个人简介

B.Sc. & Ph.D - Queen's University

研究领域

Chemical Biology

Chemical Biology molecular mimicry, glycomimetics, protein-ligand interactions, immunochemistry, enzyme inhibitors, NMR/molecular modeling, drug and vaccine design Our group is studying the nature and origin of carbohydrate mimicry for the purpose of drug and vaccine design. We take our leads from molecular mimicry displayed by Nature. Our goals are the understanding of the molecular mechanisms of recognition that can be used to tailor specific immune responses or inhibit specific enzymatic reactions. The results have implications for the control or treatment of bacterial and viral diseases, diabetes Type 2, and cancer. The development of NMR/molecular modeling protocols for probing bioactive conformations of ligands bound to protein receptors. The development of drug candidates for the treatment of Type 2 diabetes. The development of drug candidates for the treatment of metastatic cancer. The development of vaccines for Streptococcus Groups A and B, and HIV-1. The development of enzyme inhibitors for the control of bacterial pathogens. The development of nucleoside and nucleotide analogues as antiviral agents. The development of nucleotide analogues as gene-silencing agents. The control of glycoprotein trafficking in cells. The development of analytical methods for glycan profiling.

近期论文

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Mohan, S.; Kerry, P. S.; Bance, N.; Niikura, M.; Pinto, B. M. (2013). Serendipitous Discovery of a Potent Influenza Virus A Neuraminidase Inhibitor. Angew. Chem. Int. Ed. doi: 10.1002/anie.201308142 Poulin, M. B.; Shi, Y.; Protsko, C.; Dalrymple, S. A.; Sanders, D. A. R.; Pinto, B. M.; Lowary, T. L. (2013). Specificity of a UDP-GalNAc Pyranose–Furanose Mutase. A Potential Drug Target for Campylobacter jejuni Infections. ChemBioChem. doi: 10.1002/cbic.201300653 Adabala, P. J. P.; LeGresley, E.; Bance, N.; Niikura, M.; Pinto, B. M.(2013). Exploitation of the Catalytic Site and 150 Cavity for Design of Neuraminidase Inhibitors. J. Org. Chem. doi: 10.1021/jo401854w Auzanneau, F.-I.; Borrelli, S.; Pinto, B. M. (2013). Synthesis and Immunological Activity of an Oligosaccharide-conjugate as a Vaccine Candidate Against Group A Streptococcus . Bioorg. Med. Chem. Lett. doi: 10.1016/j.bmcl.2013.09.042 Kerry, P. S.; Mohan, S.; Russell, R. J.; Bance, N.; Niikura, M.; Pinto, B. M. (2013). Structural basis for a class of nanomolar influenza A neuraminidase inhibitors . Sci. Rep. doi: 10.1038/srep02871 Mohan, S.; Eskandari, R.; Pinto, B.M. (2013). Naturally Occurring Sulfonium-Ion Glucosidase Inhibitors and Their Derivatives: A Promising Class of Potential Antidiabetic Agents. Acc. Chem. Res . doi:10.1021/ar400132g Gu, G.; Adabala, P. J. P.; Szczepina, M. G.; Borrelli, S.; Pinto, B.M. (2013). Synthesis and Immunological characterization of Modified Hyaluronic Acid Hexasaccharide Conjugates. J. Org. Chem . doi:10.1021/jo4012442 Greenway, K. T., LeGresley, E. B., Pinto, B.M. (2013). The Influence of 150-Cavity Binders on the Dynamics of Influenza A Neuraminidases as Revealed by Molecular Dynamics Simulations and Combined Clustering. PLoS ONE . doi:10.1371/journal.pone.0059873 Dahabieh, M.S., Samantha, D., Brodovitch, J.