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Synthetic Supramolecular Host for D-(-)-Ribose: Ratiometric Fluorescence Response via Multivalent Lectin-Carbohydrate Interactions.
Chembiochem
July 2022
Department of Chemistry, BITS-Pilani Hyderabad Campus Shameerpet, Hyderabad, 500078, Telangana, India.
Easily synthesizable, carbazole-based organic nanoaggregates have been designed for selective detection of D-(-)-ribose at physiological pH. The addition of D-ribose results in a ratiometric change in fluorescence color from green to cyan (LOD: ∼12 μM). The mechanistic studies indicate the presence of multipoint noncovalent interactions, such as hydrogen bonding and CH⋅⋅⋅π interactions between D-ribose and acyl hydrazone and terminal pyridyl units of the probe molecule.
View Article and Find Full Text PDFNovel diagnostic and prognostic factors for the advanced melanoma based on the glycosylation-related changes studied by biophysical profiling methods.
Biosens Bioelectron
May 2022
Faculty of Chemistry, Warsaw University of Technology, Warsaw, Poland. Electronic address:
Melanoma is a life-threatening disease due to the early onset of metastasis and frequent resistance to the applied treatment. For now, no single histological, immunohistochemical or serological biomarker was able to provide a precise predictive value for the aggressive behavior in melanoma patients. Thus, the search for quantifying methods allowing a simultaneous diagnosis and prognosis of melanoma patients is highly desirable.
View Article and Find Full Text PDFGlycan-Gold Nanoparticles as Multifunctional Probes for Multivalent Lectin-Carbohydrate Binding: Implications for Blocking Virus Infection and Nanoparticle Assembly.
J Am Chem Soc
October 2020
School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.
Multivalent lectin-glycan interactions are widespread in biology and are often exploited by pathogens to bind and infect host cells. Glycoconjugates can block such interactions and thereby prevent infection. The inhibition potency strongly depends on matching the spatial arrangement between the multivalent binding partners.
View Article and Find Full Text PDFHow Complex Is the Concanavalin A-Carboxypeptidase Y Interaction?
ACS Chem Biol
July 2019
Institute of Physics, Faculty of Technical Physics , Poznan University of Technology, Piotrowo 3 , PL-60965 Poznan , Poland.
Article Synopsis
- Lectin-carbohydrate interactions can be utilized for highly sensitive biochemical recognition and medical diagnoses, but require specific methodologies for detailed characterization.
- This study focuses on the unbinding properties of the concanavalin A-carboxypeptidase Y complex, crucial for understanding glycoproteins on cell surfaces.
- The researchers developed a methodology combining dynamic force spectroscopy and theoretical models, leading to insights into the unbinding mechanisms and characteristics of this important receptor-ligand complex.
Functional Characterization of OXYL, A SghC1qDC LacNAc-specific Lectin from The Crinoid Feather Star .
Mar Drugs
February 2019
Graduate School of NanoBio Sciences, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan.
We identified a lectin (carbohydrate-binding protein) belonging to the complement 1q(C1q) family in the feather star (a crinoid pertaining to the phylum Echinodermata). The combination of Edman degradation and bioinformatics sequence analysis characterized the primary structure of this novel lectin, named OXYL, as a secreted 158 amino acid-long globular head (sgh)C1q domain containing (C1qDC) protein. Comparative genomics analyses revealed that OXYL pertains to a family of intronless genes found with several paralogous copies in different crinoid species.
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