Carbohydrate-protein interactions trigger a wide range of biological signaling pathways, the mainstays of physiological and pathological processes. However, there are an incredible number of carbohydrate-binding proteins (CBPs) that remain to be identified and characterized. This study reports for the first time the covalent labeling of CBPs by triazinyl glycosides, a new and promising class of affinity-based glycoprobes. Mono- and bis-clickable triazinyl glycosides were efficiently synthesized from unprotected oligosaccharides (chitinpentaose and 2'-fucosyl-lactose) in a single step. These molecules allow the specific covalent labeling of chitin-oligosaccharide-binding proteins (wheat germ agglutinin WGA and ChiA1 D202A, an inactivated chitinase) and fucosyl-binding lectin (UEA-I), respectively.
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http://dx.doi.org/10.1021/acs.bioconjchem.9b00432 | DOI Listing |
Sci Rep
January 2025
Department of Applied Chemistry, Faculty of Engineering, University of Miyazaki, 1-1 Nishi, Gakuen-Kibanadai, Miyazaki, 889-2192, Japan.
The ligand-docking behavior of hevein, the major latex protein from the rubber tree Hevea brasiliensis (Euphorbiaceae), has been investigated by the unguided molecular dynamics (MD) simulation method. An oligosaccharide molecule, initially placed in an arbitrary position, was allowed to move around hevein for a prolonged simulation time, on the order of microseconds, with the expectation of spontaneous ligand docking of the oligosaccharide molecule to the binding site of hevein. In the binary solution system consisting of a hevein molecule and a chito-trisaccharide (GlcNAc) molecule, three out of the six separate simulation runs successfully reproduced the complex structure of the observed binding from.
View Article and Find Full Text PDFMar Drugs
December 2024
Biotechnology Unit, University of Ribeirão Preto/UNAERP, Ribeirão Preto 14096-900, SP, Brazil.
Lectins are non-covalent glycan-binding proteins found in all living organisms, binding specifically to carbohydrates through glycan-binding domains. Lectins have various biological functions, including cell signaling, molecular recognition, and innate immune responses, which play multiple roles in the physiological and developmental processes of organisms. Moreover, their diversity enables biotechnological exploration as biomarkers, biosensors, drug-delivery platforms, and lead molecules for anticancer, antidiabetic, and antimicrobial drugs.
View Article and Find Full Text PDFMacromolecules
January 2025
Department of Biochemistry, Virginia Tech, Blacksburg, Virginia 24061, United States.
The environmental and economic challenges posed by the widespread use and disposal of plastics, particularly poly(ethylene terephthalate) (PET), require innovative solutions to mitigate their impact. Such mitigation begins with understanding physical properties of the polymer that could enable new recycling technologies. Although molecular simulations have provided valuable insights into PET interactions with various PET hydrolases, current nonpolarizable force fields neglect the electronic polarization effects inherent to PET interactions.
View Article and Find Full Text PDFCarbohydr Res
January 2025
Université Paris Cité and Université des Antilles and Université de la Réunion, INSERM, BIGR, F-75015 Paris, France. Electronic address:
Protein-carbohydrate interactions play a crucial role in numerous fundamental biological processes. Thus, description and comparison of the carbohydrate binding site (CBS) architecture is of great importance for understanding of the underlying biological mechanisms. However, traditional approaches for carbohydrate-binding protein analysis and annotation rely primarily on the sequence-based methods applied to specific protein classes.
View Article and Find Full Text PDFQRB Discov
December 2024
Department of Chemistry, University of Oslo, NO-0315 Oslo, Norway.
Despite major efforts toward its eradication, cholera remains a major health threat and economic burden in many low- and middle-income countries. Between outbreaks, the bacterium responsible for the disease, , survives in aquatic environmental reservoirs, where it commonly forms biofilms, for example, on zooplankton. -acetyl glucosamine-binding protein A (GbpA) is an adhesin that binds to the chitinaceous surface of zooplankton and breaks its dense crystalline packing thanks to its lytic polysaccharide monooxygenase (LPMO) activity, which provides with nutrients.
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