Gaucher disease is really a rare genetic lysosomal storage disease characterised with a lack of function within the glucocerebrosidase (GCase) enzyme, which accounts for hydrolyzing glucocerebroside (GC) within the lysosome. When cells die, macrophages use GCase to interrupt lower GC, a significant constituent of cell walls. With deficient functional GCase, GC builds up inside the lysosome, giving rise to the look of bloated Gaucher cells this can be a hallmark from the disease. Certain mutated GCase proteins, after production within the endoplasmic reticulum (ER), don’t fold correctly and therefore are degraded through the proteasome path rather to be transported towards the lysosome. One therapeutic technique is to build up small molecule chaperones, which upon binding to GCase ensure proper folding and subsequent transport from the mutant protein towards the lysosome, where it may resume activity. The primary challenge in the introduction of molecular chaperones for Gaucher disease is the fact that all the formerly described chaperones are inhibitors from the enzyme. This complicates their clinical development, since it is hard to generate a suitable in vivo exposure where a substance exhibits chaperone activity, but doesn’t hinder the enzyme’s function. Using high throughput screening, we’ve identified two chemical series that don’t hinder the enzyme’s action, but could still facilitate its translocation towards the lysosome as measured by immunostaining of glucocerebrosidase in patient fibroblasts. These chemical series are exemplified by ML198 and ML266. These compounds function as beginning suggests create a novel approach towards small molecule strategy to patients struggling with Gaucher disease.