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Inhibition of amyloid beta peptide oligomerization: Empirical and ab initio studies
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Medicinal Chemistry

ISSN: 2161-0444

Open Access

Inhibition of amyloid beta peptide oligomerization: Empirical and ab initio studies


5th International Conference on Medicinal Chemistry & Computer Aided Drug Designing and Drug Delivery

December 05-07, 2016 Phoenix, USA

Arvi Rauk

University of Calgary, Canada

Scientific Tracks Abstracts: Med chem

Abstract :

The primary neurodestructive agent in Alzheimerâ??s disease is an aggregated form of the amyloid beta peptide, A?²(1-40) and A?²(1-42), probably acting in conjunction with redox active transition metals, copper and iron (in the form of heme). The approach in our laboratory for the past ten years has been the in silico development and characterization of short peptide strings which are designed to bind selectively to A?² and prevent its oligomerization. The ?²-sheet-blocking peptides can interact with A?² to form a large variety of complexes. We present here the results of a case study by molecular dynamics simulations aimed at determining the structures and relative binding affinities of one of our nano-MABs interacting with full length A?²(1- 42).

Biography :

Arvi Rauk has completed his PhD from Queen’s University in Kingston, Ontario and Postdoctoral studies from Princeton University, Department of Chemistry. He has published more than 200 papers in reputed journals and has been serving as an Editorial Board Member of repute.

Email: rauk@ucalgary.ca

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Citations: 6627

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