Hexbyte Glen Cove Graphene sensor rapidly detects opioid metabolites in wastewater

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Hexbyte Glen Cove Change of scenery: New research outlines how recreation will shift with climate change in the west

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Building resilience in outdoor recreation systems will take careful planning, according to new research. Winter-based recreation sites may need to expand operations to include shoulder- and summer-based activities in order to stay viable in a warming climate. Summer operations may need to adjust budgets and staffing for longer seasons, and be better prepared for extreme temperatures. Credit: Stefan Haehnel

Change can be hard, especially when it involves soaring summer temperatures, mega-droughts, invasive species and other items from the list of unpleasant outcomes of climate change. There are innumerable economic and social implications from a changing climate—but in the Western U.S. where skiing, hiking, biking, hunting and other forms of outdoor recreation are core to many people’s lives, and where local economies rely on income generated by these activities, the impacts are already difficult to ignore.

New research from the Institute of Outdoor Recreation and Tourism, works to define what, specifically, the changing will mean for the future of outdoor recreation in the West. The lesson at the heart of the review is that adaptation will be a critical skill as the new climate offers unpredictable scenarios to individuals, , land-management infrastructures and long-term planners. The review, published in the Journal of Forestry, compiles the existing research that explores the ways in which climate change alters the types and timing of outdoor recreation activities, and the indirect effects of these shifts on everything from bear populations to new problems with seasonal staffing.

Campsites that are too hot, with fluctuating snowpacks, rivers with low water levels, and forests crowned with a halo of wildfire smoke all affect the number of people who participate in outdoor recreation and the quality of their experiences. These impacts change the way people move through the landscape, value the experience and spend their money—but the specifics can be hard to define. For instance, if a campsite is too smokey, one group of recreationists may decide to drive further to reach an alternate site. Another might wait until the smoke clears, and another might choose to give up a particular activity altogether and go home. In the paper, the researchers provide activity-specific adaptation strategies that can be used to plan for these consequences (for instance, increasing capacities of existing outdoor recreation settings, adjusting season lengths, or improving communications to manage visitors’ expectations).

“Land managers can prepare for climate change by learning the best strategies for adaptation, as we currently understand them,” said Anna Miller, lead author on the study. “Learning from past successes and failures when responding to things like can help managers better understand what’s going to best help them adapt to change—if and when it happens again.”

Building resilience in outdoor recreation systems will take careful planning, according to the research. For example, developing collaborations and communication strategies between agencies within a local region right now will allow managers to respond more effectively as new situations arise. Managers also need to carefully consider how adaptation strategies can improve equitable access to recreation opportunities.

Winter-based recreation sites may need to expand operations to include shoulder- and summer-based activities in order to stay viable in a warming climate. Summer operations may need to adjust budgets and staffing for longer seasons, and be better prepared for extreme temperatures. Wildlife and forest-product-gathering activities will have to build in flexibility and prepare for fundamental changes in the ecosystem as well. 

“We may not know precisely what’s in store for managers in the next decades,” said Miller, “but using our collective experience can help us learn how to adapt planning for the most likely futures.”

More information:
Anna B Miller et al, Climate Change and Recreation in the Western United States: Effects and Opportunities for Adaptation, Journal of Forestry (2022). DOI: 10.1093/jofore/fvab072

Change of scenery: New research outlines how recreation will shift with climate change in the west (2022, February 25)
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Hexbyte Glen Cove How much energy does a dolphin use to swim?

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Researchers use noninvasive movement tags and a device that measures oxygen consumption to assess how much energy a dolphin uses while swimming. Credit: Dolphin Quest

From foraging for prey to evading predators, ship strikes or other dangers, a dolphin’s survival often hinges on being able to crank up the speed and shift its swimming into high gear.

But burning all that rubber burns a lot of energy too, which, over time, can deplete reserves vital for growth, health and reproduction if the animal’s movements use more calories than it can take in.

Being able to estimate these of locomotion (COL) and determine where the metabolic tipping point might be is essential for answering fundamental questions about dolphin physiology and ecology, and for understanding the impacts of human disturbance on them. Because measuring costs of locomotion in dolphins in the wild is extremely difficult, past studies have estimated it based on the number of fluke stokes per minute. Since not all fluke strokes are the same size, it’s an imprecise measure of swimming effort.

A new Duke University-led study provides a more reliable way to estimate energy costs in dolphins by using overall dynamic body acceleration (ODBA), an integrated measure of all body motions a dolphin makes during swimming.

