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Quantifying the Nanomachinery of the Nanoparticle–Biomolecule Interface
Author(s) -
de Puig Helena,
Federici Stefania,
Baxamusa Salmaan H.,
Bergese Paolo,
HamadSchifferli Kimberly
Publication year - 2011
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201100530
Subject(s) - nanorod , biomolecule , nanoparticle , thrombin , nanoscopic scale , materials science , nanotechnology , conjugated system , aptamer , work (physics) , molecule , chemistry , polymer , organic chemistry , thermodynamics , physics , platelet , genetics , immunology , composite material , biology
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 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.