ChemInform Abstract: A Novel Double Deprotection-Peptide Cyclization Procedure and Its Application to the Synthesis of Analogues of the Cyclic Tetrapeptide HC- Toxin.

ChemInform ◽  
1987 ◽  
Vol 18 (52) ◽  
Author(s):  
R. E. SHUTE ◽  
D. H. RICH
Keyword(s):  
Peptide Cyclization ◽  
Hc Toxin ◽  
Cyclic Tetrapeptide

ChemInform Abstract: JM47, a Cyclic Tetrapeptide HC-Toxin Analogue from a Marine Fusarium Species

ChemInform ◽  
2010 ◽  
Vol 33 (38) ◽  
pp. no-no
Author(s):  
Zhong Jiang ◽  
Marc-Olivier Barret ◽  
Kenneth G. Boyd ◽  
David R. Adams ◽  
Alan S. F. Boyd ◽  
...  
Keyword(s):  
Fusarium Species ◽  
Hc Toxin ◽  
Cyclic Tetrapeptide

Total Synthesis of the Cyclic Tetrapeptide, HC-Toxin

1983 ◽  
Vol 24 (48) ◽  
pp. 5309-5312 ◽  
Author(s):  
Megumi Kawai ◽  
Daniel H. Rich
Keyword(s):  
Total Synthesis ◽  
Hc Toxin ◽  
Cyclic Tetrapeptide

scholarly journals Histone Deacetylase Activity and Phytotoxic Effects Following Exposure of Duckweed (Lemna pausicostata L.) to Apicidin and HC-Toxin

2001 ◽  
Vol 91 (12) ◽  
pp. 1141-1148 ◽  
Author(s):  
Hamed K. Abbas ◽  
John W. Gronwald ◽  
Kathryn L. Plaisance ◽  
Rex N. Paul ◽  
Yin W. Lee
Keyword(s):  
Cell Division ◽  
Histone Deacetylase ◽  
Chlorophyll Synthesis ◽  
Effective Concentration ◽  
Starch Accumulation ◽  
Fusarium Spp ◽  
Cochliobolus Carbonum ◽  
Hc Toxin ◽  
Cyclic Tetrapeptide

The effects of two cyclic tetrapeptide fungal toxins, apicidin (from Fusarium spp.) and HC-toxin (from Cochliobolus carbonum), on duckweed (Lemna pausicostata L.) were examined. Both toxins inhibited histone deacetylase (HD) activity from duckweed plantlets; the effective concentration (EC50) for inhibition of HD was 5.6 and 1.1 μM for apicidin and HC-toxin, respectively. Approximately 65 and 85% of in vitro HD activity was inhibited by 50 μM apicidin or HC-toxin, respectively. Exposing duckweed for 72 h to apicidin or HC-toxin (25 or 50 μM) enhanced cellular leakage, impaired chlorophyll synthesis, and inhibited growth (cell division). At equivalent concentrations, the effects of HC-toxin were more pronounced than those of apicidin. In fronds, 72 h of exposure to 50 μM apicidin resulted in chloroplast deterioration indicated by loss of orientation and excess starch accumulation. In roots, a 72-h treatment with 50 μM apicidin resulted in the loss of the root cap and increased vacuolization and starch accumulation in plastids.

JM47, a cyclic tetrapeptide HC-toxin analogue from a marine Fusarium species

2002 ◽  
Vol 60 (1) ◽  
pp. 33-38 ◽  
Author(s):  
Zhong Jiang ◽  
Marc-Olivier Barret ◽  
Kenneth G Boyd ◽  
David R Adams ◽  
Alan S.F Boyd ◽  
...  
Keyword(s):  
Fusarium Species ◽  
Hc Toxin ◽  
Cyclic Tetrapeptide

Structure of HC-toxin, a cyclic tetrapeptide from helminthosporium carbonum

Tetrahedron ◽  
1982 ◽  
Vol 38 (1) ◽  
pp. 45-48 ◽  
Author(s):  
Jerrold M. Liesch ◽  
Charles C. Sweeley ◽  
Glenn D. Staffeld ◽  
Matt S. Anderson ◽  
Darrell J. Weber ◽  
...  
Keyword(s):  
Toxin A ◽  
Hc Toxin ◽  
Cyclic Tetrapeptide

The backbone and side chain conformations of the cyclic tetrapeptide HC-toxin

1983 ◽  
Vol 113 (1) ◽  
pp. 10-17 ◽  
Author(s):  
Paolo Mascagni ◽  
Mark Pope ◽  
William A. Gibbons ◽  
Lynda M. Ciuffetti ◽  
Herman W. Knoche
Keyword(s):  
Side Chain ◽  
Hc Toxin ◽  
Chain Conformations ◽  
Cyclic Tetrapeptide

scholarly journals Massiliamide, a cyclic tetrapeptide with potent tyrosinase inhibitory properties from the Gram-negative bacterium Massilia albidiflava DSM 17472T

2020 ◽  
Author(s):  
Andri Frediansyah ◽  
Jan Straetener ◽  
Heike Brötz-Oesterhelt ◽  
Harald Gross
Keyword(s):  
Absolute Configuration ◽  
Inhibitory Activity ◽  
Liquid Culture ◽  
Spectroscopic Analysis ◽  
2D Nmr ◽  
Negative Bacterium ◽  
Gram Negative ◽  
The Absolute ◽  
Potent Inhibitory Activity ◽  
Cyclic Tetrapeptide

AbstractA cyclic tetrapeptide, designated massiliamide, was isolated from the liquid culture of the Gram-negative bacterium Massilia albidiflava DSM 17472T. The structure was elucidated through extensive spectroscopic analysis, including HR-MS and 1D and 2D NMR experiments. The absolute configuration was determined using the Marfey´s method. Massiliamide showed potent inhibitory activity towards tyrosinase with an IC50 value of 1.15 µM and no cytotoxicity.

scholarly journals PenA, a penicillin-binding protein-type thioesterase specialized for small peptide cyclization

2021 ◽  
Author(s):  
Kenichi Matsuda ◽  
Kei Fujita ◽  
Toshiyuki Wakimoto
Keyword(s):  
Enzymatic Activity ◽  
Computational Model ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Small Peptide ◽  
Peptide Cyclization ◽  
Chain Lengths ◽  
Non Ribosomal Peptides

Abstract Penicillin binding protein-type thioesterases (PBP-type TEs) are a recently identified group of peptide cyclases that catalyze head-to-tail macrolactamization of non-ribosomal peptides. PenA, a new member of this group, is involved in the biosyntheses of cyclic pentapeptides. In this study, we demonstrated the enzymatic activity of PenA in vitro, and analyzed its substrate scope with a series of synthetic substrates. A comparison of the reaction profiles between PenA and SurE, a representative PBP-type TE, showed that PenA is more specialized for small peptide cyclization. A computational model provided a possible structural rationale for the altered specificity for substrate chain lengths.

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