Microbead analysis of cell binding to immobilized lectin. Part II: Quantitative kinetic profile assay for possible identification of anti-infectivity and anti-cancer reagents |
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| Affiliation: | 1. Center of Biotechnology of Sfax, University of Sfax, BP K 3018, Sfax, Tunisia;2. Department of Anatomy-Pathology, Habib Bourguiba Hospital, Sfax, Tunisia;3. Department of Surgery, Habib Bourguiba Hospital, Sfax, Tunisia;1. Burn and Plastic Surgery, The Second Affiliated Hospital, Shantou University Medical College, North DongXia Road, Shantou, Guangdong Province 515041, PR China;2. Research Center for Translational Medicine, Shantou University Medical College, North DongXia Road, Shantou, Guangdong Province 515041, PR China;3. Department of Histology and Embryology, Shantou University Medical College, 22 Xin Ling Road, Shantou, Guangdong Province 515041, PR China;4. Burns Institute, The First Affiliated Hospital, Chinese PLA General Hospital, Trauma Center of Postgraduate Medical School, 51 Fu Cheng Road, Beijing 100037, PR China;1. Membrane Molecular Interactions Research Group, School of Chemical and Food Engineering, Post-graduation Program in Technological and Environmental Chemistry, Federal University of Rio Grande, Av. Itália, Km 8, Campus Carreiros, 96203-900, Rio Grande, RS, Brazil;2. Post-graduation Program in Material Science and Engineering, Federal University of Santa Catarina, 88040-900, Florianópolis, SC, Brazil;3. Federal Institute of Education, Science and Technology of Santa Catarina, Campi Abelardo Luz, 89051-000, Blumenau, SC, Brazil;2. Department of Comparative Anatomy, Institute of Zoology, Jagiellonian University, Gronostajowa 9, 30-387 Krakow, Poland;3. Poison Information Centre, Jagiellonian University Medical College, Śniadeckich 10, 31-531 Krakow, Poland;1. Division of Anatomy, Faculty of Dental Medicine, “Carol Davila” University of Medicine and Pharmacy, Bucharest, Romania;2. MEDCENTER, Center of Excellence in Laboratory Medicine and Pathology, Bucharest, Romania;3. International Society of Regenerative Medicine and Surgery (ISRMS), Romania;4. Department of Medicine and Surgery, University of Catania, Italy;5. Division of Ophthalmology, S.C.U.O., Faculty of Medicine, “Carol Davila” University of Medicine and Pharmacy, Bucharest, Romania;6. Clinical Hospital of Ophthalmologic Emergencies (S.C.U.O.), Bucharest, Romania |
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| Abstract: | There has been a re-emergence of the use of lectins in a variety of therapeutic venues. In addition lectins are often responsible for the binding of pathogens to cells and for cancer cell clumping that increases their escape from body defenses. It is important to define precisely the activity of inhibitors of lectin-binding that may be used in anti-infection and anti-cancer therapeutics. Here we describe a kinetic assay that measures the activity of saccharide inhibitors of lectin binding using a model system of yeast (Saccharomyces cerevisiae) and lectin (Concanavalin A, Con A) derivatized agarose microbeads that mimics pathogen-cell binding. We show that old methods (part I of this study) used to identify inhibitor activity using only one sugar concentration at one time point can easily provide wrong information about inhibitor activity. We assess the activity of 4 concentrations of 10 saccharides at 4 different times in 400 trials and statistically evaluate the results. We show that d-melezitose is the best inhibitor of yeast binding to the lectin microbeads. These results, along with physical chemistry studies, provide a solid foundation for the development of drugs that may be useful in anti-infectivity and anti-cancer therapeutics. |
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| Keywords: | Lectins Yeast Sugar inhibition Con A derivatized beads Anti-infectivity Anti-cancer therapeutics |
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