“Researchers have used movement tags to measure ODBA in other species, but this is the first published study calibrating ODBA with energy expenditure in multiple dolphins,” said study leader Austin Allen, a postdoctoral researcher in marine biology at Duke’s Nicholas School of the Environment. The work appears Feb. 24 in Journal of Experimental Biology.

As a proxy for measuring cost of locomotion in wild animals, Allen and his colleagues conducted swim trials on six trained bottlenose dolphins at Dolphin Quest, a zoological facility on Oahu, Hawaii, during May 2017, 2018, and 2019.

Using a non-invasive device known as a pneumotachometer, they measured each dolphin’s oxygen consumption while at rest and immediately after it swam an 80-meter underwater lap across a lagoon. Non-invasive biologging tags were also used to record each animal’s three-dimensional body motions over each section of the trial—such as when it was slowing down to make a turn or speeding up mid-lap.

By analyzing the collected data, a pattern began to emerge.

“There was some individual variation, but, overall, the results showed significant correlation between and body acceleration, which suggests ODBA can be a reliable proxy for COL,” Allen said.

“Working with dolphins in zoos or aquariums is allowing us to use data we’ve already collected using these tags in the field to evaluate the cost of in wild populations,” he said.

More information:
Austin S. Allen et al, Dynamic body acceleration as a proxy to predict the cost of locomotion in bottlenose dolphins, Journal of Experimental Biology (2022). DOI: 10.1242/jeb.243121

How much energy does a dolphin use to swim? (2022, February 24)
retrieved 25 February 2022
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Hexbyte Glen Cove New therapy breakthrough changes the shape of treatment for undruggable diseases

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DUBTACs are heterobifunctional molecules consisting of a protein-targeting ligand linked to a DUB recruiter via a linker. DUBTACs are ideally used for stabilizing the levels of actively ubiquitinated proteins that are degraded by the proteasome. Credit: Nomura Lab

For some time, scientists have been working on the major challenge of developing new therapies against many human diseases. Many of these diseases are caused by the abberant action of certain proteins in our cells that are considered “undruggable,” or difficult to therapeutically target using classical drug discovery methods. A major class of “undruggable” proteins are those that are aberrantly degraded and destroyed in the cell leading to many human diseases, including cancer, neurodegenerative diseases, metabolic diseases, and hundreds of genetic disorders.

These proteins are frequently destroyed through tagging with chains of a protein known as ubiquitin, which signals the cell to destroy the proteins through the “cellular trash can” called the proteasome.

While these proteins would benefit therapeutically by stopping their destruction and stabilizing and increasing the levels of the actively destroyed proteins, targeted protein stabilization of an actively degraded protein with a small-molecule drug has thus far remained impossible or “undruggable.”

Now, a team of researchers from the lab of Daniel Nomura, Professor of Chemical Biology and Director of the Novartis-Berkeley Center for Proteomics and Chemistry Technologies at UC Berkeley, in collaboration with researchers from the Novartis Institutes for BioMedical Research have reported the discovery of a new therapeutic paradigm called Deubiquitinase Targeting Chimeras (DUBTACs) to address the challenge of targeted protein stabilization.

DUBTACs are dumbbell shaped molecules that consist of a that binds to the disease-causing protein linked via a linker to another chemical recruiter of an enzyme called deubiquitinase or DUB. The DUB removes the ubiquitin chains from actively degraded proteins, thus preventing their destruction and stabilizing their protein levels.

In new research published in Nature Chemical Biology, the researchers report on how DUBTACs stabilize the mutant form of the CFTR chloride channel protein that is otherwise degraded to cause the debilitating disease . Cystic fibrosis was chosen as the initial test case for DUBTACs as this disease is caused by mutations in the CFTR channel which cause this protein to become unstable and actively degraded, leading to the cystic fibrosis pathology. The researchers postulated that a DUBTAC against mutant CFTR could stabilize and increase the levels of this mutant protein to restore CFTR function in cystic fibrosis patients.

The research has demonstrated that the CFTR DUBTAC restores chloride channel function in primary human bronchial epithelial cells from cystic fibrosis patients compared to currently approved therapies. The researchers also showed that a DUBTAC could be applied to cancers as well. They developed a DUBTAC to stabilize a tumor suppressor WEE1 kinase. WEE1 kinase is actively degraded in many tumors to promote cancer cell proliferation. Stabilizing the levels of WEE1 kinase in cancer cells could stop tumor growth.

