acting insulin analogues, the so-called ‘designer insulins’, developed through genetic engineering in the 1990s, paved the way for more physiological insulin therapy. They were theoretically less problematic in terms of hypoglycemia and patient satisfaction. They made the treatment flexible, safer and simpler. Newer Insulins are faster acting preprandial insulin or longer acting basal insulin which provide a constant concentration with no peak increase in insulin level. Newer analogues exist as monomers and are absorbed much faster (insulin aspart or lispro) or absorbed very slowly (insulin glargine or detemir).The newer analogues have increased stability, less variability and selective action which will help in developing individualized treatment suitable to specific patient characteristics and will improve glycaemic control. Structure function studies have shown that amino acid essential for binding the insulin receptor include A 1- 3,19, B-6,12,23-25. The B 26-30 region is critical for insulin receptor recognition and has been the site preferred for structural alteration with the aim to modify the pharmacokinetic profile of insulin molecule  . It is also important in mediating the formation of dimers.