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- Leurs, P, et al.
(författare)
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Effects of hemodiafiltration on uremic inflammation
- 2013
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Ingår i: Blood purification. - : S. Karger AG. - 1421-9735 .- 0253-5068. ; 3535 Suppl 1, s. 11-17
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Tidskriftsartikel (refereegranskat)abstract
- Chronic inflammation is highly prevalent among end-stage renal disease patients and is linked to, and thought to contribute to, the high morbidity and mortality in this patient population. Hemodiafiltration (HDF) may potentially reduce inflammatory stimuli induced by the bioincompatibility of conventional hemodialysis (HD) systems. In addition, HDF may more efficiently remove inflammatory mediators. This brief review shows that the circulating levels of various markers of systemic inflammation in general are somewhat reduced in patients treated by HDF as compared to HD. On the other hand, according to the current literature, this favorable small impact on inflammation biomarkers does not seem to translate into better clinical outcomes. It is possible that this is due to inadequate design, inadequate number of investigated patients and too short duration of previous studies. The results of larger, better-designed ongoing prospective studies may hopefully clarify this.
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- de Kloe, Gerdien E, et al.
(författare)
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Surface Plasmon Resonance Biosensor Based Fragment Screening Using Acetylcholine Binding Protein Identifies Ligand Efficiency Hot Spots (LE Hot Spots) by Deconstruction of Nicotinic Acetylcholine Receptor α7 Ligands
- 2010
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Ingår i: Journal of Medicinal Chemistry. - : American Chemical Society (ACS). - 0022-2623 .- 1520-4804. ; 53:19, s. 7192-7201
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Tidskriftsartikel (refereegranskat)abstract
- The soluble acetylcholine binding protein (AChBP) is a homologue of the ligand-binding domain of the nicotinic acetylcholine receptors (nAChR). To guide future fragment-screening using surface plasmon resonance (SPR) biosensor technology as a label-free, direct binding, biophysical screening assay, a focused fragment library was generated based on deconstruction of a set of α7 nAChR selective quinuclidine containing ligands with nanomolar affinities. The interaction characteristics of the fragments and the parent compounds with AChBP were evaluated using an SPR biosensor assay. The data obtained from this direct binding assay correlated well with data from the reference radioligand displacement assay. Ligand efficiencies for different (structural) groups of fragments in the library were correlated to binding with distinct regions of the binding pocket, thereby identifying ligand efficiency hot spots (LE hot spots). These hot spots can be used to identity the most promising hit fragments in a large scale fragment library screen.
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