化学
纳米颗粒
纳米技术
化学工程
工程类
材料科学
作者
Mrinmoy De,Chang‐Cheng You,Sudhanshu Srivastava,Vincent M. Rotello
摘要
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 α-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 ΔH and TΔS with a slope (α) of 1.07 and an intercept (TΔS0) of 35.2 kJ mol-1. This behavior is closer to those of native protein−protein systems (α = 0.92 and TΔS0 = 41.1 kJ mol-1) than other protein−ligand and synthetic host−guest systems.
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