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Full Paper
Isomeric Control of Protein Recognition with Amino Acid- and Dipeptide-Functionalized Gold Nanoparticles
Article first published online: 30 OCT 2007
DOI: 10.1002/chem.200701234
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
You, C.-C., Agasti, S. and Rotello, V. (2008), Isomeric Control of Protein Recognition with Amino Acid- and Dipeptide-Functionalized Gold Nanoparticles. Chemistry - A European Journal, 14: 143–150. doi: 10.1002/chem.200701234
Publication History
- Issue published online: 17 DEC 2007
- Article first published online: 30 OCT 2007
- Manuscript Received: 7 AUG 2007
Funded by
- NIH. Grant Number: GM077173
Keywords:
- chirality;
- gold;
- molecular recognition;
- nanoparticles;
- proteins
Graphical Abstract
Recognition of protein surfaces: Calorimetric investigation revealed that nanoparticles (NPs) bearing enantiomeric and diastereoisomeric amino acids/dipeptides (see graphic) display distinctly different binding affinities toward protein targets. This isomeric control of protein recognition has been demonstrated to arise from the noncompensatory enthalpy and entropy contributions in the complex formation.
Abstract
Amino acid and dipeptide-functionalized gold nanoparticles (NPs) possessing L/D-leucine and/or L/D-phenylalanine residues have been constructed in order to target the surfaces of α-chymotrypsin (ChT) and cytochrome c (CytC). Isothermal titration calorimetry (ITC) was conducted to evaluate the binding thermodynamics and selectivity of these NP–protein interactions. The chirality of the NP end-groups substantially affects the resultant complex stability, with up to 20-fold differences seen between particles of identical hydrophobicity, demonstrating that structural information from the ligands can be used to control protein recognition.