Biomolecular Recognition: Analysis of DFS Data - Dynamic Force Spectroscopy and Biomolecular Recognition - page 165

protein attachment protein receptor (SNARE) complex, which is made of syntaxin,
synaptosome-associated protein of 25 kDa (SNAP25), and synaptobrevin 2 (Sb2)
(Liu et al. 2006) or with SNAP23 (Montana et al. 2009); iron transporter protein
transferring (Tf) and its cell surface receptor (TfR) (Yersin et al. 2008); human
tumor suppressor p53 with the bacterial redox protein azurin (Taranta et al. 2008);
actin and heparin-binding hemagglutinin (HBHA) from Mycobacterium tuberculo-
sis (Verbelen et al. 2008); Staphylococcus aureus surface protein IsdA with human
proteins present on cornified envelope of desquamated epithelial cells: involucin,
loricin, and cytokeratin K10 (Clarke et al. 2009); signal-transducing proteins with
the Phox homology domain of mammalian phospholipase D1 (PLD1) and the Src
homology domain (SH3) of phospholipase c- 1), and Munc-18-1 (Kim,

2009). DFS has also been used to study protein-protein homophilic interactions
such as the vascular endothelial (VE)-cadherin (Baumgartner et al. 2000a); quadru-
ple H-bonded ureido-4[1H]-pyrimidinone (UPy) dimmers (Zou et al. 2005); HBHA-
HBHA (Verbelen et al. 2007); extracellular fragment of nectin-1 (nef-1) with the
wild-type L-fibrinoblasts that express nectin-1 (Vedula et al. 2007); tight-junction
proteins Claudin-1 (Lim et al. 2008b) and Claudin-2 (Lim et al. 2008a); negatively-
charged aggregan molecules extracted from bovine cartilage extracellular matrix
(Harder et al. 2010). DFS was used to study interaction of proteins with trans-
membrane (TM) proteins such as the multivalent Psythyrella velutina lectin (PVL)
and the most abundant TM protein in human erythrocyte glycophorin A (Yan et al.
2009). DFS was applied on the study of protein-peptide interactions such as the
GCN4(7P14P) peptide and a scFv at different maturation level (Morfill et al. 2007);
PDZ protein Tax-interacting protein-1 (TIP-1) and its recognition peptide derived
from

γ 1(PLC- γ

-catenin (Maki et al. 2007).
DFS has also been applied on various types of molecules other than peptides
or proteins. In particular, DFS has been used to study interactions between DNA
and proteins such as the regulatory DNA-binding protein ExpG from Sinorhi-
zobium meliloti 2011 and its target exp gene sequences (Bartels et al. 2003);
BsoBI and XhoI restrictions enzymes with their specific DNA sites using a
clever unzipping approach (Koch & Wang, 2003); various length of aptamers
(22-nt, 29-nt, and 37-nt) with IgE antibodies (Yu et al. 2007); DNA-binding domain
of the PhoB transcription factor from Escherichia coli and DNA-binding sequences
(Wollschlager et al. 2009). Other types of ligand studied by DFS include small
molecules such as fluorescein and anti-fluorescein scFv (Schwesinger. et al. 2000);
digoxigenin and antidigoxigenin antibodies (Neuert et al. 2006); uranyl-dicarboxy-
phenanthroline chelate with monoclonal antibodies (Odorico et al. 2007a; Teulon
et al. 2007; Teulon et al. 2008). DFS was used to study protein-carbohydrate inter-
actions such as AlgE4 epimerase and mannuronan (Sletmoen et al. 2004; Slet-
moen et al. 2005); extracellular matrix network between fibronectin and heparin
(Mitchell et al. 2007); Helicobacter pylori adhesion-receptor complex BabA and
fucosylated ABO/Lewis b blood group antigen (Bjornham et al. 2009). DFS showed
applications for studying the interactions between SNARE proteins and egg L-

β

-
phosphatidylcholine bilayers (Abdulreda et al. 2008). Application of DFS also covers

α