Single-Molecule Multivalent Interactions Revealed by Plasmon-Enhanced Fluorescence.

ABSTRACT: Multivalency as an interaction principle is widely utilized in nature. It enables specific and strong binding by multiple weak interactions through enhanced avidity and is a core process in immune recognition and cellular signaling, which is also a current concept in drug design. Here, we use the high signals from plasmon-enhanced fluorescence of nanoparticles to extract binding kinetics and dynamics of multivalent interactions on the single-molecule level and in real time. We study mono-, bi-, and trivalent binding interactions using a DNA Holliday Junction as a model construct with programmable valency and introduce a step-binding model for binding kinetics relevant for structured macromolecules by including an experimentally extractable binding restriction term ω to quantify the effects

SUBMITTER: Okholm KR 

PROVIDER: S-EPMC11698027 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature