The proteomic characterization of the low-molecular-weight subfractions of Naja mandalayensis venom revealed that these samples are predominantly composed of toxin families commonly found in elapid venoms. Mass spectrometry analysis identified 19 proteins in SF4, 27 proteins in SF5, and 4 proteins in SFX, indicating a greater proteomic diversity within the subfractions that exhibited the strongest neuroprotective effects. Among the components detected were cytotoxins, three-finger toxins, and neurotoxins, all of which are well known for their ability to modulate neuronal receptors and affect membrane stability.