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Cited by 318

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Biomimetic Interactions of Proteins with Functionalized Nanoparticles: A Thermodynamic Study

De, Mrinmoy, You, Chang-Cheng, Srivastava, Sudhanshu, Rotello, Vincent M.·2007·Journal of the American Chemical Society

Abstract

Gold nanoparticles (NPs) functionalized with L-amino acid-terminated monolayers provide an effective platform for the recognition of protein surfaces. Isothermal titration calorimetry (ITC) was used to quantify the binding thermodynamics of these functional NPs with alpha-chymotrypsin (ChT), histone, and cytochrome c (CytC). The enthalpy and entropy changes for the complex formation depend upon the nanoparticle structure and the surface characteristics of the proteins, e.g., distributions of charged and hydrophobic residues on the surface. Enthalpy-entropy compensation studies on these NP-protein systems indicate an excellent linear correlation between DeltaH and TDeltaS with a slope (alpha) of 1.07 and an intercept (TDeltaS0) of 35.2 kJ mol(-1). This behavior is closer to those of native protein-protein systems (alpha = 0.92 and TDeltaS0 = 41.1 kJ mol(-1)) than other protein-ligand and synthetic host-guest systems.

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Metadata

Authors
De, M., You, C.-C., Srivastava, S., & Rotello, V. M.
Venue
Journal of the American Chemical Society
Published
2007-08-02
Volume
129
Issue
35
Pages
10747-10753
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
OpenAlex
W2014960272
Cited by
318
References
2
FWCI
10.18
Type
journal article
Language
en
Open access
closed

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