145313-30-0Relevant articles and documents
Liquid Phase Peptide Synthesis via One-Pot Nanostar Sieving (PEPSTAR)
Yeo, Jet,Peeva, Ludmila,Chung, Seoyeon,Gaffney, Piers,Kim, Daeok,Luciani, Carla,Tsukanov, Sergey,Seibert, Kevin,Kopach, Michael,Albericio, Fernando,Livingston, Andrew
, p. 7786 - 7795 (2021/03/01)
Herein, a one-pot liquid phase peptide synthesis featuring iterative addition of amino acids to a “nanostar” support, with organic solvent nanofiltration (OSN) for isolation of the growing peptide after each synthesis cycle is reported. A cycle consists of coupling, Fmoc removal, then sieving out of the reaction by-products via nanofiltration in a reactor-separator, or synthesizer apparatus where no phase or material transfers are required between cycles. The three-armed and monodisperse nanostar facilitates both efficient nanofiltration and real-time reaction monitoring of each process cycle. This enabled the synthesis of peptides more efficiently while retaining the full benefits of liquid phase synthesis. PEPSTAR was validated initially with the synthesis of enkephalin-like model penta- and decapeptides, then octreotate amide and finally octreotate. The crude purities compared favorably to vendor produced samples from solid phase synthesis.
Bispidine as a helix inducing scaffold: Examples of helically folded linear peptides
Haridas,Sadanandan, Sandhya,Gopalakrishna,Bijesh,Verma, Ram. P.,Chinthalapalli, Srinivas,Shandilya, Ashutosh
, p. 10980 - 10982 (2013/11/19)
We designed and synthesized bispidine-anchored peptides and showed that these peptides as small as B3 (containing four chiral α-amino acid residues) adopt a right handed helical conformation. Bispidine anchored linear peptide B3 adopts a helical conformat
A novel L-amino acid ligase from bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis
Kino, Kuniki,Arai, Toshinobu,Tateiwa, Daisuke
experimental part, p. 129 - 134 (2010/04/24)
L-Amino acid ligase catalyzes dipeptide synthesis from unprotected L-amino acids in an ATP-dependent manner. We have purified a new L-amino acid ligase, RizA, which synthesizes dipeptides whose N-terminus is Arg, from Bacillus subtilis NBRC3134, a microorganism that produces a rhizocticin peptide antibiotic. It was suggested that RizA is probably involved in rhizocticin biosynthesis. In this study, we performed sequence analysis of unknown regions around rizA, and newly identified a gene that encodes a protein that possesses an ATP-grasp motif upstream of rizA. This gene was designated rizB, and its recombinant protein was prepared. Recombinant RizB synthesized homo-oligo-mers of branched-chain L-amino acids and L-methionine consisting of two to five amino acids in an ATP-dependent manner. RizB also synthesized various heteropeptides. Further examination showed that RizB might elongate a peptide chain at the N-terminus. This is the first report on an L-amino acid ligase catalyzing oligopeptide synthesis.
