874986-46-6Relevant academic research and scientific papers
Conformational flexibility of glycosylated peptides
Bollmann, Stefan,Burgert, Anne,Plattner, Carolin,Nagel, Lilly,Sewald, Norbert,Loellmann, Marc,Sauer, Markus,Doose, Soeren
, p. 2907 - 2911 (2011)
With a twist: The conformational dynamics of glycosylated glycine-serine peptides is studied using contact- induced fluorescence quenching analysed by fluorescence correlation spectroscopy. End-to-end contact rates on ns-μs timescales reveal enthalpic and entropic contributions to the reduction of contact formation rates in glycopeptides (see picture). Copyright
Design of potent inhibitors for Schistosoma japonica glutathione S-transferase
Jao, Shu-Chuan,Chen, Jessica,Yang, Kelvin,Li, Wen-Shan
, p. 304 - 318 (2007/10/03)
We implemented both structure-based drug design and the concept of polyvalency to discover a series of potent and unsymmetrical Schistosoma japonicum glutathione S-transferase (SjGST) inhibitors 10-12. This strategy achieved not only an excellent enhancement (10- to 490-fold) in the inhibitory potency, compared to the monofunctional analogues 1-5, but was also an effective modification by selecting a hydrophobic moiety with a flexible linker. The designed compounds with a low micromolar hit demonstrate special values in refining the new generation of SjGST inhibitors. The stoichiometry of the binding is one inhibitor molecule per SjGST monomer via isothermal titration calorimetric measurement.
