Probing Specificity of Protein-Protein Interactions with Chiral Plasmonic Nanostructures.
Marion RodierChantal KeijzerJoel MilnerAffar S KarimullahLaurence D BarronNikolaj GadegaardAdrian J LapthornMalcolm KadodwalaPublished in: The journal of physical chemistry letters (2019)
Protein-protein interactions (PPIs) play a pivotal role in many biological processes. Discriminating functionally important well-defined protein-protein complexes formed by specific interactions from random aggregates produced by nonspecific interactions is therefore a critical capability. While there are many techniques which enable rapid screening of binding affinities in PPIs, there is no generic spectroscopic phenomenon which provides rapid characterization of the structure of protein-protein complexes. In this study we show that chiral plasmonic fields probe the structural order and hence the level of PPI specificity in a model antibody-antigen system. Using surface-immobilized Fab' fragments of polyclonal rabbit IgG antibodies with high specificity for bovine serum albumin (BSA), we show that chiral plasmonic fields can discriminate between a structurally anisotropic ensemble of BSA-Fab' complexes and random ovalbumin (OVA)-Fab' aggregates, demonstrating their potential as the basis of a useful proteomic technology for the initial rapid high-throughput screening of PPIs.
Keyphrases
- protein protein
- small molecule
- single molecule
- capillary electrophoresis
- ionic liquid
- loop mediated isothermal amplification
- label free
- structural basis
- mass spectrometry
- living cells
- neural network
- molecular docking
- molecular dynamics simulations
- machine learning
- convolutional neural network
- transcription factor
- dna binding