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The chemical synthesis of peptides can be carried out using classical solution-phase techniques, although these have been replaced in most research and development settings by solid-phase methods (see below). [3] Solution-phase synthesis retains its usefulness in large-scale production of peptides for industrial purposes moreover.
Native chemical ligation forms the basis of modern chemical protein synthesis, and has been used to prepare numerous proteins and enzymes by total chemical synthesis. The payoff in the native chemical ligation method is that coupling long peptides by this technique is typically near quantitative and provides synthetic access to large peptides ...
The "chemical ligation" concept was introduced by Kent in the early 1990s. [1] It consisted of a novel approach to the covalent condensation of unprotected peptide segments by means of "unique, mutually reactive functionalities, one on each reacting peptide segment, designed to react only with each other and not with any of the functional groups found in (native) peptides".
In chemistry, solid-phase synthesis is a method in which molecules are covalently bound on a solid support material and synthesised step-by-step in a single reaction vessel utilising selective protecting group chemistry. Benefits compared with normal synthesis in a liquid state include: High efficiency and throughput; Increased simplicity and speed
In 1990 three groups described methods for preparing peptide libraries by biological methods [15] [16] [17] and one year later Fodor et al. published a remarkable method for synthesis of peptide arrays on small glass slides. [18] A "parallel synthesis" method was developed by Mario Geysen and his colleagues for preparation of peptide arrays. [19]
These rely on organic synthesis techniques such as chemical ligation to produce peptides in high yield. [50] Chemical synthesis allows for the introduction of non-natural amino acids into polypeptide chains, such as attachment of fluorescent probes to amino acid side chains. [51] These methods are useful in laboratory biochemistry and cell ...
Natural product synthesis serves as a critical tool across various scientific fields. In organic chemistry, it tests new synthetic methods, validating and advancing innovative approaches. In medicinal chemistry, natural product synthesis is essential for creating bioactive compounds, driving progress in drug discovery and therapeutic ...
[1] [2] A polypeptide is a longer, continuous, unbranched peptide chain. [3] Polypeptides that have a molecular mass of 10,000 Da or more are called proteins . [ 4 ] Chains of fewer than twenty amino acids are called oligopeptides , and include dipeptides , tripeptides , and tetrapeptides .