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    Peptide Synthesis

    Peptides are used to prepare epitope-specific antibodies, map antibody epitopes and enzyme binding sites and to design novel enzymes, drugs and vaccines. While peptide synthesis used to be labor-intensive and produce low yields, improved methods of production and peptide chemistry have made peptide synthesis more available for general research applications.

    Peptide synthesis is characterized as the formation of a peptide bond between two amino acids. While there is no definitive definition of a peptide, it usually refers to flexible (little secondary structure) chains of up to 30-50 amino acids.

    The ability to form peptide bonds to link amino acids together is over 100 years old, although the first peptides to be synthesized, including oxytocin and insulin, did not occur for another 50-60 years, demonstrating the difficult task of chemically synthesizing chains of amino acids. In the last 50 years, advances in protein synthesis chemistry and methods have developed to the point where peptide synthesis today is a common approach in even high-throughput biological research and product and drug development.

    The benefit of peptide synthesis strategies today is that besides having the ability to make peptides that are found in biological specimens, creativity and imagination can be tapped to generate unique peptides to optimize a desired biological response or other result.

    Applications of synthetic peptides

    The invention of peptide synthesis in the fifties and sixties spurred the development of different application areas in which synthetic peptides are now used, including the development of epitope-specific antibodies against pathogenic proteins, the study of protein functions and the identification and characterization of proteins. Furthermore, synthetic peptides are used to study enzyme-substrate interactions within important enzyme classes such as kinases and proteases, which play a crucial role in cell signaling.

    In cell biology, receptor binding or the substrate recognition specificity of newly discovered enzymes can often be studied using sets of homologous synthetic peptides. Synthetic peptides can resemble naturally occurring peptides and act as drugs against cancer and other major diseases. Finally, synthetic peptides are used as standards and reagents in mass spectrometry (MS)-based applications. Synthetic peptides play a central role in MS-based discovery, characterization and quantitation of proteins, especially those that serve as early biomarkers for diseases.

    Solid-phase peptide synthesis (SPPS)

    Solid-phase synthesis is a common technique for peptide synthesis. Usually, peptides are synthesised from the carbonyl group  side (C-terminus) to amino group side (N-terminus) of the amino acid chain in the SPPS method, although peptides are biologically synthesised in the opposite direction in cells. In peptide synthesis, an amino-protected amino acid is bound to a solid phase material or resin (most commonly, low cross-linked polystyrene beads), forming a covalent bond between the carbonyl group and the resin, most often an amido or an ester bond.[6] Then the amino group is deprotected and reacted with the carbonyl group of the next N-protected amino acid. The solid phase now bears a dipeptide. This cycle is repeated to form the desired peptide chain. After all reactions are complete, the synthesised peptide is cleaved from the bead.

    The protecting groups for the amino groups mostly used in the peptide synthesis are 9-fluorenylmethyloxycarbonyl group (Fmoc) and t-butyloxycarbonyl (Boc). A number of amino acids bear functional groups in the side chain which must be protected specifically from reacting with the incoming N-protected amino acids. In contrast to Boc and Fmoc groups, these have to be stable over the course of peptide synthesis although they are also removed during the final deprotection of peptides.

    Our peptides are made from amino acids and have been chemically synthesized by solid-phase peptide synthesis (1.synthesis, 2.cleavage, 3.purification, 4.lyophilization). The ingredients and finished products were not derived from any animal or cell culture and does not contain any animal or cell culture.

    Not for human use. Used only for in-vitro research, such as Receptor-ligand binding studies, Enzyme activity assays, Cell proliferation assays, Cell signaling assays, Epitope mapping and Analytical studies.

    THE GOODS OFFERED BY THE SELLER IS INTENDED FOR SCIENTIFIC AND DEVELOPMENT PURPOSES ONLY. The goods offered by the Seller include chemical substances that shall not be used as a drug, medicine, active substance, medical aid, cosmetic product, a substance for production of a cosmetic product neither for human consumption that is any food or food supplement or otherwise similarly used on humans or animals.