The Alchemist Newsletter: November 15, 2005

In this issue, The Alchemist discovers the gecko's climbing secret, why red kiwi fruits could become all the rage for fitness fanatics, and finds a natural approach for the chemical industry. Also this month, a molecular Lego set wins the 2005 Feynman Prize and Alzheimer's insights provide an explanation for drug's effects.

	physical: Geckos get stickier as the humidity rises
	biochemistry: The reds in the fruitbowl
	industry: A natural approach to the chemical industry
	nanotechnology: Feynman Winners
	pharma: Alzheimer's filament

Geckos get stickier as the humidity rises

Geckos are well known as expert climbers, they're the biggest creatures that can hang unassumedly from a ceiling. Now, as part of the international effort to understand how geckos achieve their inverted trick, researchers at the Max Planck Institute for Metals Research in Stuttgart and Saarbruecken, Nuernberg-Erlangen and the ETH Zurich have demonstrated that the "stickiness" of the soles of a gecko's feet increases as the humidity rises. The researchers suggest that their microscopic analysis could open up new avenues of research into artificial adhesive systems.

Hairy Feet Stick Better to Wet Ceiling

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The reds in the fruitbowl

Red-fleshed kiwi fruits could soon be making a healthy debut on supermarket shelves. A team of researchers in Italy and New Zealand has already demonstrated why they could make a fitting choice for consumers. The researchers used HPLC to analyze the fruit's pigments and compared their findings with authentic standards. They also used liquid chromatography-mass spectrometry to obtain a tentative identification of the major anthocyanins in red-fleshed kiwifruit. Red-fleshed kiwifruit, they say, contain significant quantities of anthocyanins, bright red pigments that the researchers explain are highly potent antioxidants, thought to provide protection against heart disease and cancer.

Red kiwi poised to make a healthy debut

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A natural approach to the chemical industry

A sustainable chemical process developed by researchers at the University of Amsterdam and Radboud University in Nijmegen and partners Synthon could lead to higher reaction rates, substantially bigger yields, and less waste. The development of the process, for which Synthon has a patent pending was supported by NWO ACTS (Advanced Chemical Technologies for Sustainability). The one-pot approach developed by the Dutch team combines a metal-catalyzed conversion with an enzymic step at optimized pH and temperature. The overall reaction times were shorter when the process was carried out using a one-pot approach and yields were higher than when each step was carried out separately.

Natural chemistry finds its way to market

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Feynman Winners

Christian Schafmeister of University of Pittsburgh and his team have won the 2005 Feynman prize awarded by the Foresight Nanotech Institute for their work in developing what they call a "molecular Lego set". Like the children's construction kit, the researchers say their molecular kit can be used to piece together sturdy, predictable nanostructures. The Pitt team designed fourteen small molecular building blocks that carry two removable molecular caps. Controlled reactions strategically strip away the caps, causing the molecules to link together in predictable ways. The researchers have already snapped together nanometer rods and crescents and reckon they could produce a wide variety of structures with their technique.

Pitt professor, student win Feynman prizes for work on 'molecular Lego® set'

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Alzheimer's filament

Researchers at the Salk Institute and the University of Lausanne working with pharmaceutical company Roche have solved the three-dimensional structure of the long thread-like fibers that are present in the brain tissue of Alzheimer's disease patients. The structure reveals that theses proteins zipper together to make the fibrils, a process that might be a target for novel drugs to combat the debilitating effects of the disease. Salk's Roland Riek says that the study will primarily help explain how one drug currently in European clinical trials works. Apparently, the drug binds to the end of the fibril chain of beta amyloid proteins and stops them accumulating to form the telltale amyloid plaques of Alzheimer's disease.

3-D Structure of Alzheimer's Disease Filament Shows How It Zips Up Peptides

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-- David Bradley, Science Journalist