Quantifying the nanomachinery of the nanoparticle-biomolecule interface
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de-puig_Small_2011.pdf
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Main article
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Author(s)
de Puig Guixe, Helena
Federici, Stefania
Baxamusa, Salmaan H.
Bergese, Paolo
Hamad-Schifferli, Kimberly
Date Issued
June 2011
Journal
Small
Publisher
Wiley-VCH
Citation
de Puig, Helena et al. “Quantifying the Nanomachinery of the Nanoparticle-Biomolecule Interface.” Small (2011) : v. 7, issue 17, p. 2477-2484, Sept. 2011. Copyright © 2011 WILEY-VCH Verlag GmbH & Co.
Version
Author's final manuscript
Abstract
A study is presented of the nanomechanical phenomena experienced by nanoparticle-conjugated biomolecules. A thermodynamic framework is developed to describe the binding of thrombin-binding aptamer (TBA) to thrombin when the TBA is conjugated to nanorods. Binding results in nanorod aggregation (viz. directed self-assembly), which is detectable by absorption spectroscopy. The analysis introduces the energy of aggregation, separating it into TBA–thrombin recognition and surface-work contributions. Consequently, it is demonstrated that self-assembly is driven by the interplay of surface work and thrombin-TBA recognition. It is shown that the work at the surface is about −10 kJ mol−1 [mol superscript -1] and results from the accumulation of in-plane molecular forces of pN magnitude and with a lifetime of <1 s, which arises from TBA nanoscale rearrangements fuelled by thrombin-directed nanorod aggregation. The obtained surface work can map aggregation regimes as a function of different nanoparticle surface conditions. Also, the thermodynamic treatment can be used to obtain quantitative information on surface effects impacting biomolecules on nanoparticle surfaces.
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
Massachusetts Institute of Technology. Department of Mechanical Engineering
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DOI of Published Version
https://doi.org/10.1002/smll.201100530
