title: Isomeric control of protein recognition with amino acid- and dipeptide-functionalized gold nanoparticles.
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.
authors.affiliation: Department of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, MA 01002, USA.
authors.forename: Chang-Cheng
authors.initials: CC
authors.lastname: You
authors.forename: Sarit S
authors.initials: SS
authors.lastname: Agasti
authors.forename: Vincent M
authors.initials: VM
authors.lastname: Rotello
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D000818:Animals; D002151:Calorimetry; D002417:Cattle; D002918:Chymotrypsin / Q000737:chemistry*; D002942:Circular Dichroism; D045304:Cytochromes c / Q000737:chemistry*; D004151:Dipeptides / Q000737:chemistry*; D006046:Gold / Q000737:chemistry*; D006736:Horses; D057927:Hydrophobic and Hydrophilic Interactions; D007536:Isomerism; D008024:Ligands; D053768:Metal Nanoparticles / Q000737:chemistry*; D008958:Models, Molecular; D013696:Temperature; D013816:Thermodynamics; D017186:Titrimetry
chemical_list: D000596:Amino Acids; D004151:Dipeptides; D008024:Ligands; D006046:Gold; D045304:Cytochromes c; D002918:Chymotrypsin; C117608:alpha-chymotrypsin