title: Environmentally responsive histidine-carboxylate zipper formation between proteins and nanoparticles.
abstract: Interfacing synthetic materials with biomacromolecules provides new systems for biological applications. We report the creation of a reversible multivalent supramolecular "zipper" recognition motif between gold nanoparticles and proteins. In this assembly, carboxylate-functionalized nanoparticles interact strongly with oligohistidine tags. This interaction can be tuned through His-tag length, and offers unique binding profiles based on the pH and electrolyte concentration of the medium.
authors: Department of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA. rotello@chem.umass.edu.
authors: Rubul
authors: R
authors: Mout
authors: Gulen Yesilbag
authors: GY
authors: Tonga
authors: Moumita
authors: M
authors: Ray
authors: Daniel F
authors: DF
authors: Moyano
authors: Yuqing
authors: Y
authors: Xing
authors: Vincent M
authors: VM
authors: Rotello
mesh_terms: D001672:Biocompatible Materials / Q000737:chemistry*; D002264:Carboxylic Acids / Q000737:chemistry*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000378:metabolism; D005818:Genetic Engineering; D006046:Gold / Q000737:chemistry; D049452:Green Fluorescent Proteins / Q000737:chemistry; D006639:Histidine / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007477:Ions; D008024:Ligands; D046911:Macromolecular Substances / Q000737:chemistry; D053768:Metal Nanoparticles / Q000737:chemistry; D053758:Nanoparticles / Q000737:chemistry*; D011485:Protein Binding; D015202:Protein Engineering; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D001672:Biocompatible Materials; D002264:Carboxylic Acids; D007477:Ions; D008024:Ligands; D046911:Macromolecular Substances; D011506:Proteins; D011994:Recombinant Proteins; D049452:Green Fluorescent Proteins; D006639:Histidine; D006046:Gold