inhibitor of Amyloid Aggregation

Protein misfolding and aggregation results in many human diseases and some diseases are caused when protein aggregation leads to amyloid formation(Chiti and Dobson, 2006). Amyloids are rigid, insoluble, unbranched, fibrous and well organized proteinaceous materials having cross-β\ud core structure(Chiti and Dobson, 2006)(Nelson et al., 2005). They have characteristic “cross β-sheet” structure, revealed by X-ray diffraction studies. Detection of amyloid can be done by both congo red binding and thioflavin-T (Th-T) assay. Thermodynamic properties of complexes of Congo Red (CR) dye with amyloid β(Aβ) peptides were studied by absorption spectroscopy and thioflavin-T were studied by fluorescence spectroscopy. Inhibition of pathogenic protein aggregation may be an important and straight forward therapeutic strategy for curing amyloid diseases.inhibitory effect of 3-aminophenol, GPS-1, GPS-2 on bovine serum \ud albumin, lysozyme, rnq1 prion protein amyloid aggregates were studied. 3aminophenol shows significant inhibitory action on lysozyme amyloid aggregates