Isomeric control of protein recognition with amino acid- and dipeptide-functionalized gold nanoparticles.
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.
You
Chang-Cheng
CC
Department of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, MA 01002, USA.
Agasti
Sarit S
SS
Rotello
Vincent M
VM
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
D000596:Amino Acids; D004151:Dipeptides; D008024:Ligands; D006046:Gold; D045304:Cytochromes c; D002918:Chymotrypsin; C117608:alpha-chymotrypsin