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Our resins for solid phase peptide synthesis vary greatly ..
N2 - We describe a simple manually operated synthesizer for solid-phase peptide synthesis (SPPS). The synthesis is performed on standard polystyrene-based resin in a flow reactor under low-pressure conditions. The usefulness of the present configuration of SPPS is exemplified on the synthesis of two octapeptide and one decapeptide amides.
Solid-phase peptide synthesis consists of three distinct sets of operations: 1) chain assembly on a resin; 2) simultaneous or sequential cleavage and deprotection of the resin-bound, fully protected chain; and 3) purification and characterisation of the target peptide. Various chemical strategies exist for the chain assembly and cleavage/deprotection operations, but purification and characterisation methods are more or less invariant to the methods used to generate the crude peptide product.
Resins for Solid Phase Peptide and Organic Synthesis
Solvation and swelling of peptide-containing resins in solid-phase peptide synthesis, pp 5463 - 5470, Copyright 1980 American Chemical Society." class="disabled">
AB - We describe a simple manually operated synthesizer for solid-phase peptide synthesis (SPPS). The synthesis is performed on standard polystyrene-based resin in a flow reactor under low-pressure conditions. The usefulness of the present configuration of SPPS is exemplified on the synthesis of two octapeptide and one decapeptide amides.
Resins for Solid Phase Peptide Synthesis
We describe a simple manually operated synthesizer for solid-phase peptide synthesis (SPPS). The synthesis is performed on standard polystyrene-based resin in a flow reactor under low-pressure conditions. The usefulness of the present configuration of SPPS is exemplified on the synthesis of two octapeptide and one decapeptide amides.
CBL has played a historical role in advancing solid-phase synthesis to the large scale. CBL’s partnership with Roche and the Fuzeon program (a chemically complex anti-HIV peptide) required a manufacturing process capable of producing tons of solid phase resin which was then “loaded” with the necessary Fmoc amino acids. As a result of the CBL’s involvement in the Fuzeon program, the cost of raw materials, particularly resins, has decreased significantly, enabling complex peptides to be produced chemically at the ton scale.
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Solid-phase oligonucleotide synthesis - ATDBio
Solid phase organic synthesis is now the core technology employed in the automated routine peptide synthesis as well as in combinatorial chemistry. CBL was founded on the discovery and development of the trityl resins, including , also known as the “Barlos resin”. Today, CBL is recognized as the leading supplier of high-quality resins for solid-phase synthesis.
Peptide Synthesizer, Automated Peptide Synthesizer
Two major chemistries for solid phase peptide synthesis are Fmoc (base labile protecting group) and t-Boc (acid labile a-amino protecting group). Each method involves fundamentally different amino acid side-chain protection and consequent cleavage/deprotection methods, and resins; t-Boc method requires use of stronger HF containing anisole alone or anisole plus other scavengers, where peptide-resins assembled by Fmoc chemistry usually cleaved by less harsh Reagents K or R. Fmoc chemistry is known for peptide synthesis of higher quality and in greater yield than t-Boc chemistry. Impurities in t-Boc-synthesized peptides mostly attributed to cleavage problems, dehydration and t-butylation. For peptide assembly HBTU/HOBt, carbodiimide-mediated coupling and PyBOP/HOBt are the most popular routines. Peptides usually purified by reversed-phase HPLC (high performance liquid chromatography) using columns such as C-18, C-8, and C-4.
ChemPep - Peptide Synthesis, Peptide Array, HATU, …
In 1984 , an American chemist of Rockefeller University won the Nobel Prize for his contribution to the advancement of peptide chemistry. He developed a solid phase peptide synthesis (SPPS) methodology of peptides, which uses a polymer with reactive sites (solid supports, insoluble resin supports) that chemically combine to the developing peptide chain. That solved the problem of previous peptide chemistry. Using Merrifield's technique, the problems associated with low yields due to separation and purification are avoided. The polymer can be filtered and washed without mechanical losses because the polymer is very insoluble.
ChemPep: One stop for peptide synthesis
The most common and commercially available BFC comprise esters (-nitrophenyl, pentafluorophenyl, -hydroxysuccinimide, sulfo--hydroxysuccinimide), isothiocyanates, maleimides, hydrazides, α-haloamides for the reaction with nucleophilic functional groups (-NH2, -SH, -OH) of vector molecules and formation of amide, urea, thiourea, Schiff-base, or thioester bond . Methods have been developed for the conjugation with peptides by solid-phase peptide synthesis (SPPS) resulting in defined position and number of chelate moieties. The outcome of the conjugation in solution wherein peptides and proteins comprise several reactive sites is very often a mixture of bioconjugate molecules with various content of the chelator. Such heterogeneity may cause the interpretation ambiguity of the performance of such imaging agents. Regioselective conjugation to antibodies was achieved by enzymatic reaction with lysine and glutamine residues using bacterial and human tissue transglutaminase as catalysts .
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