Following aptamer-thrombin binding by force measurements

Bernhard Basnar; Roey Elnathan; Itamar Willner

doi:10.1021/ac052289e

Following aptamer-thrombin binding by force measurements

Bernhard Basnar
, Roey Elnathan
, Itamar Willner^*

^*Corresponding author for this work

Institute of Chemistry

Research output: Contribution to journal › Article › peer-review

88 Scopus citations

Abstract

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 ̃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.

Original language	English
Pages (from-to)	3638-3642
Number of pages	5
Journal	Analytical Chemistry
Volume	78
Issue number	11
DOIs	https://doi.org/10.1021/ac052289e
State	Published - 1 Jun 2006

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title = "Following aptamer-thrombin binding by force measurements",

abstract = "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{\~ }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.",

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N2 - 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 ̃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.

AB - 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 ̃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.

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Following aptamer-thrombin binding by force measurements

Abstract

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