-C., Frech, C., O'Neill, M.A., Pinto, B.M. (2012). Sequence Dependent Structural Dynamics of Primate Adenosine-to-Inosine Editing Substrates. ChemBioChem. doi:10.1002/cbic.201200526 Zandberg, W., Kumarasamy, J., Pinto, B.M., Vocadlo, D. (2012). Metabolic Inhibition of Sialyl-LewisX Biosynthesis by 5-Thiofucose Remodels the CEll Surface and Impairs Selectin-Mediated Cell Adhesion. J. Biol. Chem. doi:10.1074/jbc.M112.403568 Greenway, K.T., Bischoff, A.L., Pinto, B.M. (2012). Hyperconjugation as Probed Experimentally with the Conformational Deuterium Isotope Effect. J. Org. Chem. doi:10.1021/jo3017988 Jones, K, Eskarandari, R., Jones, K., Reddy, R.K., Quezada-Valvillo R., Nichols, B., Rose, D.R., Hamaker, B., Pinto, B.M. (2012). Investigations of Structures and Properties of the Human Intestinal Enzymes MGAM and SI . J. Pediatr. Gastroenterol. Nutr. doi:10.1097/01.mpg.0000421403.34763.71 Yu, B.-H., Eskarandari, R., Jones, K., Reddy, R.K., Quezada-Calvillo, R., Nichols, B., Rose, D.R., Hamaker, B., Pinto, B.M. (2012). Modulation of Starch Digestion for Slow Glucose Release Through "Toggling" of Activities of Mucosal alpha-Glucosidases. J. Biol. Chem. doi:10.1074/jbc.M112.351858 Mohan, S., McAtamney S., Jaykanthan, J., Eskarandi, R., von Itzstein, M., Pinto, B.M. (2012). Antiviral activities of sulfonium-ion glucosidase inhibitors and 5-thiomannosylamine-disaccharide derivatives against dengue virus. Int. J. Antimicrob. Agents . doi:10.1016/j.ijantimicag.2012.05.002 Fernandez-Herrera, M.A, Lopez-Munoz, H, Hernandez-Cazquez, J.M.V, Sanchez-Sanchez, L., Escobar-Sanchez, M.L., Pinto, B.M., Sandoval-Ramirez, J.(2012). Synthesis and selective anticancer activity of steroidal glycoconjugates. Eur. J. Med. Chem. . doi:10.1016/j.ejmech.2012.06.027 Shi, Y., Pinto, B. M (2012). Molecular dynamics simulations of carbohydrate-mimetic haptens in complex with a complementary anti-carbohydrate antibody. Carbohydr. Res. doi:10.1016/j.carres.2012.05.024 Eskandari, R., K. Jones, D. R. Rose, B. M. Pinto (2011). Selectivity of 3'-O-Methylponkoranol for Inhibition of N- and C-terminal Maltase Glucoamylase and Sucrase Isomaltase, Therapeutic Targets for Digestive Disorders and Their Sequelae. Bioorg. Med. Chem. Lett.. doi:10.1016/j.bmcl.2011.08.069 Eskandari R, Jones K, Ravinder Reddy K, Jayakanthan K, Chaudet M, Rose DR, Pinto BM. (2011). Probing the Intestinal α-Glucosidase Enzyme Specificities of Starch-Digesting Maltase-Glucoamylase and Sucrase-Isomaltase: Synthesis and Inhibitory Properties of 3'- and 5'-Maltose-Extended De-O-sulfonated Ponkoranol. Chem. Eur. J . doi:10.1002/chem.201102109 Eskandari R, Jones K, Rose DR, Pinto BM. (2011). The effect of heteroatom substitution of sulfur for selenium in glucosidase inhibitors on intestinal α-glucosidase activities. Chem Commun (Camb). doi:10.1039/c1cc13052h Szczepina, M.G., D.W. Bleile, B.M. Pinto (2011). Investigation of the Binding of a Carbohydrate-mimetic Peptide to its Complementary Anti-carbohydrate Antibody by STD-NMR Intensity-restrained CORCEMA Optimization (SICO) and Molecular Dynamics Simulations. Chem. Eur. J. doi:10.1002/chem.201100222