Research led by Prof. Ramamoorthy and collaborators has been selected as one of the research of special significance in the field of Alzheimer's disease and listed in F1000Prime. The research titled "Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid-β species" is published in Proceedings of the National Academy of Sciences of the United States of America, 2013 (DOI: 10.3410/f.718002371.793475358) and can be found here.
Researchers at the University of Michigan have found a new potential benefit of a molecule in green tea: preventing the misfolding of specific proteins in the brain.
Prof. Ramamoorthy says, " A cup of green tea a day keeps the Alzheimer's disease away". He and his collaborators have found that EGCG, an ingredient found in green tea extract prevents the aggregate formation and break down of already formed amyloid aggregates which are known to be the key in Alzheimer's disease. A detailed note on this ground breaking discovery has been published in ScienceDaily here.
Read the ScienceDaily Science News article published on Samer's recent paper: here.
We also wish Samer farewell and wish him the best in medical school!
The JACS Image Challenge #106 was drawn from Pieter's recent dendrimer publication! September 22, 2010
Try to see if you can solve the challenge here!
You can also access the original publication here.
Avanti Polar Lipics, Inc. Begins Selling a New Type of Lipids Based on Research Done in Our Lab! August 23, 2010
Avanti is now selling 14:0 PE-DTPA(Cu) lipids. The addition of these lipids to their catalog was inspired by exciting research performed in our lab! This is outstanding vallidation that the research done in the Ramamoorthy lab is extremely important and relevant in both the NMR and biological fields. A detailed pdf brochure can be downloaded by following this link.
"Inclusion of copper (Cu2+) ions in bicelles in the form of a lipid chelate resulted in a 10-fold T1 reduction and 2.7-fold increase in S/N of spectra for static experiments. This improvement would allow 2D experiments on membrane proteins in aligned lipid bilayers that typically take 3 days to be completed in <1.5 days. The technique is particularly beneficial to the study of membrane disrupting/permeating systems (such as antimicrobial peptides, toxins, amyloid peptides, and fusion peptides) whose concentration cannot be increased, as they result in nonlamellar conditions."
ANN ARBOR, Mich.—In type 2 diabetes, a protein called amylin forms dense clumps that shut down insulin-producing cells, wreaking havoc on the control of blood sugar. But in people without diabetes, amylin doesn't misbehave; it actually pitches in to help with blood sugar regulation. What accounts for the difference?
Read more here.
- Covered in the News Service of the University of Michigan
Featured in "Nanotechnology Now." (See full article here)
"The research by scientists at the University of Michigan is reported in the Dec. 2 issue of the Journal of the American Chemical Society.
'If people think of bone at all—and they usually don't, until they have a fracture—they think of it as an inert material,' said Ayyalusamy Ramamoorthy, professor of chemistry and of biophysics. 'But like everything else, bone is also made up of molecules whose behavior is reflected in its structure, toughness and mechanical strength, making bone really exciting in terms of its chemistry and its contribution to health and well-being.'
Understanding the structure and structural changes of bone, a highly heterogeneous material with a complex hierarchical architecture, continues to be a significant challenge even for high-resolution solid-state NMR spectroscopy. While it is known that dehydration affects mechanical properties of bone by decreasing its strength and toughness, the underlying structural mechanism at the atomic level is unknown. Solid-state NMR spectroscopy, controlled dehydration, and H/D exchange were used for the first time to reveal the structural changes of an intact piece of bovine cortical bone."
Link to Journal of the American Chemical Society Paper: Time-Resolved Dehydration-Induced Structural Changes in an Intact Bovine Cortical Bone Revealed by Solid-State NMR Spectroscopy
"An enigmatic component of human semen, SEVI, semen-derived enhancer of virus infection, boosts infectivity of the human immunodeficiency virus (HIV) which causes AIDS. Since its discovery in 2007, researchers have been hoping to learn more about its structure with the aim of inhibiting its infection-promoting activity; NMR spectroscopy has now produced new clues.
Sexual intercourse is the major route to HIV transmission, but identifying the various biochemical and physical factors that allow some people to become infected with the virus more readily than others is an important focus of research into this potentially lethal disease.
