Glycoform Differentiation by a Targeted, Self-Assembled, Pattern-Generating Protein Surface Sensor
| Autor: | Ronny Peri-Naor, Zohar Pode, Aharon Rabinkov, Naama Lahav-Mankovski, David Margulies, Leila Motiei |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Anthracenes
Scaffold Glycosylation Molecular Structure Surface Properties Supramolecular chemistry Therapeutic protein Nanotechnology General Chemistry 010402 general chemistry 01 natural sciences Biochemistry Boronic Acids Catalysis 0104 chemical sciences Self assembled chemistry.chemical_compound Colloid and Surface Chemistry chemistry Oligodeoxyribonucleotides Periplasmic Binding Proteins Surface protein Function (biology) |
| Zdroj: | Journal of the American Chemical Society. 142(37) |
| ISSN: | 1520-5126 |
| Popis: | A method for generating targeted, pattern-generating, protein surface sensors via the self-assembly of modified oligodeoxynucleotides (ODNs) is described. The simplicity by which these systems can be created enabled the development of a sensor that can straightforwardly discriminate between distinct glycoform populations. By using this sensor to identify glycosylation states of a therapeutic protein, we demonstrate the diagnostic potential of this approach as well as the feasibility of integrating a wealth of supramolecular receptors and sensors into higher-order molecular analytical devices with advanced properties. For example, the facile device integration was used to attach the well-known anthracene-boronic acid (An-BA) probe to a biomimetic DNA scaffold and consequently, to use the unique photophysical properties of An-BA to improve glycoform differentiation. In addition, the noncovalent assembly enabled us to modify the sensor with a trinitrilotriacetic acid (tri-NTA)-Ni2+ complex, which endows it with selectivity toward a hexa-histidine tag (His-tag). The selective responses of the system to diverse His-tag-labeled proteins further demonstrate the potential applicability of such sensors and validate the mechanism underlying their function. |
| Databáze: | OpenAIRE |
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