Related Experiment Video
Updated: Apr 27, 2026

Direct Protein Delivery to Mammalian Cells Using Cell-permeable Cys2-His2 Zinc-finger Domains
Published on: March 25, 2015
Environmentally responsive histidine-carboxylate zipper formation between proteins and nanoparticles
Rubul Mout1, Gulen Yesilbag Tonga, Moumita Ray
1Department of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA. rotello@chem.umass.edu.
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.
More Related Videos
06:26Synthesis of Stimuli-responsive Nanogels using Aqueous One-step Crosslinking and Co-nanopolymerization
Published on: January 24, 2025
08:42Determination of Zeta Potential via Nanoparticle Translocation Velocities through a Tunable Nanopore: Using DNA-modified Particles as an Example
Published on: October 26, 2016
Related Concept Videos
Protein-protein Interfaces
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...