13071-57-3Relevant articles and documents
Structure-activity relationships in toll-like receptor-2 agonistic diacylthioglycerol lipopeptides
Wu, Wenyan,Li, Rongti,Malladi, Subbalakshmi S.,Warshakoon, Hemamali J.,Kimbrell, Matthew R.,Amolins, Michael W.,Ukani, Rehman,Datta, Apurba,David, Sunil A.
experimental part, p. 3198 - 3213 (2010/10/02)
The N-termini of bacterial lipoproteins are acylated with a (S)-(2,3-bisacyloxypropyl)cysteinyl residue. Lipopeptides derived from lipoproteins activate innate immune responses by engaging Toll-like receptor 2 (TLR2) and are highly immunostimulatory and yet without apparent toxicity in animal models. The lipopeptides may therefore be useful as potential immunotherapeutic agents. Previous structure-activity relationships in such lipopeptides have largely been obtained using murine cells, and it is now clear that significant species-specific differences exist between human and murine TLR responses. We have examined in detail the role of the highly conserved Cys residue as well as the geometry and stereochemistry of the Cys-Ser dipeptide unit. (R)-Diacylthioglycerol analogues are maximally active in reporter gene assays using human TLR2. The Cys-Ser dipeptide unit represents the minimal part-structure, but its stereochemistry was found not to be a critical determinant of activity. The thioether bridge between the diacyl and dipeptide units is crucial, and replacement by an oxoether bridge results in a dramatic decrease in activity.
Synthesis of the sialyl Lewis X epitope attached to glycolipids with different core structures and their selectin-binding characteristics in a dynamic test system
Gege, Christian,Vogel, Jan,Bendas, Gerd,Rothe, Ulrich,Schmidt, Richard R.
, p. 111 - 122 (2007/10/03)
Sialyl Lewis X (sLe(X))/selectin-mediated leukocyte rolling along endothelial cells has recently gained wide interest. In this paper the influence of the spacer length of laterally clustered neoglycolipids 1a-d on cell rolling in a dynamic test system is
Inhibition of human erythrocyte membrane phosphatidylinositol 4-kinase by phospholipid analogues
Young,Downes,Jones,Milliner,Rana,Ward
, p. 537 - 549 (2007/10/02)
Analogues of phosphatidylinositol (PtdIns, 1) have been synthesized to investigate the structural requirements for inhibition of a PtdIns 4-kinase obtained from human erythrocyte membranes. While the presence of either D-1 or D-3 stereochemistry in the inositol moiety greatly influences the degree of inhibition produced by PtdIns analogues, the stereochemistry of the glycerol moiety is of little consequence. Neither structural feature however, makes a significant contribution to binding affinity. Competitive inhibitory activity was found to be retained (or even enhanced) in substantially simpler analogues consisting of 1 or 2 hydrocarbon chains attached to a charged phosphate head group, such as in the phosphatidic acids, 24 and 26. The observation that the phosphatidylinositol 4-phosphate (PtdIns 4P) and phosphatidic acid analogues (eg, 16 or 17, and 26 respectively) inhibit PtdIns 4-kinase may suggest that such species have a regulatory role in PtdIns turnover.