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Two Texas Enemies Died years apart. This is the untold story Former Texas Governor Mark White and Radio Preacher Lester Roloff “Radio preacher… Patricia Champion - 1st Participant GlycoScience Institute Memorial Scholarship Patricia Ann Champion - February 11, 1945 - March 31, 2016 First… Let’s Improve the Brain Safely & Naturally Without Drugs- Glycoscience Lesson #5 Every brain is eligible for improvement and this may be that for which… Breeding Better Fruits and Vegetables - GMO Alternative - Glycoscience Lesson #4 Blending of old world experience and ultrahigh technology by JC Spencer Early Diagnoses of Cognitive Problems - Glycoscience #3 Memory loss and ability for instant recall is a growing challenge for many.

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Two Texas Enemies Died years apart. This is the untold story
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Patricia Champion - 1st Participant GlycoScience Institute Memorial Scholarship
Patricia Ann Champion - February 11, 1945 - March 31, 2016

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Let’s Improve the Brain Safely & Naturally Without Drugs- Glycoscience Lesson #5
Every brain is eligible for improvement and this may be that for which…
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Memory loss and ability for instant recall is a growing challenge for many.

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This booklet is a project of National Institute of Health. The glycomics information is highlighted in yellow.

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New Research Study Explains HOW the Sugar Trehalose Inhibits Alzheimer�s

Comments by J. C. Spencer

Over the last few years research in Universities around the world have supported evidence that the sugar trehalose inhibits protein plaque buildup that causes neurodegenerative diseases including Alzheimer�s, Parkinson�s, and Huntington�s diseases. A new report from the Tianjin University in China explains just how trehalose is able to accomplish this remarkable event in the brain. We learn that the trehalose molecules cluster around the peptide at a specific distance. The intra-peptide hydrophobic interactions are weakened and the Aβ42 contacts are decreased by the trehalose. This finding shines light on the actual molecular mechanism that has the inhibiting effect. More research is needed. This evidence helps point the way for better mental health and neurodegenerative research.

Here is the Abstract and supporting references.

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Molecular Dynamics Simulation of the Conformational Transition of Amyloid Peptide 42 Inhibited by Trehalose

LIU Fu-Feng, DONG Xiao-Yan, SUN Yan

Department of Biochemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, P. R. China

Abstract:

The molecular mechanism of the conformational transition of amyloid peptide (Aβ) 42 inhibited by trehalose was studied using molecular dynamics simulations. It is confirmed that the conformational transition of Aβ42 is prevented by trehalose in a dose-dependent manner. In water and low-concentration trehalose (0.18 mol�L-1) solutions, Aβ42 transforms from its initial α-helix to a β-sheet. In 0.37 mol�L-1 trehalose, however, the conformational transition of Aβ42 is prevented. It is obvious that there is a hydration shell within about 0.2 nm from the closest atoms of Aβ42 on the peptide surface, which is caused by the preferential exclusion of trehalose. Trehalose molecules cluster around the peptide at a distance of 0.4 nm. In addition, the intra-peptide hydrophobic interactions are weakened and the number of long range contacts of Aβ42 is decreased by trehalose. Therefore, the hydrophobic collapse of the peptide is alleviated and the conformational transition is inhibited. The work has shed some light on the molecular mechanism of the inhibition effect for the conformational transition of Aβ in the presence of trehalose. These findings are important for the rational design of a highly efficient inhibitor of Alzheimer's disease.

Keywords: Molecular dynamics simulation Alzheimer's disease Amyloid peptide Trehalose Received: 2009-12-10 Accepted: 2010-03-03 Online: 2010-04-23 Corresponding Authors: SUN Yan Email: [email protected]

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