Hey there! As a supplier of Exendin - 4, I often get asked about its chemical structure. So, let's dive right into it and break down what makes Exendin - 4 tick.
Exendin - 4 is a peptide, which is basically a short chain of amino acids. It's got 39 amino acids in total, and these amino acids are like the building blocks that come together to form this unique molecule.
Let's start by looking at the general structure of an amino acid. Every amino acid has a central carbon atom, called the alpha - carbon. Attached to this alpha - carbon, there's an amino group (NH₂), a carboxyl group (COOH), a hydrogen atom, and a side chain, which is what makes each amino acid different from the others.
In Exendin - 4, these 39 amino acids are linked together through peptide bonds. A peptide bond is formed when the carboxyl group of one amino acid reacts with the amino group of another amino acid, releasing a molecule of water in the process. This chain of amino acids forms the primary structure of Exendin - 4.
The sequence of these 39 amino acids in Exendin - 4 is crucial. It's what gives the peptide its specific biological activity. The exact sequence is: His - Gly - Glu - Gly - Thr - Phe - Thr - Ser - Asp - Leu - Ser - Lys - Gln - Met - Glu - Glu - Glu - Ala - Val - Arg - Leu - Phe - Ile - Glu - Trp - Leu - Lys - Asn - Gly - Gly - Pro - Ser - Ser - Gly - Ala - Pro - Pro - Pro - Ser.
Now, the primary structure is just the beginning. The peptide doesn't just stay as a straight chain. It folds up in three - dimensional space, and this folding is determined by various forces.
One of the important folding patterns is the secondary structure. Exendin - 4 has regions of alpha - helices. An alpha - helix is a coiled structure where the peptide chain twists around like a spiral staircase. These alpha - helices are stabilized by hydrogen bonds between the carbonyl oxygen of one amino acid and the amide hydrogen of an amino acid four residues away.
The tertiary structure of Exendin - 4 is the overall three - dimensional shape that results from the folding of the secondary structures. It's like the final shape of a ball of yarn after it's been carefully wound up. The tertiary structure is held together by a variety of forces, including hydrogen bonds, disulfide bonds (although Exendin - 4 doesn't have disulfide bonds as there are no cysteine residues which can form them), hydrophobic interactions, and ionic bonds.
The unique chemical structure of Exendin - 4 is what allows it to interact with specific receptors in the body. It binds to the glucagon - like peptide - 1 (GLP - 1) receptor. When it binds to this receptor, it activates a series of signaling pathways inside the cell, which ultimately leads to increased insulin secretion, reduced glucagon secretion, slowed gastric emptying, and decreased food intake.
Now, if you're into peptides, you might also be interested in some other related ones. Check out our Fibronectin - Binding Protein, Protein Kinase C Substrate, and Substance P. These peptides also have their own unique chemical structures and biological functions.
As a supplier of Exendin - 4, we ensure that our product has the correct chemical structure. We use advanced purification and analysis techniques to make sure the peptide is of high quality and has the right sequence and folding. We understand the importance of the chemical structure in determining the biological activity of Exendin - 4, and we take every step to maintain its integrity.
If you're in the market for Exendin - 4 or any of our other peptide products, we'd love to have a chat with you. Whether you're a researcher working on diabetes studies or a pharmaceutical company looking for a reliable peptide supplier, we're here to help. Just reach out, and we can start a discussion about your specific needs.
In conclusion, the chemical structure of Exendin - 4 is a fascinating combination of amino acid sequence, secondary and tertiary folding, which together give it its important biological functions. And if you're interested in exploring more about peptides or need a quality supply of Exendin - 4, don't hesitate to get in touch.
References
- Drucker DJ. The biology of incretin hormones. Cell Metab. 2006;3(3):153 - 165.
- Gallwitz B, Holst JJ. Glucagon - like peptide 1 agonists in the treatment of type 2 diabetes mellitus. Lancet. 2009;373(9673):2181 - 2193.