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Peptide chemistry has gone through more than 100 years of glorious history, in 1902, Emil Fischer first began to focus on peptide synthesis, due to too little knowledge in peptide synthesis, synthesis of progress is quite slow when using benzoyl, ACETYLATED, and difficult, peptide chains and is prone to breaking. Until 1932, Max Bergmann, who started using cbz (Z) to protect Alpha-amino, the protecting groups can be used in catalytic hydrogenation or HYDROBROMIC ACID quantitative removal of conditions, peptide synthesis began to have a certain degree of development. To has in the 1950 of the 20th century, with increasingly more of biological activity more peptide of found, greatly promoted has organic chemistry home are on more peptide synthesis method and protection base of research, so this a stage of research results also very rich, people synthesis has large of biological activity more peptide, including oxytocin pigment (oxytocin), insulin,, while in more peptide synthesis method and amino acids protection base above also made has many results, this for later of solid synthesis method of appeared also provides has experiment and theory based. This stage, Fred Sanger invented the method for determination of amino acid sequence, and won the 1958 Nobel Prize in chemistry. Also he later invented the method of DNA sequencing, and again won the Nobel Prize in chemistry in 1980, becoming so far the only two scientists of the Nobel Prize in chemistry. 1963, Merrifield proposed has solid more peptide synthesis method (SPPS), this in more peptide chemical Shang has milestone meaning of synthesis method, a out, on due to its synthesis convenient, quickly, now has became more peptide synthesis of preferred method, then of development also proved has the method just a synthesis method, and also brings has organic synthesis Shang of once revolution, and became has a support independent of subject, solid organic synthesis (SPOS). Of course, Merrifield also won the 1984 Nobel Prize in chemistry. It is Merrifield, who after repeated screening of, eventually abandoned the cbz (Z) in use on a solid first tert-butoxycarbonyl (BOC) used to protect the α-amino group and used in solid-phase peptide synthesis, the quantitative removal under acidic conditions, and the response was very quick and 30min can respond fully. Because tert-butoxycarbonyl (BOC) method, the benzyl protecting groups is mostly based on the amino acid side chain (Bzl), also known as the BOC-Bzl policy. Also, Merrifield in the late 1960 of the 20th century invented the first fully automated peptide synthesizer, and the first synthesis of proteases, Ribonuclease (124 amino acids). Subsequent peptide chemistry research focused on solid-phase synthetic resin, condensation of peptide reagents, amino acid protecting group study. 1972,Lou Carpino first of 9-fluorenylmethoxycarbonyl (FMOC) used to protect Alpha-amino-, in alkaline conditions can be quickly removed, 10min will be able to respond fully, and due to its mild reaction conditions, quickly get widespread use, in the 1980 of the 20th century replaced the tert-butoxycarbonyl (BOC) as the preferred method of solid-phase peptide synthesis. The tert-butyl amino acid side chains are based on (But) and, therefore, also known as the FMOC-But policy. Meanwhile, polypeptide synthetic resin, condensation of reagents and amino acids to protect, including amino acids for synthesis of peptide orthogonal protection also achieved fruitful results.
into the 21st century with the study of proteomics, requires not only synthesis of peptide chemistry methods and more focus on peptide tag with the modified method, simulations of peptide and protein structure and function of the synthetic long peptide or protein synthesis.