PubMed · 810688
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B Willms. 1975-10-10. [Issue topic: Insulin, introduction].. https://pubmed.ncbi.nlm.nih.gov/810688/
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Adaptation to efficient heterologous expression is a prerequisite for recombinant proteins to fulfill their clinical and biotechnological potential. We describe a rational strategy to optimize the secretion efficiency in yeast of an insulin precursor by structure-based engineering of the folding stability. The yield of a fast-acting insulin analogue (Asp(B28)) expressed in yeast was enhanced 5-fold by engineering a specific interaction between an aromatic amino acid in the connecting peptide and a phenol binding site in the hydrophobic core of the molecule. This insulin precursor is characterized by significantly enhanced folding stability. The improved folding properties enhanced the secretion efficiency of the insulin precursor from 10 to 50%. The precursor remains fully in vitro convertible to mature fast-acting insulin.
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The author summarizes basic findings on the formation of insulin, its secretion and bond to insulin receptors and other phenomena at the post-receptor level. He summarizes basic indications for insulin treatment also beyond the sphere of diabetology. In a separate part the author summarizes briefly the history since the discovery of insulin up to the present time with modern therapeutic procedures (insulin injections, insulin pumps). The greatest part of the paper is devoted to contemporary insulin preparations and their use in therapy. A separate section is devoted also to insulin absorption and ways to influence its action. Attention is drawn to some differences in insulin absorption in relation to the site of injection, insulin concentration, body temperature and other factors which can be influenced. The objective of the paper is an overview of insulin and its use in therapy since to discovery of insulin to the present time.