Biosensors measure the concentration of molecules in biological samples for biomedical, environmental, and industrial applications, and, ideally, they should provide real time, continuous data. However, the continuous monitoring of small molecules at low concentrations is problematic. Researchers at Eindhoven University of Technology have developed an innovative sensing approach based on molecular lookalikes. This could prove pivotal in future biosensors for monitoring health and disease.
The field of biosensors has a rich and inventive history. The “father of biosensors” is seen by many to be Leland C. Clark Jr., who designed a sensor to measure oxygen in blood in the early 1960s.
However, as happens in pioneering works, things didn’t start out as he had hoped. His initial sensor designs failed because blood components affected the sensing electrode.
Clark’s solution was to separate the electrode and the blood by a cellophane wrapper from a cigarette packet,
Using the model Orobanchaceae parasitic plant Phtheirospermum japonicum, scientists from Nagoya University and other research institutes from Japan have discerned the molecular mechanisms underlying plant parasitism and cross-species grafting, pinpointing enzyme β-1,4-glucanase (GH9B3) as an important contributor to both phenomena. Targeting this enzyme may help control plant parasitism in crops. Also, this mechanism can be exploited for novel cross-species grafting techniques to realize the goal of sustainable agricultural technologies.
Plant parasitism is a phenomenon by which the parasite plant latches onto and absorbs water and nutrients from a second host plant, with the help of a specialized organ called the “haustorium.” Once the haustorium forms, specific enzymes then help in forming a connection between the tissues of the parasite and host plants, known as a “xylem bridge,” which facilitates the transport of water and nutrients from the host to the parasite.
By applying natural language processing tools to the movements of protein molecules, University of Maryland scientists created an abstract language that describes the multiple shapes a protein molecule can take and how and when it transitions from one shape to another.
A protein molecule’s function is often determined by its shape and structure, so understanding the dynamics that control shape and structure can open a door to understanding everything from how a protein works to the causes of disease and the best way to design targeted drug therapies. This is the first time a machine learning algorithm has been applied to biomolecular dynamics in this way, and the method’s success provides insights that can also help advance
The surface of metals plays a key role in many technologically relevant areas, such as catalysis, sensor technology and battery research. For example, the large-scale production of many chemical compounds takes place on metal surfaces, whose atomic structure determines if and how molecules react with one another. At the same time, the surface structure of a metal influences its electronic properties. This is particularly important for the efficiency of electronic components in batteries. Researchers worldwide are therefore working intensively on developing new kinds of methods to tailor the structure of metal surfaces at the atomic level.
A team of researchers at the University of Münster, consisting of physicists and chemists and led by Dr. Saeed Amirjalayer, has now developed a molecular tool which makes it possible, at the atomic level, to change the structure of a metal surface. Using computer simulations, it was possible to predict that the restructuring of
We hear sounds in part because tiny filaments inside our inner ears help convert voices, music and noises into electrical signals that are sent to our brains for processing. Now, scientists have mapped and simulated those filaments at the atomic level, a discovery that shed lights on how the inner ear works and that could help researchers learn more about how and why people lose the ability to hear.
The findings, published last week in the Proceedings of the National Academy of Sciences, involve very fine filaments in the inner ear called tip links. When sound vibrations reach the inner ear, the vibrations cause those tip links to stretch and open ion channels of sensory cells within the inner-ear cochlea, a tiny snail-shaped organ that allows our brains to sense sound. When tip links open those channels, that act triggers the cochlear electrical signals that we interpret as sound.
Viral and bacterial pathogens wield pathogenic or virulent proteins that interact with high-value targets inside human cells, attacking what is known as the host interactome. The host interactome is the network map of all the protein-protein interactions inside cells.
Such networks have been studied in organisms as diverse as plants, humans and roundworms, and they show a similarity to social networks like Facebook or airline route maps. In Facebook, a few people will have a huge number of friend connections, some will have many, and a vast majority will have much fewer. Similarly, airlines have a few hubs that many passengers pass through on the way to their destinations.
Host interactomes show a limited number of high-powered hubs — where a protein has a large number of connections — and a limited number of important bottlenecks, which are sites with a large number of short paths to a node. These