1253891-13-2Relevant academic research and scientific papers
Saturation transfer difference NMR reveals functionally essential kinetic differences for a sugar-binding repressor protein
Perez-Victoria, Ignacio,Kemper, Sebastian,Patel, Mitul K.,Edwards, John M.,Errey, James C.,Primavesi, Lucia F.,Paul, Matthew J.,Claridge, Timothy D. W.,Davis, Benjamin G.
, p. 5862 - 5864 (2009)
The binding kinetics of disaccharides trehalose and trehalose-6-phosphate to repressor protein TreR have been determined using STD NMR and shed light on the contrasting biological roles of these two sugars.
Control of phosphoryl migratory transesterifications allows regioselecive access to sugar phosphates
Patel, Mitul K.,Davis, Benjamin G.
supporting information, p. 346 - 349 (2013/03/14)
Phosphate esters in polyhydroxylated systems are normally blighted by uncontrolled migration under a variety of reaction conditions. Cesium fluoride is demonstrated as a reagent to control migration of primary phosphates during transesterifications. This allows easy exchange of phosphoryl protecting groups enabling enhanced synthetic strategic flexibility and regioselective phosphate installation. Mechanistic analysis suggests that a fluoride-induced extended solvent sphere modulates steric bulk at phosphorus to favor the primary position.
Simple one-pot regioselective 6-O-phosphorylation of carbohydrates and trehalose desymmetrization
Abragam Joseph,Chang, Chun-Wei,Wang, Cheng-Chung
, p. 11497 - 11499 (2013/12/04)
Biologically essential carbohydrate 6-phosphates, especially trehalose 6-phosphate, can be synthesized easily in excellent overall yields in 2 steps involving minimum protecting group manipulations. We can cleave the diphenylphosphate group for further synthetic objectives.
DETECTION OF MYCOBACTERIA
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Page/Page column 71, (2011/04/18)
A method for determining the presence of mycobacteria species in an organism or biological sample, the method comprising adding to the organism or biological sample a probe molecule comprising a substrate and a label, which probe molecule can be incorporated into mycobacteria, the presence of mycobacteria being determined by a detector responsive to the presence of the label, optionally after applying a stimulus; suitable probe molecules include compounds comprising a label and a substrate, which label is can be detected by a detector responsive to the presence of the label, optionally after applying a stimulus, characterised by compound being able to engage with the active site of Antigen 85B (Ag85B) such that it can form simultaneous hydrogen bonds with two or more amino acids in the active site selected from Arg 43, Trp 264, Ser126, His 262 and Leu 42, or the corresponding amino acids in Antigen 85A (Ag85A) or Antigen 85C (Ag85C), at least one of which is with Ser126.
ESI-MS assay of M. tuberculosis cell wall antigen 85 enzymes permits substrate profiling and design of a mechanism-based inhibitor
Barry, Conor S.,Backus, Keriann M.,Barry, Clifton E.,Davis, Benjamin G.
supporting information; experimental part, p. 13232 - 13235 (2011/10/10)
Mycobacterium tuberculosis Antigen 85 enzymes are vital to the integrity of the highly impermeable cell envelope and are potential therapeutic targets. Kinetic analysis using a label-free assay revealed both mechanistic details and a substrate profile tha
Flow chemistry kinetic studies reveal reaction conditions for ready access to unsymmetrical trehalose analogues
Patel, Mitul K.,Davis, Benjamin G.
supporting information; experimental part, p. 4232 - 4235 (2010/11/18)
Monofunctionalization of trehalose, a widely-found symmetric plant disaccharide, was studied in a microreactor to give valuable kinetic insights that have allowed improvements in desymmetrization yields and the development of a reaction sequence for large scale monofunctionalizations that allow access to probes of trehalose's biological function.
