What is insulin made of

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Understanding the Composition of Insulin

Insulin Structure: Amino Acids and Peptide Chains

Insulin is a peptide hormone composed of 51 amino acids arranged in two distinct peptide chains, known as the A and B chains. These chains are linked by three disulfide bonds, two of which connect the A and B chains, while the third is an intrachain bond within the A chain 157. The A chain consists of 21 amino acids, and the B chain is made up of 30 amino acids .

Molecular Assembly: Monomers, Dimers, and Hexamers

Although insulin is biologically active as a monomer, it typically exists in more complex forms during its biosynthesis and storage. Insulin molecules can assemble into dimers and, in the presence of zinc ions, further aggregate into hexamers 127. This hexameric form is particularly stable and is the primary storage form of insulin in the pancreas 210.

Structural Conformations: Helices and Sheets

The insulin molecule exhibits various structural conformations, including α-helices and β-sheets. The B chain, in particular, can adopt different helical structures depending on its state (monomeric, dimeric, or hexameric) and the presence of specific reagents like chloride and phenol 14. These conformational changes are crucial for insulin's stability and function.

Chemical Synthesis and Challenges

The chemical synthesis of insulin is a complex process due to its intricate structure. The synthesis involves the stepwise formation of the peptide chains and the correct pairing of disulfide bonds. Techniques such as solid-phase peptide synthesis (SPPS) and biomimetic folding have been developed to improve the efficiency and yield of synthetic insulin 368. Despite these advancements, the synthesis remains challenging due to the poor physicochemical properties of the individual chains and the hormone itself .

Biosynthesis and Storage

Insulin is initially synthesized as a single-chain precursor called preproinsulin, which includes an N-terminal signal sequence and a connecting peptide. This precursor undergoes several processing steps, including the removal of the signal sequence and the formation of disulfide bonds, to become proinsulin. Proinsulin is then converted to insulin and stored in the pancreas as zinc-containing hexamers 910.

Conclusion

Insulin is a small yet complex protein hormone essential for glucose regulation. Its structure consists of two peptide chains linked by disulfide bonds, and it can exist in various forms, from monomers to hexamers. The chemical synthesis of insulin is intricate, involving precise folding and bond formation. Understanding the molecular structure and biosynthesis of insulin is crucial for developing effective diabetes treatments and improving synthetic insulin production.

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Most relevant research papers on this topic

Molecular structure of insulin: the insulin monomer and its assembly.

The insulin molecule has two main conformations (B9-B20 and B1-B20), and its conformation in hexamers can influence the behavior and properties of insulin preparations.

Highly Cited

1989·

102citations

·U. Derewenda et al.

Progress in Simulation Studies of Insulin Structure and Function

Molecular dynamics simulations have helped elucidate insulin's conformational dynamics, potentially aiding in the development of synthetic insulin analogs.

2022·

15citations

·Biswajit Gorai et al.

The Chemical Synthesis of Insulin: An Enduring Challenge.

The chemical synthesis of insulin has been achieved using various strategies, leading to the production of novel analogues with optimized structural and functional features, potentially benefiting diabetes treatment.

2021·

33citations

·J. Karas et al.

Insulin: a small protein with a long journey

Understanding insulin's structure has led to the design of a new ultra-stable, fast-acting, and cheaper insulin formulation for diabetes mellitus patients.

2010·

69citations

·Q. Hua

Treatment of Diabetes Mellitus

Insulin acts by releasing glucose from the blood into the cells of the pancreas, where it stimulates the production of insulin and its effects on diabetes are well-understood.

Highly Cited

1959·

279citations

·W. Oakley

Total Synthesis of desB30 Insulin Analogues by Biomimetic Folding of Single‐Chain Precursors

This study successfully synthesized desB30 insulin analogues using biomimetic folding of single-chain precursors, resulting in a 6-7% yield and a straightforward, labor-free process for producing diabetes treatments.

2008·

44citations

·A. P. Tofteng et al.

The ABC of Insulin: The Organic Chemistry of a Small Protein.

Insulin's structure allows for chemo-selective reactions, enabling potential new treatments for diabetes and other diseases.

2020·

24citations

·M. Østergaard et al.

The Chemical Synthesis of Insulin: From the Past to the Present

The chemical synthesis of insulin has advanced, but the assembly of its two peptide chains remains challenging and requires improved methods for overcoming limitations.

2011·

25citations

·A. Belgi et al.

The chemistry and biochemistry of insulin.

Insulin promotes glycogen, fat, and protein synthesis and lowers blood sugar levels, but its exact molecular mechanism of action remains unknown.

1966·

56citations

·H. Klostermeyer et al.

The role of assembly in insulin's biosynthesis.

Insulin biosynthesis involves assembly to the zinc-containing hexamer, which plays a crucial role in its conversion to insulin and its storage as microcrystals.

Highly Cited

1998·

508citations

·G. Dodson et al.

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