alexa
Reach Us +1(850)754-6199
Molecular Mechanism Of Alzheimer’s Disease | 91080
ISSN: 2155-952X

Journal of Biotechnology & Biomaterials
Open Access

Like us on:

Our Group organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations
700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)
All submissions of the EM system will be redirected to Online Manuscript Submission System. Authors are requested to submit articles directly to Online Manuscript Submission System of respective journal.

Molecular mechanism of Alzheimer’s disease

Annual Biotechnology Congress

Zoya Leonenko

University of Waterloo, Canada

Keynote: J Biotechnol Biomater

DOI: 10.4172/2155-952X-C3-093

Abstract
Alzheimer’s disease (AD) is a neurodegenerative disease characterized by dementia and memory loss for which no cure or prevention is available. Amyloid toxicity is a result of the non-specific interaction of toxic amyloid oligomers with the plasma membrane. We studied amyloid aggregation and interaction of amyloid beta (1-42) peptide with lipid membrane using atomic force microscopy (AFM), Kelvin probe force microscopy and surface plasmon resonance (SPR). Using AFMbased atomic force spectroscopy (AFS) we measured the binging forces between two single amyloid peptide molecules. Using AFM imaging we showed that oligomer and fibril formation is affected by surfaces, presence of metals and inhibitors. We demonstrated that lipid membrane plays an active role in amyloid binding and toxicity: changes in membrane composition and properties increase amyloid binding and toxicity. Effect of lipid composition, the presence of cholesterol and melatonin are discussed. We discovered that membrane cholesterol creates nanoscale electrostatic domains which induce preferential binding of amyloid peptide, while membrane melatonin reduces amyloid-membrane interactions, protecting the membrane from amyloid attack. Using AFS we that novel pseudo-peptide inhibitors effectively prevent amyloid-amyloid binding on a single molecule level, to prevent amyloid toxicity. These findings contribute to better understanding of the molecular mechanisms of Alzheimer's disease and aid to the developments of novel strategies for cure and prevention of AD.
Biography

Zoya Leonenko is the Professor, Department of Physics and Astronomy, Department of Biology, Waterloo Institute for Nanotechnology, Center for Bioengineering and Biotechnology, University of Waterloo, Vice President of the Biophysical Society of Canada. She holds a PhD in Chemical Physics, 1996, Russian Academy of Sciences. She is leading a Biophysics research group at the University of Waterloo. Her current research interests include scanning probe microscopy, biophysics of lipid membrane and lipid-protein interactions, the role of structural changes and physical properties of lipid template in controlling biological processes and diseases, application of lipid films in bio- and nano- technology.

E-mail: [email protected]

Top