title: The binding of pentapeptides to biological and synthetic high affinity heparin.
abstract: Pentapeptides have been shown to bind the synthetic heparin fondaparinux (Arixtra) as well the biological heparins dalteparin (Fragmin) and salmon heparin. In contrast to heparin binding consensus sequences, the pentapeptides are acidic or neutral, with no arginine or histidine residue. The peptides showed an effect on in vitro heparin anti-factor X activity with a reduction of fondaparinux activity by 65-95%. Heparin binding was further studied by using peptide solid phase chromatography and NMR analysis.
authors.affiliation: Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), N-1432 Ås, Norway. Electronic address: ragnar.flengsrud@nmbu.no.
authors.forename: Ragnar
authors.initials: R
authors.lastname: Flengsrud
authors.affiliation: Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), N-1432 Ås, Norway.
authors.forename: Simen Gjelseth
authors.initials: SG
authors.lastname: Antonsen
mesh_terms: D001665:Binding Sites; D004305:Dose-Response Relationship, Drug; D006493:Heparin / Q000138:chemical synthesis* / Q000737:chemistry*; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry*; D013329:Structure-Activity Relationship
chemical_list: D009842:Oligopeptides; D006493:Heparin
keywords: Dalteparin-binding; Fondaparinux-binding; Heparin activity reversal; Heparin purification; Heparin removal; Hydrophobic interaction