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Transfer of Perceptual Gaining knowledge from Nearby Stereopsis to be able to International Stereopsis in older adults Together with Amblyopia: An initial Study.
The Platform Chemistry of the Swiss Academy of Sciences SCNAT is a small component in the Swiss network of education and research. The platform board analyses the education and research scene in Switzerland in order to identify issues that can be addressed by projects or initiatives or by coordinating efforts of others.Inhaltliche Richtigstellung zu folgendem Beitrag in der Chemical Education-Reihe C. A. Vock, Chimia 2021, 75, 443-445, https//doi.org/10.2533/chimia.2021.443.Molecular recognition of food molecules by ion channels and G-protein coupled receptors is the basis of taste perception. We explore the chemical nature of dietary molecules, and explore how salty, sour, sweet, bitter, and umami tastes can be explained at a molecular level.Nature has evolved a remarkable array of biosynthetic enzymes that install diverse chemistries into natural products (NPs), bestowing them with a range of important biological properties that are of considerable therapeutic value. This is epitomized by the ribosomally synthesized and post-translationally modified peptides (RiPPs), a class of peptide natural products that undergo extensive post-translational modifications to produce structurally diverse bioactive peptides. In this review, we provide an overview of our research into the proteusin RiPP family, describing characterized members and the maturation enzymes responsible for their unique chemical structures and biological activities. The diverse enzymology identified in the first two proteusin pathways highlights the enormous potential of the RiPP class for new lead structures and novel pharmacophore-installing maturases as biocatalytic tools for drug discovery efforts.The new Energypolis campus brings together the skills of EPFL Valais-Wallis, HES-SO Valais-Wallis, and the Ark Foundation's services. Together these partners respond to today's major concerns in the domains of energy, health, and the environment cutting-edge technology. NMDAR antagonist The spirit of this new campus is to foster innovation in these disciplines and emulate the creation of start-up companies. The HES-SO hosts the School of Engineering (HEI) at this campus, which includes the following degree programmes Life Technologies, Systems Engineering and Energy and Environmental Engineering, as well as their corresponding applied research institutes. Peptide technologies belong to the many activities that are carrying out in the Institute of Life Technologies. The present review summarizes the peptide technologies that are currently under development, that is, the regioselective labeling of therapeutic antibodies for cancer imaging, the development of peptide antivirals and antimicrobials for the treatment of infectious diseases, targeting of drugs conjugated to peptidic scaffolds as well as engineering of biomaterials.Aiming at studying cooperativity effects between amino acids in easily accessible protein models, we have explored the chemistry of peptide dendrimers, which we obtain as pure products by solid-phase peptide synthesis using a branching diamino acid such as lysine at every second or third position in a peptide sequence, followed by reverse-phase HPLC purification. This article reviews discoveries driven by combinatorial library synthesis and screening, including enantioselective esterase and aldolase enzyme models, cobalamin binding and peroxidase dendrimers, glycopeptide dendrimer biofilm inhibitors and their X-ray crystal structures as complexes with lectins, antimicrobial peptide dendrimers active against multidrug resistant Gram-negative bacteria, and transfection reagents for siRNA and CRISPR-Cas9 plasmid DNA. Latest developments include cheminformatics and artificial intelligence for exploring the peptide chemical space, and the principle of stereorandomization to understand the role of peptide chirality in activity.More than 50% of proteinogenic amino acid sidechains can bind metal ions, enabling proteins and peptides to bear these ions as cofactors. Nevertheless, post-translational modifications and incorporation of noncanonical amino acids bestow peptides and proteins myriads of other coordination capabilities, thanks to an enhanced metal binding. Here we summarize selected examples of natural and artificial systems that contain one or more noncanonical amino acids coordinating a metal ion and subsequently achieve a new or enhanced function. We report on a wide array of systems from disease-related proteins that undergo sulfurylation or phosphorylation through natural metallophores that selectively capture precious essential ions to synthetic selfassembly strategies, biocatalysts, and chelating agents against toxic metals. Regardless of their (bio)synthetic routes, all possess unique metal-binding properties that could not be effectively achieved by systems composed of canonical residues.The enormous structural and functional diversity available through combining different amino acids into peptides offers numerous exciting opportunities. This article summarizes recent research highlights from my laboratory in the areas of asymmetric catalysis, supramolecular chemistry, and chemical biology. This scope includes the development of bioinspired peptide catalysts, synthetic collagen peptides, supramolecular porous assemblies, and cell-penetrating peptides.This review on intracellular delivery and oral bioavailability of peptides reflects a number of principal investigations at Novartis. Our studies were aimed at either understanding features enabling peptides to interfere with intracellular protein-protein interactions, or to achieve a more patient-friendly delivery by the oral route. In the light of these objectives, we have also spent some effort on assay development to come up with alternative methods for monitoring cellular peptide uptake. This summary of our insights is intended to help in the assessment and development of peptide therapeutics requiring membrane transition.Proteins with large and flat binding sites as well as protein-protein interactions are considered ' undruggable ' with conventional small-molecule drugs. Cyclic peptides have been found to be capable of binding to such targets with high affinity, making this class of compounds an interesting source for possible therapeutics. However, the oftentimes poor passive membrane permeability of cyclic peptides still imposes restrictions on the applicability of cyclic peptide drugs. Here, we describe how computational methods in combination with experimental data can be used to improve our understanding of the structure-permeability relationship. Especially the conformational dynamic and chameleonic nature of cyclic peptides, which we investigate by a combination of MD simulations and kinetic modeling, is important for their ability to permeate passively through the membrane. The insights from such studies may enable the formulation of design principles for the rational design of permeable cyclic peptides.
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