Light chain (AL) amyloidosis is a disease that occurs due to the presence of a small plasma-cell clone, which produces amyloidogenic light chains. These chains can misfold and aggregate, leading to the deposition of amyloid fibrils in tissues. If left untreated or if treatment is ineffective, this can result in irreversible organ dysfunction and eventual death. Current therapeutic treatments generally target and remove the clonal plasma cell population responsible for secreting full-length light chains which is not always effective or safe, however, a different approach to halt pathological LC misfolding would be to inhibit the amyloidogenesis cascade at its starting point. Small molecules have been identified that have the ability to bind to highly conserved residues in the interface between heavy and light chains which can be used to potentially impede the process of amyloid fibril deposition before the native FL LC can misfold or undergo proteolysis to form amyloid fibrils. To test whether small-molecule kinetic stabilizers are effective in stabilizing light chains, we measured the ability of the small molecule to bind to LCs, and the ability of light chains to aggregate and unfold in the absence and presence of small-molecule. Our findings suggest that the binding of stabilizers to the interface between variable domains of the LC dimer can increase equilibrium stability and decrease the rate of aggregation, thereby delaying the onset of amyloid formation.