Articles tagged with Polypeptides
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Metabolic bariatric surgery shows promise as a cost-effective weight loss option for class II and III obesity patients. The study found bariatric surgery resulted in greater weight loss compared to GLP-1 receptor agonists.
Researchers developed a novel biomaterial called elastin domain-derived protein (EDDP) that overcomes natural elastin limitations. EDDP promotes cell adhesion and growth, aiding tissue regeneration in damaged tissues like heart valves, blood vessels, or torn ligaments.
Researchers at the University of Illinois Chicago have uncovered the detailed chemical mechanism behind preventing premature protein release. The discovery sheds light on how cells execute protein production, one of life's most essential processes, and clarifies the role of the release factor.
Two previously unknown ribosome-arresting peptides (RAPs), PepNL and NanCL, were identified in E. coli, inducing translation arrest through a unique mini-hairpin conformation in the exit tunnel of the ribosome. This discovery provides valuable insights into deciphering the hidden genetic codes within polypeptide sequences.
A study estimates that approximately one-third of eligible US adults without diabetes were excluded from clinical trials supporting GLP-1 and GLP-1/GIP medications. The FDA should consider updating labeling to advise caution on generalizing these medications' safety and effectiveness to excluded populations.
Researchers explore how side-chain modifications affect coacervation properties of homopolypeptides. They find that varying side-chain lengths and hydrophobicity impact coacervation, while charge reversal affects properties. These findings provide insights into the structure-property relationships of coacervate-forming proteins.
Researchers investigated peptide clumping behavior using molecular dynamics simulations and AI techniques. They discovered that aromatic amino acids enhance aggregation, while hydrophilic ones inhibit it, offering insights into peptide structure and function.
Scientists at Tohoku University found that boric acid catalyzes polypeptide synthesis under neutral and acidic conditions, producing up to 39 monomer-long glycine polypeptides. This discovery challenges previous studies suggesting neutral conditions hinder peptide synthesis.
A research group at Kobe University has successfully synthesized α-amino acid N-Carboxyanhydrides (NCAs), a crucial precursor for artificial polypeptides, using the photo-on-demand phosgenation method. This new synthesis method eliminates the use of toxic phosgene and is considered safe, inexpensive, and simple.
A research team led by Prof. ZHANG Kaiming uncovered a previously unrecognized mechanism for processive substrate degradation by the Lon protease. The study reveals that the protein degradation occurs at each individual proteolytic active site, following a C-to-N processive cleavage mechanism.
A team of researchers from Tokyo Tech has identified intrinsic regulatory mechanisms that enable nascent polypeptides to stabilize ribosomes and maintain uninterrupted translation. This discovery highlights the importance of peptide sequences in regulating protein synthesis.
Researchers at Texas A&M University have developed a new metal-free, recyclable polypeptide battery that degrades on demand, offering a sustainable alternative to traditional lithium-ion batteries. This breakthrough technology uses polypeptides, components of proteins, to create a non-toxic and recyclable power source.
A study in Nature Communications outlines the physical rules regulating the architecture of membraneless organelles (MLOs), also known as biomolecular condensates. The research found that RNA amount and protein amino acid sequence impact MLO surface stickiness, enabling predictive control over their arrangement.
Researchers have developed protein-based batteries using synthetic polypeptides and polymers, which could provide a sustainable and safe energy storage solution. The new technology has shown promising results, with potential applications in low-energy requirement devices like biosensors.
The nascent polypeptide-associated complex (NAC) identifies and sorts nascent polypeptide chains inside the ribosomal tunnel. NAC inserts its β-subunit into the tunnel to sense translation activity and regulate protein biogenesis.
Researchers at the University of Illinois have created a faster and more efficient way to build amino acid chains, known as polypeptides. This breakthrough could enable mass production of protein chains used in various industries, including chemistry and biology.
Researchers discovered that supercharged polypeptide fluids can form ordered phases in response to physical forces, resembling fingerprint patterns. The persisted order was detected using polarized optical microscopy, opening possibilities for biometric fingerprint detection.
Researchers at the University of Groningen create a funnel-shaped nanopore that can detect polypeptides differing by one amino acid. The technology uses electro-osmotic flow to pull polypeptides into the pore, producing a unique 'fingerprint' for each.
