Latest news with #JournaloftheAmericanChemicalSociety
News18
02-07-2025
- Health
- News18
Is Your Own Collagen Secretly Fueling Diabetes In You? IIT Study Uncovers Startling New Link
Last Updated: Scientists at IIT Bombay have found collagen protein helps form harmful hormone clumps in the pancreas, advancing understanding and opening doors to new diabetes treatments Diabetes is increasingly becoming a global health concern, with experts warning it may reach epidemic proportions in the coming decades. The disease primarily manifests in two forms: Type 1, an autoimmune condition with genetic links, and Type 2, whose precise causes remain largely unknown. In a groundbreaking study, researchers at IIT Bombay have uncovered a surprising connection between collagen, the body's most abundant structural protein, and the progression of Type 2 diabetes. Collagen appears to promote the accumulation of a hormone called amylin within the pancreas, impairing its function by reducing insulin production and thereby elevating blood sugar levels. The study, published in the Journal of the American Chemical Society, explains that alongside insulin, the body produces amylin to regulate blood sugar after meals. However, abnormal amylin can clump together as amyloid aggregates, damaging pancreatic beta cells and worsening diabetes. Professor Shamik Sen and his team revealed that fibrillar collagen 1 encourages the formation of these harmful clumps, increasing the risk of Type 2 diabetes. This new insight highlights the crucial role of structural proteins in diabetes development, beyond just blood sugar levels. These findings could lead to innovative treatments aimed at restoring pancreatic health by managing collagen and amylin levels, offering fresh hope to millions affected by Type 2 diabetes.
Yahoo
21-05-2025
- Science
- Yahoo
Single-Atom Quantum Computer Achieves Breakthrough Molecular Simulations
A single atom has performed the first full quantum simulations of how certain molecules react to light. The researchers who carried out the feat say that their minimalistic approach could dramatically speed the path towards a 'quantum advantage' — when quantum computers will be able to predict the behaviour of chemicals or materials in ways that are beyond the reach of ordinary computers. 'The key advantage of this approach is that it is incredibly hardware-efficient,' says Ting Rei Tan, an experimental quantum physicist at the University of Sydney. The single atom can encode the information that is normally spread across a dozen or so 'qubits', the computational units used in most quantum computers. The findings were published on 14 May in the Journal of the American Chemical Society. No quantum computer had simulated this level of complexity in the energy levels of molecules before, says Alán Aspuru-Guzik, a computational chemist at the University of Toronto in Canada. 'This is a tour-de-force that will remain in the history books.' [Sign up for Today in Science, a free daily newsletter] Tan and his colleagues simulated the behaviour of three different organic molecules, allene, butatriene and pyrazine, when they are hit with an energetic particle called a photon. When this happens, it triggers a cascade of events in the molecule that affects both how its atoms move with respect to each other — vibrating like balls connected by springs — and how its electrons jump to higher-energy, or excited, states. Understanding the precise sequence of these events can help chemists to design molecules that channel energy in the most useful or efficient way, for example in solar panels or in sunscreen lotion. The researchers found a way to encode these different parameters into a single ytterbium ion trapped in a vacuum using pulsating electric fields: the excitations of the molecule's electrons corresponded to similar excitations in one of the ion's electrons, and two different vibrational modes were represented by the ion wiggling inside its trap in two different directions. The team also nudged the ion with laser pulses to tailor how all of the states interacted with one another. This forced the ion to evolve over time, meaning it could mimic how the corresponding molecules act after being hit by a photon. The team then read off the state of the virtual molecules at a sequence of different stages by measuring the changing probability that the ion's electron was in an excited state over time. The results matched what was known about these three molecules, which validates the approach, Tan says. Allene, butatriene and pyrazine are still simple enough to be studied with ordinary computer simulations, but these run out of steam when they have to embody 20 or so vibrational modes, which is not uncommon for more complex molecules. Kenneth Brown, a quantum engineer at Duke University in Durham, North Carolina, calls the study 'great work', and says that it's the first time that researchers have shown how to tune such a technique to mimic the properties of specific molecules. Simulating the chemistry of molecules and materials is often described as one of the most promising uses for quantum computers — but one that will produce useful results only once the machines have scaled up to many millions of qubits. Tan and his collaborators predict that with their approach, a quantum computer could be able to do useful simulations using only a few dozen ions. This article is reproduced with permission and was first published on May 16, 2025.
