Work

Biomimetic Interactions of Proteins with Functionalized Nanoparticles: A Thermodynamic Study

Year: 2007

Type: article

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.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja071642q

Authors: Mrinmoy De, Chang-Cheng You, Sudhanshu Srivastava, Vincent M. Rotello

Institution: University of Massachusetts Amherst

Language: English

Topic: thermodynamics and calorimetric analyses

Subfield: Physical and Theoretical Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences

Award: Rapid Multi-Channel Serum Profiling for Cardiac Disease using Fluorescent Nanosensors