scholarly journals First total synthesis of hoshinoamide A

2021 ◽  
Vol 17 ◽  
pp. 2924-2931
Author(s):  
Haipin Zhou ◽  
Zihan Rui ◽  
Yiming Yang ◽  
Shengtao Xu ◽  
Yutian Shao ◽  
...  
Keyword(s):  
Amino Acids ◽  
Liquid Phase ◽  
Total Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
High Yield ◽  
Marine Cyanobacterium ◽  
Phase Synthesis ◽  
Synthetic Strategy ◽  
Coupling Yield

Hoshinoamides A, B and C, linear lipopeptides, were isolated from the marine cyanobacterium Caldora penicillata, with potent antiplasmodial activity against chloroquine-sensitive Plasmodium falciparum. Herein, we describe the first total synthesis of hoshinoamide A by the combination of liquid-phase and solid-phase peptide synthesis. Liquid-phase synthesis is to improve the coupling yield of ʟ-Val3 and N-Me-ᴅ-Phe2. Connecting other amino acids efficiency and convergence is achieved by solid-state synthesis. Our synthetic strategy could synthesize the target peptide in high yield with good purity

scholarly journals First Total Synthesis of Hoshinoamides A  

2021 ◽  
Author(s):  
Haipin Zhou ◽  
Zihan Rui ◽  
Yiming Yang ◽  
Shengtao Xu ◽  
Yutian Shao ◽  
...  
Keyword(s):  
Amino Acids ◽  
Plasmodium Falciparum ◽  
Total Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
High Yield ◽  
Marine Cyanobacterium ◽  
Phase Synthesis ◽  
Synthetic Strategy ◽  
Coupling Yield

Hoshinoamides A, B and C, linear lipopeptides, were isolated from the marine cyanobacterium Caldora penicillata, with potent antiplasmodial activity against chloroquine-sensitive Plasmodium falciparum. Herein, we describe the first total synthesis of Hoshinoamides A. Our synthetic strategy uses the combined methods of solution and solid phase peptide synthesis. Liquid phase synthesis is to improve the coupling yield of L-Val3 and N-Me-D-Phe2. Connecting other amino acids efficiency and convergence by solid state synthesis. This synthetic strategy has good purity and high yield.

scholarly journals Solution-phase-peptide synthesis via the group-assisted purification (GAP) chemistry without using chromatography and recrystallization

2014 ◽  
Vol 50 (10) ◽  
pp. 1259-1261 ◽  
Author(s):  
Jianbin Wu ◽  
Guanghui An ◽  
Siqi Lin ◽  
Jianbo Xie ◽  
Wei Zhou ◽  
...  
Keyword(s):  
Amino Acids ◽  
Liquid Phase ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Environmentally Friendly ◽  
Solution Phase ◽  
Silica Gels ◽  
Phase Synthesis ◽  
Solution Phase Synthesis

The solution phase synthesis of N-protected amino acids and peptides has been achieved through GAP chemistry by avoiding disadvantages of the solid-phase-peptide synthesis (SPPS) and liquid-phase-peptide synthesis. The environmentally friendly GAP synthesis can substantially reduce the use of solvents, silica gels, energy and manpower.

Solid-Phase Synthesis of Peptides via a,β-Unsaturated Amino Acids. Incorporation of the Amide Gronp in encZo-Positions

1981 ◽  
Vol 36 (10) ◽  
pp. 1345-1348 ◽  
Author(s):  
Kosaku Nöda ◽  
Erhard Gross
Keyword(s):  
Amino Acids ◽  
Peptide Synthesis ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Phase Synthesis ◽  
Unsaturated Amino Acids ◽  
Model Peptides

Abstract Dehydroalanine is introduced as pseudoprotecting group for the to-amide function of Asn and Gin in solid-phase peptide synthesis. Using Boc-X(Dha-NHMe)-OH (X = Asp or Glu), the model peptides, L-Leu-L-Asn-Gly-NH2 and L-Leu-Lr-Gln-Gly-NH2, were synthesized

scholarly journals Macrocylases as synthetic tools for ligand synthesis: enzymatic synthesis of cyclic peptides containing metal-binding amino acids

2021 ◽  
Vol 8 (11) ◽  
Author(s):  
Richard C. Brewster ◽  
Irati Colmenero Labeaga ◽  
Catriona E. Soden ◽  
Amanda G. Jarvis
Keyword(s):  
Amino Acids ◽  
Asymmetric Catalysis ◽  
Metal Binding ◽  
Cyclic Peptides ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Metal Catalysis ◽  
Phase Synthesis ◽  
Metal Ligands ◽  
Secondary Interactions

Improving the sustainability of synthesis is a major goal in green chemistry, which has been greatly aided by the development of asymmetric transition metal catalysis. Recent advances in asymmetric catalysis show that the ability to control the coordination sphere of substrates can lead to improvements in enantioselectivity and activity, in a manner resembling the operation of enzymes. Peptides can be used to mimic enzyme structures and their secondary interactions and they are easily accessible through solid-phase peptide synthesis. Despite this, cyclic peptides remain underexplored as chiral ligands for catalysis due to synthetic complications upon macrocyclization. Here, we show that the solid-phase synthesis of peptides containing metal-binding amino acids, bipyridylalanine ( 1 ), phenyl pyridylalanine ( 2 ) and N,N- dimethylhistidine ( 3 ) can be combined with peptide macrocylization using peptide cyclase 1 (PCY1) to yield cyclic peptides under mild conditions. High conversions of the linear peptides were observed (approx. 90%) and the Cu-bound cyclo(FSAS( 1 )SSKP) was shown to be a competent catalyst in the Friedel-Crafts/conjugate addition of indole. This study shows that PCY1 can tolerate peptides containing amino acids with classic inorganic and organometallic ligands as side chains, opening the door to the streamlined and efficient development of cyclic peptides as metal ligands.

