Article
Isomeric control of protein recognition with amino acid- and dipeptide-functionalized gold nanoparticles
Chemistry-A European Journal
(2008)
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 alpha-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.
Keywords
- chirality,
- gold,
- molecular,
- recognition,
- nanoparticles,
- proteins
Disciplines
Publication Date
January 1, 2008
Publisher Statement
DOI: 10.1002/chem.200701234
Citation Information
CC You, SS Agasti and VM Rotello. "Isomeric control of protein recognition with amino acid- and dipeptide-functionalized gold nanoparticles" Chemistry-A European Journal Vol. 14 Iss. 1 (2008) Available at: http://works.bepress.com/vincent_rotello/26/