Linkers were evaluated in lateral flow assay studies to determine the rapidity and efficiency of thiol-induced release from streptavidin bearing test-lines on nitrocellulose membranes. We show that an elongated azido-PEG3-SS-PEG4-biotin linker exhibited particularly rapid release kinetics within minutes which, when coupled with the exceptional binding capabilities of our 'dual-affinity' labels, enabled high-affinity re-binding of analytebound complexes at anti-FITC test lines of detection strips. Demonstrating the efficacy of our approach, we illustrate substantial sensitivity enhancements of 16-fold in a model system probing streptavidin capture receptor density and binding kinetics. Finally, we applied our approach to address a pervasive challenge in lateral flow assay development in the form of the limited diffusivity and capture kinetics of larger nanoparticles where, in a high sensitivity LFA system using 150 nm 'dual-affinity' labels, a 12-fold enhancement in limit of detection was realised when detecting antigen spiked in both buffer and human serum samples. Our 'capture-and-release' methodology emerges as a robust signal amplification technique with broad applicability across diverse LFA platforms, facilitated by adaptable protein modification strategies. Moreover, its rapid turnaround time (within 30 minutes) positions it as a promising diagnostic tool within the point-of-care testing landscape.