SOLID PHASE PEPTIDE SYNTHESIS ..

US7176282B1 - Solid-phase peptide synthesis and agent …

289 (Solid-Phase Peptide Synthesis), (G ..

Present study was conducted from 23rd September 2010 to 10th Jan 2011. Kisspeptin 13 (Val59-Ser60-Ala61-Tyr62-Asn63-Trp64-Asn65-Ser66-Phe67-Gly68-Leu69-Arg70-Tyr71NH2) was synthesized through solid phase peptide synthesis using HBTU/HOBt coupling method employing Fmoc chemistry. All solvents were analytical grade. 1-(Bis (dimethylamino) methylene)-1H- benzotriazoliumhexafluorophosphate (1-) 3-oxide (HBTU), 1-hydroxy-benzotriazole (HOBt), Trifluoroacetic Acid (TFA) 1, 3-diisopropylcarbodiimide (DIC), Rink Resin (0.72 mmol equiv g-1), piperidine, N,N-dimethylformamide (DMF), diisopropylethylamine (DIPEA) and all Fmoc-s were purchased from Sigma Aldrich, St Louis, MO, USA.

26. Merriefield RB. Solid Phase Peptide Synthesis. I The Synthesis of a Tetrapeptide.  1963;85:2149-54

MITF Gene - GeneCards | MITF Protein | MITF Antibody

Solid phase peptide synthesis: Kisspeptin-13 was synthesized on the rinkamide resin which is an acid labile resin widely used to prepare amide derivatives of peptides.

A 13 amino acid derivative of kisspeptin was synthesized by solid phase peptide synthesis ..

A range of cleavage reagents for peptides synthesized on 2-chlorotrityl resin has been described. TFE/AcOH/DCM (1:1:3) has been developed by Barbs [62]. Cleavage is also rapidly attained with 0.5% TFA/DCM as well as with HFIP/DCM (1:4 or 3:7) [63].

Does trifluoroacetic acid count when used for cleavage in solid-phase peptide synthesis?


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Bifunctional P-113 peptides were designed as Sortase A substrates and synthesized by solid support peptide synthesis, where the -terminuses were equipped with glycine and its analogues, and C-terminus were extended with LPETGGS, respectively. Cyclized peptides of P-113 analogues were prepared by Sortase A-mediated head to tail ligation in yields from 76% to 93%. The conformation studies by circular dichroism in aqueous buffers and in trifluroethanol (TFE) suggested that a-helix structures were produced progressively in hydrophobic environment independent of the cyclization, which displayed the similar behavior as parent peptide P-113. The detailed conformation information of these peptides in the presence of Zn (Ⅱ), Cu (Ⅱ) ion, and biological activities are undergoing in our lab and will report in full paper in future.