title: Structural basis of single molecular heparin-FX06 interaction revealed by SPM measurements and molecular simulations.
abstract: Heparin, a functionalized polysaccharide, is observed under a scanning tunneling microscope, which shows atomic scale conformational details. The peptide FX06 is found to bind to five consecutive sugar units of heparin and this interaction is directly revealed by atomic force microscopy and dynamic force spectroscopy measurements. The determined free energy change agrees well with the dynamic calculation result.
authors.affiliation: Single Molecule Study Laboratory, College of Engineering and Nanoscale Science and Engineering Center, University of Georgia, Athens, GA 30602, USA.
authors.forename: Cunlan
authors.initials: C
authors.lastname: Guo
authors.forename: Bin
authors.initials: B
authors.lastname: Wang
authors.forename: Lianchun
authors.initials: L
authors.lastname: Wang
authors.forename: Bingqian
authors.initials: B
authors.lastname: Xu
mesh_terms: D005338:Fibrin Fibrinogen Degradation Products / Q000737:chemistry* / Q000378:metabolism*; D006493:Heparin / Q000737:chemistry* / Q000378:metabolism*; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D005338:Fibrin Fibrinogen Degradation Products; D010446:Peptide Fragments; C033786:fibrinogen Bbeta (15-42); D006493:Heparin