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American Chemical Society's Weekly Presspac -- Sept. 5, 2007
Date:9/10/2007

abnormal, misfolded protein called islet amyloid polypeptide (IAPP), which may play a key role in the cell destruction.

In the new study, Daniel Raleigh, Andisheh Abedini and Fangli Meng found that changing a single amino acid in human IAPPs structure transformed it from one of the most potent amyloid-forming substances into a powerful inhibitor of amyloid formation. In laboratory studies, they showed that the mutant IAPP significantly reduced the amount of amyloid formed. In addition to opening the door for better IAPP inhibitors in type-2 diabetes, the findings provide potentially important insights into the formation and treatment of amyloid plaques in Alzheimers disease, Parkinsons disease, and other conditions, the researchers say.

ARTICLE #2 FOR IMMEDIATE RELEASE
A Single-Point Mutation Converts the Highly Amyloidogenic Human Islet Amyloid Polypeptide into a Potent Fibrillization Inhibitor

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CONTACT:
Daniel P. Raleigh, Ph.D.
State University of New York at Stony Brook
Stony Brook, NY 11794-3400
Phone: 631-632-9547
Fax: 631-632-7960
E-mail: draleigh@notes.cc.sunysb.edu

ARTICLE #3 FOR IMMEDIATE RELEASE

Magnets can boost production of ethanol for fuel
Biotechnology Progress

In a finding that could reduce the cost of ethanol fuel, researchers in Brazil report success in using low frequency magnetic waves to significantly boost the amount of ethanol produced through the fermentation of sugar. Their study is scheduled for the Oct. 5 iss
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Contact: Michael Woods
m_woods@acs.org
202-872-4400
American Chemical Society
Source:Eurekalert

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