Researchers at MIT have designed a synthetic delivery system that is four times more effective than delivering mRNA on its own. The system uses a protein cap and poly-A binding protein to help mRNA bind to ribosomes and begin translation, resulting in higher protein expression.
Researchers have developed multifunctional nano-sized drug carriers based on reactive polypept(o)ides, which can be manipulated to control their morphology and function. These carriers exhibit stable circulation behavior and show promise for immunotherapy of malignant melanoma.
Researchers at Georgia Tech formed hundreds of possible precursor molecules in the lab and found that depsipeptides formed quickly and abundantly under conditions common on prebiotic Earth. These molecules could have served as a chemical stepping stone, accelerating the birth of long peptides that make up proteins.
Researchers at DGIST have identified a thermally responsive elastin-like polypeptide that controls acute intracerebral hemorrhage by forming protein nanostructures in damaged cerebral blood vessels. The polypeptide also accelerates vascular restoration and stimulates brain tissue regeneration.
A high-resolution view of the structure of Hsp104 has been acquired, showing how it processes proteins to break down tangles. The study provides insight into a potential nanomachine that could be used to dismantle harmful protein clumps in disease.
Research at Nagoya University reveals that phloem-specific polypeptides act as mobile descending shoot-to-root signals in response to nitrogen status, triggering compensatory nitrogen uptake by roots. This sophisticated signaling system enables plants to maximize nutrient efficiency and improve fertilizer application.
A recent study by Beth Israel Deaconess Medical Center researchers found that a specific long non-coding RNA, LINC00961, plays a key role in regulating the activity of the mTORC1 protein complex. This complex is involved in various cellular processes including translation, metabolism, cell growth and proliferation.
Scientists from Duke University developed a freely available computer program based on the traveling salesman mathematics problem to find the least-repetitive genetic code. This allows synthesizers to easily explore synthetic biomaterials previously unavailable to most researchers.
Researchers at Georgia Institute of Technology find that mixing amino and hydroxy acids with wet-dry cycles can create polypeptides, key components of life. The process, which could have occurred in a drying puddle, supports the theory that life began on dry land.
Researchers found that a functional autophagy system prevents the accumulation of toxic islet amyloid polypeptide, which can lead to diabetes. In animal models, autophagy-deficient beta cells developed overt diabetes, highlighting the protective role of autophagy in pancreatic beta cell function.
Researchers at the University of Illinois have developed spiral-shaped proteins that can efficiently deliver DNA segments to cells. The polypeptides outperform commercial agents in terms of efficiency and control toxicity, offering a promising new approach for clinical gene therapy.
Researchers developed a simple way to create short, spiral-shaped polypeptide chains that dissolve in water, which could be used as building blocks for self-assembling nanostructures and agents for drug delivery. The method involves elongating side chains to increase solubility while maintaining helical structure.
A tiny polypeptide has been developed that can bind to target-seeking molecules, enhancing their properties and improving the efficiency of drug development. The concept presents a new approach to drug development, potentially allowing for rapid development of new drugs with reduced costs and time.
Rice University researchers have developed a computer program that accurately simulates protein folding dramatically faster than previous methods. The new technique allows scientists to study the roots of diseases caused by proteins that fold incorrectly, which is crucial for understanding diseases such as Alzheimer's and cystic fibrosis.
Chinese researchers report a convenient method for synthesizing short protein chains using inexpensive starting materials and a simple cobalt complex catalyst. The new technique, similar to olefin polymerization, could be ideal for industrial production and may lead to the creation of polypeptides that were previously inaccessible.
A study by CU, Scripps researchers provides evidence of how proteins fold to create their characteristic shapes and biological functions. They propose that nonpolar groups in a polypeptide chain are responsible for initial folding, which then propagates to form the final folded structure.
Researchers identified a specific protein pattern that can distinguish bladder cancer patients from healthy controls and others with similar symptoms. This discovery has the potential to predict tumour stage, recurrence, progression, and treatment response in bladder cancer patients.
Researchers found that the GroEL oligomeric structure is essential for biologically significant chaperonin function. The study showed that enclosure of an unfolded protein in the cage provides a mechanism to prevent protein aggregation during folding, particularly for aggregation-sensitive proteins.
Researchers have successfully grown monomolecular films of a helical polypeptide, poly-gamma-benzyl-L-glutamate, directly from a flat surface. The films exhibit comparable polarization to conventional ferroelectric materials, with potential applications in piezo- and pyroelectric devices.