Annelie Pichert

TL;DR: This work combines fluorescence spectroscopy, NMR experiments, docking and molecular dynamics simulations to study the configurational and recognition properties of IL-8 towards a series of HA and CS derivatives and DS, and the effects of GAG length and sulfation patterns in binding strength and specificity.

TL;DR: This review focuses on the interaction of IL-8 with sulfated glycosaminoglycans expressed on cell surfaces and the extracellular matrix, which contributes to the recruitment of polymorphonuclear cells from blood, penetration of these cells through the vessel wall, and their directed migration to inflammatory sites.

TL;DR: In this paper, Pichert et al. investigated the interaction of heparin hexasaccharides and recombinant human IL-8, consisting of 77 amino acids using fluorescence and NMR spectroscopy.

TL;DR: This work studied complexes of IL-8 and heparin (HEP) as well as other GAGs in a multidisciplinary approach, involving site-directed mutagenesis, mass spectrometry, fluorescence and solution NMR spectroscopy aswell as computer modeling.

TL;DR: Findings indicate that the N terminus of the E75K variant is more important as a second binding site for GAGs than that of the wild‐type IL‐8(1–77), and more residues in the variant responded to GAG binding than in the wild-type.