Hans India
09-05-2025
- Health
- Hans India
CCMB researchers discover key role of protein agility in binding to different molecular partners
Hyderabad: Scientists at the Centre for Cellular and Molecular Biology (CCMB) have recently made a significant discovery: proteins can perform multiple functions by temporarily changing their shape, not only based on their fixed three-dimensional structure but also through their flexibility. The study, published in the Journal of the American Chemical Society, reveals that two structurally identical plant proteins exhibit different substrate specificities, allowing them to recognise distinct substrates. The key difference is that one of the proteins is more flexible than the other. This enhanced flexibility enables it to bind to various types of RNA molecules, as the protein can dynamically rearrange its structure to align with the shape of its partner molecules. This property is crucial for gene regulation. Using nuclear magnetic resonance (NMR) spectroscopy and advanced computational methods, researchers identified transient protein structures that constitute only 1 per cent of the total protein. These structures, which briefly change shape, play a vital role in recognising different RNA forms. 'We demonstrated that a protein's ability to change shape slightly is just as important as its stable structure,' said lead author Dr Mandar V Deshmukh. Through these transient dynamic states, proteins can function efficiently in the complex conditions of the cellular environment, helping organisms to regulate their genes properly under changing circumstances. This discovery could lead to revolutionary advancements in drug design and the improvement of plant traits in the future.' The study also revealed that changes in a few amino acids in non-active site residues of a protein can result in significant functional differences. This underscores the importance of comprehensively studying both structure and dynamics, particularly in the development of drug target proteins. 'The ability of some proteins to perform multiple functions, known as functional promiscuity, reflects one of Nature's originalities,' noted Debadutta Patra and Jaydeep Paul, joint first authors of the study. The research highlights how plants precisely control RNA processing using fewer proteins and without the need for an adaptive immune system. Scientists believe this study could pave the way for new discoveries in medicine, agriculture, and biotechnology.
The Hindu
07-05-2025
- Science
- The Hindu
CCMB scientists discover proteins flexibility, could lead to new advances in medicine
Scientists at the CSIR-Centre for Cellular and Molecular Biology (CCMB) have shown that proteins do not always rely on their fixed three-dimensional shape for function, but their structures are flexible to carry out multiple tasks. These findings have the potential to pave the way for new advances in medicine, agriculture and biotechnology in helping scientists to design proteins that can multitask more efficiently, said an official release on Wednesday. In a latest study, scientists — Mandar V. Deshmukh, Debadutta Patra and Jaydeep Paul — using a powerful Nuclear Magnetic Resonance (NMR) spectroscopy and computational methods, have detected tiny populations of protein structures (just 1%) that switch into different shapes for short periods. These rare shifts are vital for recognising different RNA forms and help explain how plants manage complex gene control. 'What we have shown is that a protein's ability to change shape, even slightly, can be just as important as its structure,' said lead author Mr. Deshmukh. 'By capturing the fleeting, dynamic states of these proteins, we have shown that their ability to rearrange their structure transiently gives them a functional edge in complex cellular environments,' he said. 'This enables organisms to regulate genes efficiently under varying conditions and could change the way we think about designing new medicines or improving plant traits,' added the scientist. The study shows how subtle changes in a protein's sequence can lead to significant differences in function, emphasising the need for a combined study of both structure and dynamics, particularly for proteins that are drug targets. 'Our results reveal nature's originality in designing a unique approach to grant promiscuity to a few proteins,' remarked joint first authors of the study Mr. Patra and Mr. Paul. This study, published in the latest issue of 'Journal of the American Chemical Society', also offers a plausible explanation for how plants fine-tune RNA processing without expanding their protein repertoire, added the press release.
Observer
18-02-2025
- Science
- Observer
Sweet: Study reveals what Egyptian mummies smelled like
Ancient Egyptian mummies mostly smelled "woody,""spicy" and "sweet," according to research published in the Journal of the American Chemical Society on Thursday. Researchers analysed nine mummified bodies from the Egyptian Museum in Cairo, most of which date from the 1st and 2nd millennium BC,using a combination of tools and sensory techniques, in what they said is the first study of its kind. "The smell of mummified bodies has for years attracted significant interest from experts and the general public, but no combined chemical and perceptual scientific study has been conducted until now," said lead author Professor Matija Strli from UniversityCollege London (UCL) and the University of Ljubljana. "This ground-breaking research really helps us better plan conservation and understand the ancient embalming materials. It add sanother layer of data to enrich the museum exhibition of mummified bodies." The researchers deployed a panel of trained human "sniffers" tasked with describing the smells' quality, intensity and pleasantness as well as measuring the molecules and compounds involved using methods such as gas chromatography and mass spectrometry. This enabled the team to determine whether these components originated from preservatives, microorganisms or pesticides, for example. The experts qualified the remains mostly as "hedonically pleasant with 'balsamic' descriptors ('heavy', 'sweet', 'woody' odors),"according to the study. The smells were described as "woody" in 78% of the case studies,"spicy" in 67%, and "sweet" in 56%, while "incense-like" and "stale,rancid" got 33% each. UCL's Dr Cecilia Bembibre said the research highlights the"importance of using our senses to understand the past." Mummification in ancient Egypt normally involved treating the body with oils and resins, including those of pine, cedar and juniper, to preserve the body and soul in the afterlife and give it a pleasant smell. —dpa
