Following aptamer-thrombin binding by force measurements.
The rupture forces between an aptamer (1)-functionalized AFM tip and a thrombin-modified Au surface are analyzed. The rupture force for a single aptamer/thrombin complex is determined as approximately 4.45 pN. The analysis of the system reveals that the rupture forces correspond to the melting of the G-quadruplex structure of the aptamer bound to the thrombin. This melting of the G-quadruplex leads to the dissociation of the aptamer/thrombin complex.
Basnar
Bernhard
B
Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.
Elnathan
Roey
R
Willner
Itamar
I
D052157:Aptamers, Nucleotide / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism*; D001483:Base Sequence; D006046:Gold / Q000737:chemistry; D006860:Hydrogen Bonding; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D009691:Nucleic Acid Denaturation; D013314:Stress, Mechanical; D013917:Thrombin / Q000032:analysis* / Q000378:metabolism*
D052157:Aptamers, Nucleotide; D006046:Gold; D013917:Thrombin