Prof. Nomura states, “We believe that this new DUBTAC therapeutic platform can be used to develop a new class of medicines against many human diseases, including cancer, , and many genetic disorders by enabling access to these previously “undruggable” proteins that were actively degraded to drive these diseases.”

More information:
Nathaniel J. Henning et al, Deubiquitinase-targeting chimeras for targeted protein stabilization, Nature Chemical Biology (2022). DOI: 10.1038/s41589-022-00971-2

New therapy breakthrough changes the shape of treatment for undruggable diseases (2022, February 24)
retrieved 25 February 2022
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Hexbyte Glen Cove More intense roasting of cocoa beans lessens bitterness, boosts chocolate liking

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Credit: Pixabay/CC0 Public Domain

Confection makers who want to develop products containing 100% chocolate and no sugar for health-conscious consumers can reduce bitterness and optimize flavor acceptance by roasting cocoa beans longer and at higher temperatures.

That’s the conclusion of a team of researchers who conducted a new study in Penn State’s Sensory Evaluation Center in the Department of Food Science. The study involved 27 100%- preparations made from cocoa beans roasted at various intensities and 145 people who came to the center on five consecutive days, evaluating five different samples each day.

The research confirmed that bitterness and astringency are negatively correlated to consumer liking, and demonstrated that those qualities in chocolate can be reduced through optimizing roasting, according to research team member Helene Hopfer, Rasmussen Career Development Professor in Food Science in the College of Agricultural Sciences.

“More and more people these days are eating darker chocolates with less sugar and more cacao because they are trying to cut down on sugar intake or they want to take advantage of perceived health benefits,” she said. “Dark chocolate is particularly high in flavonoids, particularly a subtype called flavan-3-ols and their oligomers, which are all considered functional ingredients due to their associated health effects.”

However, unsweetened chocolate is too bitter for most people to enjoy, so researchers experimented with roasting treatments to modify the flavor—investigating more than basic tastes such as sour and bitter—making it more acceptable for consumers, Hopfer explained.

For the study, research team member Alan McClure, founder of craft chocolate company Patric Chocolate and related consultancy Patric Food & Beverage Development, partnered with Hopfer and Penn State to characterize the flavor and acceptability of the chocolates.

Part of his doctoral degree dissertation research, McClure chose cocoa beans from three origins—Madagascar, Ghana and Peru, harvested in 2018 and 2019. He roasted and ground all samples into cocoa liquor at his factory in Columbia, Missouri, and then shipped the solidified 100% chocolate to Penn State, where he and Hopfer remelted and portioned out the chocolates into small disks for sensory evaluation.

McClure found the reaction of study participants to his 27 100% chocolate preparations especially interesting, and he suggested that what he learned from this research will guide him, and roasting staff at other chocolate manufacturing companies, in creating future products through an increased scientific understanding of the complex changes resulting from cocoa roasting.

In findings published in Current Research in Food Science, the researchers reported that more intense roasting conditions—such as 20 minutes at 340 degrees Fahrenheit, 80 min at 275 F, and 54 min at 304 F—all led to chocolate consumers finding unsweetened chocolate the most acceptable. Conversely, research participants did not find 100% chocolate acceptable when made from raw or lightly roasted cacao, such as beans roasted 11 minutes at 221 F, or 55 minutes at 147 F.

Hopfer noted that scientists’ understanding of the variation of cacao-related bitterness has historically come from instrumental investigation of the bitter compounds found in , but the Penn State research is novel because of its use of human sensory evaluation to quantify such variation.

“Our research was intended to learn about bitterness perception and the liking of chocolate made from cacao roasted with a variety of roasting profiles to see if wide consumer acceptability of 100% chocolate is possible,” she said.

“A chocolate maker doesn’t have many other options to influence the flavor quality of 100% chocolate except to vary how he or she roasts the beans, and our results show optimal roasting can adequately reduce bitterness.”

More information:
Alan P. McClure et al, Optimizing consumer acceptability of 100% chocolate through roasting treatments and effects on bitterness and other important sensory characteristics, Current Research in Food Science (2022). DOI: 10.1016/j.crfs.2022.01.005

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Hexbyte Glen Cove Live wire: New research on nanoelectronics

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Credit: ACS

Proteins are among the most versatile and ubiquitous biomolecules on earth. Nature uses them for everything from building tissues to regulating metabolism to defending the body against disease.

Now, a new study shows that proteins have other, largely unexplored capabilities. Under the right conditions, they can act as tiny, current-carrying wires, useful for a range human-designed nanoelectronics.

