The stabilisation of recombinant glycosidases by exogenous ligands, known as pharmacological chaperones or enzyme stabilisers, has recently garnered great clinical interest. This strategy can prevent enzyme degradation in the blood, reducing required dosages of recombinant enzyme and extending IV injection intervals, thereby reducing side effects, improving patient lifestyles and treatment costs. While this therapeutic approach has been successfully implemented for treating Pompe and Fabry diseases, clinical studies for Gaucher disease using chaperones alone or in combination with enzyme replacement therapy (ERT) have been limited, and no small molecule chaperones have yet been approved for this condition. Developing such therapies requires selective and effective reversible GBA1 ligands. Here, we describe the development of a new class of selective macrocyclic peptide GBA1 ligands using random nonstandard peptides integrated discovery (RaPID) technology, and demonstrate their ability to bind and stabilise rhGBA1 in plasma at nanomolar concentrations. These cyclic peptides do not inhibit endogenous GBA1 in cells due to poor cell permeability but can stabilise extracellular rhGBA1 in plasma, presenting significant potential as a combinatorial ERT-pharmacological chaperone therapy for Gaucher disease.