Capture-and-release strategies are ubiquitous in a variety of analytical or separation techniques, such as chromatography or immunoprecipitation, often with the aim of sequestering and enriching a target from its matrix, and subsequently triggering its release in a controlled manner. In the context of LFAs, the ability to enrich biomarkers in a sample volume represents a powerful opportunity towards bypassing poor assay kinetics. In the case of nucleic acid detection, biomarker enrichment has been demonstrated with the use of recombinase polymerase amplification (RPA) workflows as a sample pre-processing step. The application of such strategies for antigen-based LFAs, however, remains limited and comparatively difficult. Key examples of this include an immobilised metal-affinity chromatography (IMAC) inspired 'capture-and-release' approach where magnetic beads were utilised to manipulate sample concentration prior to LFA detection. Here, Bauer et al. relied on the affinity between Zn(II) and a characteristic histidine-rich motif in the structure of a malarial HRP2 antigen to afford specific, non-covalent capture prior to triggered elution using competitive ligands (such as imidazole). The application of this IMAC approach has been further explored by utilising non-covalent aptamer binding and hexahistidine-tagged antibodies to mediate 'capture-and-release' of non-histidine rich antigen targets in a similar fashion. Finally, studies by Moore et al. have shown that Zn(II) functionalised cellulose can be used to perform 'capture-and-release' of histidine-rich HRP2 antigens without relying on magnetic bead technologies, demonstrating improved potential for field-based testing. In each of these examples, sample pre-processing workflows require users to elute and collect the concentrated analyte sample as a flowthrough volume, which is then applied to a LFA test. Whilst efforts have sought to realise this approach with improved userfriendliness, for instance by moving from a tube containing magnetic beads to a cellulose membrane platform, these 'capture-and-release' examples are limited to being performed externally to the LFA device itself, ultimately necessitating users to handle and operate additional equipment to produce a LFA readout. Furthermore, the ability to selectively bind protein-based biomarkers in orthogonal ways without 'using-up' target epitopes has been highlighted as being non-trivial, presenting additional challenges when considering In this work, we describe an alternative LFA 'capture-and-release' methodology which seeks to address limitations regarding poor assay binding kinetics and generate signal amplification for enhanced sensitivity. To accomplish this, we introduce a folding 'twostrip' LFA architecture where antigen complexes are initially sequestered in a capture strip via the binding of immunoproteins modified with cleavable linkers. Following triggered linker cleavage, immunocomplexes are released and subsequently rebound with higher affinity in a detection strip where a higher density of particles and subsequent signal is obtained. The capabilities of this 'capture-and-release' strategy, which we term as the "AmpliFold" approach, is highlighted by augmenting the analyte binding region within capture strips. In the AmpliFold approach, a large surface area of capture receptors can be implemented to expand the opportunity for target capture, thus enabling a greater proportion of sample analyte to be sequestered and labelled. We demonstrate that the benefits of an enhanced degree of analyte capture could be realised within our AmpliFold platform where, through triggered linker cleavage, antigen-bound complexes could be redistributed and concentrated at the test line of the detection strip. For a model system, where low capture receptor density was used to emulate poor capture affinity, the AmpliFold platform was shown to yield a 16-fold sensitivity enhancement when compared to a traditional LFA format. The application of the AmpliFold approach was further demonstrated in a LFA system utilising large (150 nm) nanoparticle labels. Specifically, large capture areas were shown to address limited binding kinetics -associated with poor particle diffusivity -within an AmpliFold approach, resulting in a 12-fold improvement in sensitivity when compared to traditional LFA methods.