Specific His6-tag attachment to metal-functionalized polymersomes relies on molecular recognition
| Autor: | Cornelia G. Palivan, Pascal Tanner, Maria Ezhevskaya, Wolfgang Meier, Sabine Van Doorslaer, Rainer Nehring |
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| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Stereochemistry Fluorescence correlation spectroscopy Peptide binding 02 engineering and technology 010402 general chemistry 01 natural sciences Molecular recognition Materials Chemistry Copolymer Butadienes Histidine Physical and Theoretical Chemistry chemistry.chemical_classification Chemistry Vesicle Polymer 021001 nanoscience & nanotechnology 0104 chemical sciences 3. Good health Surfaces Coatings and Films Polyethylene Polymersome Biophysics Nanocarriers 0210 nano-technology Peptides Copper |
| Zdroj: | Journal of Physical Chemistry B The journal of physical chemistry : B : condensed matter, materials, surfaces, interfaces and biophysical |
| ISSN: | 1520-5207 1520-6106 |
| Popis: | The development of nanocarriers for drug/protein delivery is in focus today as they can serve to both decrease dosages and improve localization to a desired biological compartment. A powerful tool to functionalize these carriers is specific affinity tagging supported by molecular recognition a key principle in biology. However the geometry of the binding region in a molecular recognition process and thus its conformation and specifi city are in many cases poorly understood. Here we demonstrate that short model peptides His6 tags selectively recognize CuII trisnitrilotriacetic acid moieties (CuII trisNTA) when exposed at the surfaces of polymer vesicles designed to serve as nanocarriers or as surfaces for proteins binding. A mixture of poly(butadiene) b poly(ethylene oxide) (PB b PEO) and Cu II trisNTA functionalized PB b PEO diblock copolymers (10:1) self assembles in aqueous solution generating vesicles with a hydrodynamic radius of approximately 100 nm as established by light scattering and TEM. Fluorescently labeled His6 tags specifically bind to metal centers exposed on vesicles' surface with a dissociation constant of 0.6 ± 0.2 µM as determined by fluorescence correlation spectroscopy. The significant rearrangement in the geometry of the metal center upon peptide binding was characterized by a combination of CW EPR pulse EPR and DFT computations. Understanding the binding configuration around the metal center inside NTA pocket exposed at the surface of vesicles supports further development of efficient targetable nanocarriers that can be recognized selectively by molecular recognition in a biological environment and facilitates their immobilization on solid supports and their use in two dimensional protein arrays. (Figure Presented) © 2012 American Chemical Society. |
| Databáze: | OpenAIRE |
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