In 2007, Frank Kirchhoff of the Institute of Virology, University Clinic of Ulm, in Germany, and colleagues reported in Cell (2007, 131, 1059-1071; 10.1016/j.cell.2007.10.014) screened a complex peptide/protein library derived from human semen and demonstrated that naturally occurring fragments of the abundant biomarker prostatic acidic phosphatase (PAP) can form tiny fibres of amyloid material..."
"University of Michigan researchers have developed new molecular tools that can be used to investigate the process. The molecules also hold promise in Alzheimer's disease treatment. The research, led by assistant professor Mi Hee Lim, was published online this week in the Journal of the American Chemical Society..."
We have solved the atomic-level resolution structure of the SEVI precursor PAP248−286 using NMR spectroscopy in SDS micelles, which serve as a model membrane system. PAP248−286, which does not disrupt membranes like most amyloid proteins, binds superficially to the surface of the micelle, in contrast to other membrane-disruptive amyloid peptides that generally penetrate into the core of the membrane. The structure of PAP248−286 is unlike most amyloid peptides in that PAP248−286 is mostly disordered when bound to the surface of the micelle, as opposed to the α-helical structures typically found of most amyloid proteins.
Related Links:Journal of the American Chemical Society paper, "NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP248-286 Biophysical Journal paper, "Helical Conformation of the SEVI Precursor Peptide PAP248-286, a Dramatic Enhancer of HIV Infectivity, Promotes Lipid Aggregation and Fusion"
Featured in Science Daily
"Scientists in Michigan are reporting discovery of the secret behind the fabled healing power of the main ingredient in turmeric — a spice revered in India as "holy powder.'..."
Featured in Science Daily
"Revered in India as 'holy powder,' the marigold-colored spice known as turmeric has been used for centuries to treat wounds, infections and other health problems. In recent years, research into the healing powers of turmeric's main ingredient, curcumin, has burgeoned, as its astonishing array of antioxidant, anti-cancer, antibiotic, antiviral and other properties has been revealed..."
Featured in The University Record
"By comparing the human form of IAPP to the rat version, which does not cause cell death, Associate Professor of Chemistry and Biophysics Ayyalusamy Ramamoorthy and co-workers showed that a difference of a single amino acid (protein building block) at a position designated as residue 18 accounts for the difference in toxicity..."
Featured in the University of Michigan News
"Ayyalusamy Ramamoorthy and co-workers show in the new study that membrane damage can occur independently of amyloid formation and that the protein involved, known as Islet Amyloid Polypeptide Protein (IAPP), has separate regions responsible for amyloid formation and membrane disruption..."
Featured in The University Record and the University of Michigan News Service
"When is a biological membrane like a U-M football game? Always, if you ask associate professor of chemistry and biophysics and diehard football fan Ayyalusamy Ramamoorthy, who illustrates his lectures and scientific papers with maize-and-blue, gridiron-inspired images..."
"By mimicking a brick-and-mortar molecular structure found in seashells, University researchers created a composite plastic that's as strong as steel but lighter and transparent..."
Featured in Science Daily and The University Record
"Using atom-level imaging techniques, University researchers have revealed important structural details of an enzyme system known as "Mother Nature's blowtorch" for its role in helping the body efficiently break down many drugs and toxins..."
Featured in Science/Technology ACS Meeting News
"WHAT DO YOU GET when you cross a frog with a nonstick frying pan? The answer: antibiotics with fluorinated amino acids..."
Featured in The University Record
"Frog skin and human lungs hold secrets to developing new antibiotics, and a technique called solid-state NMR spectroscopy is a key to unlocking those secrets. That's the view of U-M researcher Ayyalusamy Ramamoorthy, who was scheduled to discuss his group's progress toward that goal March 3 at the annual meeting of the Biophysical Society in Baltimore, Md..."
Featured in The University Record
"U-M researchers will develop a module to deliver drugs directly to tumor cells, using a manmade polymer molecule called a dendrimer that is small enough to slip through tiny openings in cell membranes. The dendrimer module will be joined to another polymer, which will allow researchers to target cancer cells for imaging or treatment..."