Subset of Fluorophores Is Responsible for Radiation Brightening in Viromimetic Particles
Year: 2021
Type: article
Abstract: , to a cooperative process occurring within a subset of the virus-supported fluorophores. Until now, the distribution of fluorophores among potential conjugation sites and the nature of the active subset remained unknown. With the help of mass spectrometry and molecular dynamics simulations, we found which conjugation sites in the brome mosaic virus capsid are accessible to fluorophores. Reactive external surface lysines but also those at the lumenal interface where the coat protein N-termini are located showed virtually unrestricted access to dyes. The third type of labeled lysines was situated at the intercapsomeric interfaces. Through limited proteolysis of flexible N-termini, it was determined that dyes bound to them are unlikely to be involved in the radiation brightening effect. At the same time, specific labeling of genetically inserted cysteines on the exterior capsid surface alone did not lead to radiation brightening. The results suggest that lysines situated within the more rigid structural part of the coat protein provide the chemical environments conducive to radiation brightening, and we discuss some of the characteristics of these environments.
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: green
Awards: G3530726959, G3743496716, Protein Cross-Linking Technology and Applications, Phase I IUCRC at Indiana University: Center for Bioanalytic Metrology, Characterizing proteasome-substrate interactions by mass spectrometry proteomics, Super-radiant virus-like particles as targeted contrast agents for laser-guided surgery, G8764065780
OpenAlex ID: W3198858872
