Surface Plasmon Resonance: A Useful Strategy for the Identification of Small Molecule Argonaute 2 Protein Binders
Autor: | Francesco Fazi, Gianni Colotti, Elena Poser, Ilaria Genovese, Teresa Bellissimo, Silvia Masciarelli |
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Jazyk: | angličtina |
Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
Analyte Materials science education Ligand Ligands Protein-inhibitor interaction Small molecules Surface plasmon resonance Argonaute Proteins High-Throughput Screening Assays Humans MicroRNAs Molecular Docking Simulation Protein Binding Small Molecule Libraries Surface Plasmon Resonance 03 medical and health sciences 0302 clinical medicine molecular biology Molecule genetics analyte ligand protein-inhibitor interaction small molecules surface plasmon resonance business.industry Argonaute Small molecule 030104 developmental biology Biochemistry Docking (molecular) 030220 oncology & carcinogenesis Optoelectronics Thin metal Settore BIO/17 - ISTOLOGIA business Refractive index |
Zdroj: | pp. 223–237. New York: Springer, 2017 info:cnr-pdr/source/autori:Poser, Elena; Genovese, Ilaria; Masciarelli, Silvia; Bellissimo, Teresa; Fazi, Francesco; Colotti, Gianni/titolo:Surface Plasmon Resonance: A Useful Strategy for the Identification of Small Molecule Argonaute 2 Protein Binders./titolo_volume:/curatori_volume:/editore: /anno:2017 Methods in Molecular Biology ISBN: 9781493965618 |
Popis: | Surface plasmon resonance (SPR) is one of the most important techniques for the detection and the characterization of molecular interactions. SPR technology is a label-free approach for monitoring biomolecular interactions in real time. The binding of analytes to molecules immobilized on a thin metal film (ligand) determines a change in the refractive index and, therefore in the angle of extinction of light, is reflected when polarized light hits the film, monitored in real time as a change in the position of the dip in reflected intensity. Since SPR detects mass, the technique is label-free.Here, we describe the use of SPR techniques to study the interaction between Argonaute 2 and small molecular compounds selected by means of high-throughput docking screening. |
Databáze: | OpenAIRE |
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