Brookhaven Science Associates, the company that operates and manages the U.S. Department of Energy’s Brookhaven National Laboratory (BNL), and Biosurface Engineering Technologies, Inc. (BioSET), have been issued a U.S. patent on a synthetic peptide, called B2A.

Dr. Sonia Oliani and colleagues at São Paulo State University have identified a potential new molecule that inhibits inflammation, receptor for formylated peptides-2 (FPR-2). These findings are presented in the January 2009 issue of The American Journal of Pathology.

Scientists have identified a new antitumor drug that might prove useful in developing treatments for a multiple human cancers.

Determining the structure of unknown natural compounds is a slow and expensive part of drug screening and development – but this may now change thanks to a new combination of experimental and computational protocols developed at the University of California, San Diego and presented at RECOMB 2008 (Research in Computational Molecular Biology) on March 31 in Singapore.

Discovery by Hebrew University of Jerusalem researchers of a new communication factor that enables bacteria to “talk to each other” and causes their death could have significant consequences leading to development of a new class of antibiotic medications.

Researchers in Australia have developed a “switchable” detergent with a wide range of potential applications — from a laundry detergent that hardly needs a rinse cycle to a non-irritating eye rinse to increasing the amount of oil that companies can extract from a well.

The National Institute of Standards and Technology (NIST) has issued its first-ever reference material designed to improve the performance and reliability of experiments to measure the masses and concentrations of peptides in biomolecular samples. The new reference material is expected to be an important tool in the analysis of proteins, both for disease diagnosis and drug discovery.

UCLA AIDS Institute researchers have discovered that when a crucial portion of a peptide structure in monkeys that defends against viruses, bacteria and other foreign invaders is reversed, the peptide actually encourages infection with HIV.

UCLA AIDS Institute researchers have discovered that when a crucial portion of a peptide structure in monkeys that defends against viruses, bacteria and other foreign invaders is reversed, the peptide actually encourages infection with HIV.

Proteins, which form much of the molecular machinery required for life, are the targets of most drug molecules. One third of all proteins are membrane proteins - embedded within the cell's fatty outer layer. While scientists can easily study the other two-thirds using such tools as antibodies, they have not had such methods to investigate the membrane-embedded portions of proteins.

New peptide boosts body's own immunity
Imagine the desperation of trying to fight lethal infections when antibiotics fail to work.