scholarly journals Synthesis of novel conjugates of a saccharide, amino acids, nucleobase and the evaluation of their cell compatibility

2014 ◽  
Vol 10 ◽  
pp. 2406-2413 ◽  
Author(s):  
Dan Yuan ◽  
Xuewen Du ◽  
Junfeng Shi ◽  
Ning Zhou ◽  
Abdulgader Ahmed Baoum ◽  
...  
Keyword(s):  
Amino Acids ◽  
Liquid Phase ◽  
Mammalian Cell ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Facile Synthesis ◽  
Cell Compatibility ◽  
Amidation Reaction ◽  
Multiple Step

This article reports the synthesis of a novel type of conjugate of three fundamental biological build blocks (i.e., saccharide, amino acids, and nucleobase) and their cell compatibility. The facile synthesis starts with the synthesis of nucleobase and saccharide derivatives, then uses solid-phase peptide synthesis (SPPS) to build the peptide segment (Phe-Arg-Gly-Asp or naphthAla-Phe-Arg-Gly-Asp with fully protected groups), and later, an amidation reaction in liquid phase connects these three parts together. The overall yield of these multiple step synthesis is about 34%. Besides exhibiting excellent solubility, these conjugates of saccharide–amino acids–nucleobase (SAN), like the previously reported conjugates of nucleobase–amino acids–saccharide (NAS) and nucleobase–saccharide–amino acids (NSA), are mammalian cell compatible.

scholarly journals Efficient Synthesis of Peptides with 4-Methylpiperidine as Fmoc Removal Reagent by Solid Phase Synthesis

2017 ◽  
Vol 58 (4) ◽  
Author(s):  
Javier Eduardo García Castañeda ◽  
Cristian Francisco Vergel Galeano ◽  
Zuly Jenny Rivera Monroy ◽  
Javier Eduardo Rosas Pérez
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Peptide Synthesis ◽  
Synthetic Peptides ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Amino Group ◽  
Efficient Synthesis ◽  
Phase Synthesis

<p>Solid phase peptide synthesis using the Fmoc/<em>t</em>-Bu strategy (SPPS-Fmoc/tBu) is the most widely used methodology for obtaining synthetic peptides. In this paper, we evaluate the viability of using 4-methylpiperidine as a reagent for deprotection of the amino acid alpha amino group in SPPS-Fmoc/tBu. For this purpose, the peptide (RRWQWRMKKLG) was simultaneously synthesized using 4-methylpiperidine or piperidine for Fmoc removal reagent. The obtained products had similar purities and yields. Finally, 21 peptides were synthesized using 4-methylpiperidine. Our results suggest that is possible to obtain synthetic peptides efficiently by the strategy SPPS-Fmoc/tBu when 4-methylpiperidine was used as reagent to remove Fmoc groups N-alpha protected amino acids.</p>

The Boc/Solid Phase Synthesis of Glu-Abu(P)-Leu

1992 ◽  
Vol 45 (10) ◽  
pp. 1765 ◽  
Author(s):  
JW Perich ◽  
EC Reynolds
Keyword(s):  
Amino Acids ◽  
Peptide Synthesis ◽  
Trifluoroacetic Acid ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Hydrogen Bromide ◽  
Solid Phase Peptide Synthesis ◽  
Polymer Support ◽  
Methyl Groups ◽  
Phase Synthesis

The synthesis of the 4-phosphono-2-aminobutanoyl-containing tripeptide , H- Glu -Abu(P)- Leu-OH.CF3C02H was accomplished by the use of Boc-Abu(PO3Me2)-OH in Boc /solid phase peptide synthesis. Peptide synthesis was performed by using Boc-Leu-polystyrene as the polymer support with the peptide assembled by the use of 1H-benzotriazol-1-yloxytris(pyrro1idin-1-yl) phosphonium hexafluorophosphate ( PyBOPR ) for the coupling of Boc amino acids and 50% CF3C02H/CH2C12 for cleavage of the Boc group from the Boc -peptide after each coupling cycle. The protected peptide was cleaved from the polymer support by hydrogen bromide in trifluoroacetic acid and final cleavage of the methyl groups from Glu-Abu(PO2Me2)-Leu was effected by silylitic treatment with 30% bromotrimethylsilane in acetonitrile.

Vasopressin and oxytocin analogs with interchanged sequence of amino acids in positions 7 and 8. synthesis and biological effects

1981 ◽  
Vol 46 (9) ◽  
pp. 2136-2139 ◽  
Author(s):  
Ivo Bláha ◽  
Viktor Krchňák ◽  
Milan Zaoral
Keyword(s):  
Amino Acids ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Biological Effects ◽  
Free Flow ◽  
Protecting Groups ◽  
Pressor Effect ◽  
Phase Synthesis ◽  
Antidiuretic Effect

p-Toluenesulfonyl-S-benzylcysteinyl-tyrosyl-phenylalanyl-glutaminyl-asparaginyl-S-benzylcysteinyl-NG-p-toluenesulfanylarginyl-prolyl-glycineamide (I) and S-benzylcysteinyl-tyrosyl-isoleucyl-glutaminyl-asparaginyl-S-benzylcysteinyl-leucyl-prolyl-glycine amide (III) were prepared by solid phase synthesis. After removal of the protecting groups, closure of the disulfide ring, and purification by continuous free-flow electrophoresis [arginine7, proline8]vasopressin (II) and [leucine7, proline8]oxytocin (IV) were obtained. The antidiuretic effect of II is markedly higher than its pressor effect; IV possesses c. 6% of the uterotonic and c. 10% of the galactogogous effect of oxytocin.

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