Biomimetic interactions of proteins with functionalized nanoparticles: a thermodynamic study.
J Am Chem Soc
; 129(35): 10747-53, 2007 Sep 05.
Article
de En
| MEDLINE
| ID: mdl-17672456
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.
Recherche sur Google
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Chymotrypsine
/
Histone
/
Matériaux biomimétiques
/
Cytochromes c
/
Nanoparticules métalliques
/
Acides aminés
Type d'étude:
Prognostic_studies
Langue:
En
Journal:
J Am Chem Soc
Année:
2007
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique