Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 116, Issue 17, Pages 5316-5322Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp301765n
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Funding
- National Science Foundation [ECCS 0823849, CBET 1139057]
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [1139057] Funding Source: National Science Foundation
- Directorate For Engineering
- Div Of Electrical, Commun & Cyber Sys [0823849] Funding Source: National Science Foundation
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We studied the molecular details of DNA aptamer ricin interactions. The toxic protein ricin molecules were immobilized on a Au(111) surface using a N-hydroxysuccinimide (NHS) ester to specifically react with lysine residues located on the ricin B chains. A single ricin molecule was visualized in situ using the AFM tip modified with an antiricin aptamer. Computer simulation was used to illustrate the protein and aptamer structures, the single-molecule ricin images on a Au(111) surface, and the binding conformations of ricin-aptamer and ricin-antibody complexes. The various ricin conformations on a Au(111) surface were caused by the different lysine residues reacting with the NHS ester. It was also observed that most of the binding sites for aptamer and antibody on the A chains of ricin molecules were not interfered by the immobilization reaction. The different locations of the ricin binding sites to aptamer and antibody were also distinguished by AFM recognition images and interpreted by simulations.
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