In new research appearing in the journal ACS Nano, Stuart Lindsay and his colleagues show that certain proteins can act as efficient electrical conductors. In fact, these tiny protein wires may have better conductance properties than similar nanowires composed of DNA, which have already met with considerable success for a host of human applications.

Professor Lindsay directs the Biodesign Center for Single-Molecule Biophysics. He is also professor with ASU’s Department of Physics and the School of Molecular Sciences.

Just as in the case of DNA, proteins offer many attractive properties for nanoscale electronics including stability, tunable conductance and vast information storage capacity. Although proteins had traditionally been regarded as poor conductors of electricity, all that recently changed when Lindsay and his colleagues demonstrated that a protein poised between a pair of electrodes could act as an efficient conductor of electrons.

The new research examines the phenomenon of electron transport through proteins in greater detail. The study results establish that over long distances, display better conductance properties than chemically-synthesized nanowires specifically designed to be conductors. In addition, proteins are self-organizing and allow for atomic-scale control of their constituent parts.

Synthetically designed protein nanowires could give rise to new ultra-tiny electronics, with potential applications for medical sensing and diagnostics, nanorobots to carry out search and destroy missions against diseases or in a new breed of ultra-tiny computer transistors. Lindsay is particularly interested in the potential of protein nanowires for use in new devices to carry out ultra-fast DNA and protein sequencing, an area in which he has already made significant strides.

In addition to their role in nanoelectronic devices, charge transport reactions are crucial in living systems for processes including respiration, metabolism and photosynthesis. Hence, research into transport properties through designed proteins may shed new light on how such processes operate within living organisms.

While proteins have many of the benefits of DNA for nanoelectronics in terms of electrical conductance and self-assembly, the expanded alphabet of 20 used to construct them offers an enhanced toolkit for nanoarchitects like Lindsay, when compared with just four nucleotides making up DNA.

Transit Authority

Though electron transport has been a focus of considerable research, the nature of the flow of electrons through proteins has remained something of a mystery. Broadly speaking, the process can occur through electron tunneling, a quantum effect occurring over very short distances or through the hopping of electrons along a peptide chain—in the case of proteins, a chain of amino acids.

One objective of the study was to determine which of these regimes seemed to be operating by making quantitative measurements of electrical conductance over different lengths of protein nanowire. The study also describes a mathematical model that can be used to calculate the molecular-electronic properties of proteins.

For the experiments, the researchers used protein segments in four nanometer increments, ranging from 4-20 nanometers in length. A gene was designed to produce these from a DNA template, with the protein lengths then bonded together into longer molecules. A highly sensitive instrument known as a scanning tunneling microscope was used to make precise measurements of conductance as electron transport progressed through the protein nanowire.

The data show that conductance decreases over nanowire length in a manner consistent with hopping rather than tunneling behavior of the electrons. Specific aromatic amino acid residues, (six tyrosines and one tryptophan in each corkscrew twist of the protein), help guide the electrons along their path from point to point like successive stations along a train route. “The electron transport is sort of like skipping stone across water—the stone hasn’t got time to sink on each skip,” Lindsay says.

Wire wonders

While the conductance values of the protein nanowires decreased over distance, they did so more gradually than with conventional molecular wires specifically designed to be efficient conductors.

When the protein nanowires exceeded six nanometers in length, their conductance outperformed molecular nanowires, opening the door to their use in many new applications. The fact that they can be subtly designed and altered with atomic scale control and self-assembled from a gene template permits fine-tuned manipulations that far exceed what can currently be achieved with conventional transistor design.

One exciting possibility is using such protein nanowires to connect other components in a new suite of nanomachines. For example, could be used to connect an enzyme known as a DNA polymerase to electrodes, resulting in a device that could potentially sequence an entire human genome at low cost in under an hour. A similar approach could allow the integration of proteosomes into nanoelectronic devices able to read amino acids for protein sequencing.

“We are beginning now to understand the electron transport in these proteins. Once you have quantitative calculations, not only do you have great molecular electronic components, but you have a recipe for designing them,” Lindsay says. “If you think of the SPICE program that electrical engineers use to design circuits, there’s a glimmer now that you could get this for electronics.”

More information:
Bintian Zhang et al, Electronic Transport in Molecular Wires of Precisely Controlled Length Built from Modular Proteins, ACS Nano (2022). DOI: 10.1021/acsnano.1c10830

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