In a discovery that points to potential new antibiotic medicines, scientists from Rice University and the University of Michigan have deciphered the workings of a common but little-understood bacterial switch that cuts off protein production.
Scientists have found a new way of joining groups of atoms together into shape-changing molecules -- opening up the possibility of a new area of chemistry and the development of countless new drugs, microelectronics and materials. Discoveries of new ways to make isomers -- molecules made of the same atoms connected together differently -- were last reported in 1961 and before then in 1914. Proof-of-principle and prototype demonstration of this important finding are expected within 30 months.
A rare genetic disorder in which people are suddenly overcome with profound weakness or temporary paralysis is caused by a hole in a membrane protein that allows sodium ions to leak across cell membranes. The results of a new study reveal the mechanisms of periodic paralysis at the atomic level and suggest designs for drugs that may prevent this ion leak and provide relief to these patients
This vision of simplifying disease diagnosis using topically applied nanotechnology could change the way skin diseases such as abnormal scars are diagnosed and managed.
For women, mammograms are a sometimes uncomfortable, but necessary, annual ritual. But this procedure doesn't always provide accurate results, and it exposes women to X-rays. In a study appearing in ACS' journal Molecular Pharmaceutics, scientists report that they have developed a non-invasive 'disease screening pill' that can make cancerous tumors light up when exposed to near-infrared light in mice without using radiation.
Penicillin-based antibiotics contain a five-membered hydrocarbon cycle, additionally incorporating a sulfur and a nitrogen atom. Nadine Zumbrägel, doctoral student at the Chair of Organic Chemistry I at Bielefeld University, has succeeded in selectively synthesizing this important substructure with different residues on this cycle using a biotechnological method.
Motion is crucial for proper functioning of a kinase enzyme, a University of Arizona-led research team found. Not only must the kinase have all needed parts in place, the enzyme must move in the correct manner and at the correct speed to function properly in a cell. Focusing on ways to impede the enzyme's motion may be an avenue for developing new drugs to combat cancer and other diseases.
In the race to create more potent and stable medicines, scientists know that adding fluorine can improve drug molecules. However, there is only one fluorination reaction known to occur in nature. And this process is performed by complex and highly specialized enzymes that are difficult to replicate. Now, scientists have developed a new, streamlined molecule that can do the work of enzymes but be designed and controlled minutely. This new catalyst transforms a safe, affordable fluoride salt into fluorinated organic molecules.
Researchers have lab-tested a molecule that can combat the common cold virus by preventing it from hijacking human cells.
The development of this method will allow one to get previously inaccessible compounds and to study their biological activity. The work of the young researcher has been published in the authoritative international journal Tetrahedron Letters, which presents the latest achievements in organic synthesis, biochemistry, and medicinal chemistry.