title: Probing single-stranded DNA and its biomolecular interactions through direct catalytic activation of factor XII, a protease of the blood coagulation cascade.
abstract: Triggered self-activation of factor XII, a blood coagulation protease, was utilized for the amplified visual detection of ss-DNA targets in a non-sequence specific way. Factor XII holds potential as a low-affinity and therefore non-interfering probe for DNA secondary structure and for the screening of protein binding to ss-DNA. The observation that ss-DNA also accelerates coagulation of human blood plasma is relevant to the emerging field of aptamer therapeutics.
authors.affiliation: Anorganisch-Chemisches Institut, Im Neuenheimer Feld 270, 69120 Heidelberg, Germany.
authors.forename: Valeri
authors.initials: V
authors.lastname: Pavlov
authors.forename: Michael
authors.initials: M
authors.lastname: Zorn
authors.forename: Roland
authors.initials: R
authors.lastname: Krämer
mesh_terms: D001777:Blood Coagulation; D002384:Catalysis; D004277:DNA, Single-Stranded / Q000235:genetics*; D005174:Factor XII / Q000378:metabolism*; D006801:Humans; D010447:Peptide Hydrolases / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D004277:DNA, Single-Stranded; D005174:Factor XII; D010447:Peptide Hydrolases