One-pot hydrazide-based native chemical ligation for efficient chemical synthesis and structure determination of toxin Mambalgin-1

2014 ◽  
Vol 50 (44) ◽  
pp. 5837-5839 ◽  
Author(s):  
Man Pan ◽  
Yao He ◽  
Ming Wen ◽  
Fangming Wu ◽  
Demeng Sun ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Snake Venom ◽  
Structure Determination ◽  
Native Chemical Ligation ◽  
One Pot ◽  
Chemical Ligation ◽  
Venom Toxin ◽  
Snake Venom Toxin ◽  
Switch Strategy

An efficient one-pot chemical synthesis of snake venom toxin Mambalgin-1 was achieved using an azide-switch strategy combined with hydrazide-based native chemical ligation.

One-pot native chemical ligation of peptide hydrazides enables total synthesis of modified histones

2014 ◽  
Vol 12 (29) ◽  
pp. 5435-5441 ◽  
Author(s):  
Jiabin Li ◽  
Yuanyuan Li ◽  
Qiaoqiao He ◽  
Yiming Li ◽  
Haitao Li ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Total Synthesis ◽  
Native Chemical Ligation ◽  
One Pot ◽  
Chemical Ligation

One of the rising demands in the field of protein chemical synthesis is the development of facile strategies that yield the protein in workable quantities and homogeneity, with fewer handling steps.

scholarly journals A Straightforward Methodology to Overcome Solubility Challenges for N-Terminal Cysteinyl Peptide Segments Used in Native Chemical Ligation

2020 ◽  
Author(s):  
Skander Abboud ◽  
El hadji Cisse ◽  
Michel Doudeau ◽  
Hélène Bénédetti ◽  
Vincent AUCAGNE
Keyword(s):  
Amino Acids ◽  
Chemical Synthesis ◽  
Building Blocks ◽  
Native Chemical Ligation ◽  
Synthetic Approach ◽  
Chemical Ligation ◽  
Limited Solubility ◽  
Peptide Segments

One of the main limitations encountered during the chemical synthesis of proteins through native chemical ligation (NCL) is the limited solubility of some of the peptide segments. The most commonly used solution to overcome this problem is to derivatize the segment with a temporary solubilizing tag. Conveniently, the tag can be introduced on the thioester segment in such a way that it is removed concomitantly with the NCL reaction. We herein describe a generalization of this approach to N-terminal cysteinyl segment counterparts, using a straightforward synthetic approach that can be easily automated from commercially available building blocks, and applied it to a well-known problematic target, SUMO-2 (93 amino acids).

Facile and efficient chemical synthesis of APET×2, an ASIC-targeting toxin, via hydrazide-based native chemical ligation

Tetrahedron ◽  
2015 ◽  
Vol 71 (21) ◽  
pp. 3363-3366
Author(s):  
Si-Jian Li ◽  
Da-Liang Qu ◽  
Ye-Hai Wang ◽  
Yao He ◽  
Min Wen ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Native Chemical Ligation ◽  
Chemical Ligation

scholarly journals A synthetic approach to ‘click’ neoglycoprotein analogues of EPO employing one-pot native chemical ligation and CuAAC chemistry

2019 ◽  
Vol 10 (3) ◽  
pp. 815-828 ◽  
Author(s):  
D. J. Lee ◽  
A. J. Cameron ◽  
T. H. Wright ◽  
P. W. R. Harris ◽  
M. A. Brimble
Keyword(s):  
Native Chemical Ligation ◽  
Synthetic Approach ◽  
One Pot ◽  
Chemical Ligation ◽  
Synthetic Methodologies

The batch-wise variability of commercial erythropoietin (EPO) preparations warrants development of more advanced synthetic methodologies. We have developed a diverse chemical toolkit to prepare ‘click’ neoglycoprotein variants of EPO.

scholarly journals The mechanism of Ca2+ releasing action of a snake venom toxin in sarcoplasmic reticulum

1992 ◽  
Vol 58 ◽  
pp. 208
Author(s):  
Kaori Funayama ◽  
Ken-Ichi Furukawa ◽  
Yoshiteru Ohshima ◽  
Anthony T. Tu ◽  
Yasushi Ohizumi
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Snake Venom ◽  
Venom Toxin ◽  
Snake Venom Toxin

P-788 The snake venom toxin taipoxin confers specific toxicity to smallcell lung cancer cell lines

Lung Cancer ◽  
2005 ◽  
Vol 49 ◽  
pp. S326-S327
Author(s):  
T. Poulsen ◽  
N. Pedersen ◽  
M. Pedersen ◽  
H. Poulsen
Keyword(s):  
Lung Cancer ◽  
Cell Lines ◽  
Cancer Cell ◽  
Snake Venom ◽  
Cancer Cell Lines ◽  
Lung Cancer Cell ◽  
Venom Toxin ◽  
Snake Venom Toxin

Amino acid sequence of a snake venom toxin that binds to the muscarinic acetylcholine receptor

Toxicon ◽  
1991 ◽  
Vol 29 (4-5) ◽  
pp. 521-526 ◽  
Author(s):  
Evert Karlsson ◽  
Carl Risinger ◽  
Mikael Jolkkonen ◽  
Christer Wernstedt ◽  
Abdu Adem
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acetylcholine Receptor ◽  
Snake Venom ◽  
Muscarinic Acetylcholine Receptor ◽  
Muscarinic Acetylcholine ◽  
Venom Toxin ◽  
Snake Venom Toxin

Characterization of inflamin, the first member of a new family of snake venom proteins that induces inflammation

2013 ◽  
Vol 455 (2) ◽  
pp. 239-250 ◽  
Author(s):  
Bhaskar Barnwal ◽  
R. Manjunatha Kini
Keyword(s):  
Phospholipase A2 ◽  
Snake Venom ◽  
Calcium Dependent ◽  
Venom Toxin ◽  
New Family ◽  
Snake Venom Toxin ◽  
Venom Proteins

Inflamin, a novel snake venom toxin from Aipysurus eydouxii, leads to the activation of calcium-dependent phospholipase A2 by phosphorylation at Ser505, resulting in inflammation and pain.

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