Diabetes affects millions of people worldwide. Depending upon the medical condition of the patient, one or more of insulin, glucagon, GLP-1, exenatide, pramlintide are used for the treatment. However, these peptides are highly susceptible to oligomerization and fibrillation which lead to major storage and handling issues and also immunogenicity. Various strategies are routinely used to stabilize the protein by introducing chemical modifications to the protein structure such as PEGylation, lipidation, glycosylation, cyclization, and non-natural amino acids. As a natural modification, glycosylation is considered to be the most useful modifications as it is known to improve the therapeutic efficacy. Chemical methods enable the acquisition of homogenous glycopeptides. We will report the development of novel chemical strategies for the synthesis of glycoinsulin and glycoglucagon in excellent yields. We will also report that both glycoinsulin and glycoglucagon analogues are highly potent full agonists at the insulin and glucagon receptors respectively. More importantly, they exhibit markedly reduced propensity for fibrillation, as well as enhanced thermal and metabolic stability. Thus, our novel insulin and glucagon analogues lead to the production of stable formulations that will improve patient compliance and minimize wastage.