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Protein fibrillation inhibition by polycyclic planner small molec | 29534
Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

+44 1223 790975

Protein fibrillation inhibition by polycyclic planner small molecules


International Conference on Protein Engineering

October 26-28, 2015 Chicago, USA

Mojtaba Falahati, Paniz Esfandfar and Ali Akbar Saboury

University of Tehran, Iran

Posters-Accepted Abstracts: J Proteomics Bioinform

Abstract :

Neurodegenerative disease such as Alzheimer, Parkinson, Huntington and so many related diseases are linked with a form of protein conformational aggregation known as amyloid fibrils products. It was vastly documented that fibrils and protofibrils intermediates are the most cytotoxic species and numerous reports have been attempt to inhibit fibrillation process as a therapeutic methods. Peptides, surfactants and aromatic small molecules have been used as fibrillation inhibitors. In this report, we examined the interaction of the four natural small molecules (daidzein, resveratrol, fisetin and quercetin dihydrate) with hen egg white lysozyme (HEWL) for inhibiting the fibril formation products with different kinds of methods such as fluorescence, dynamic light scattering, transmission electron microscopy, circular dichroism and isothermal calorimetry. The aim of this study was based on bringing new information into possible association/dissociation constant of natural small molecules with amyloid formation products.

Biography :

Email: falahati@ibb.ut.ac.ir

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