Nanoparticle mobility over a surface as a probe for weak transient disordered peptide-peptide interactions

Abstract

Weak interactions form the core basis of a vast number of biological processes, in particular, those involving intrinsically disordered proteins. Here, we establish a new technique capable of probing these weak interactions between synthetic unfolded polypeptides using a convenient yet efficient, quantitative method based on single particle tracking of peptide-coated gold nanoparticles over peptide-coated surfaces. We demonstrate that our technique is sensitive enough to observe the influence of a single amino acid mutation on the transient peptide-peptide interactions. Furthermore, the effects of buffer salinity, expected to alter weak electrostatic interactions, are also readily detected and examined in detail. The method presented here has the potential to evaluate in a high throughput manner, weak interactions for a wide range of disordered proteins, polypeptides, and other biomolecules.

References in corpus (4)

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• Strange kinetics of bulk-mediated diffusion on lipid bilayers
• Phosphorylation-induced mechanical regulation of intrinsically disordered neurofilament protein assemblies
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Cited by in corpus (5)

• Two Coupled Mechanisms Produce Fickian, yet non-Gaussian Diffusion in Heterogeneous Media
• Order from disorder with intrinsically disordered peptide amphiphiles
• Motion of an active particle with dynamical disorder
• Intrinsically Disordered Proteins at the Nano-scale
• Hidden Markov modeling of single particle diffusion with stochastic tethering