Total Solid Phase Synthesis of the Biologically Active Peptaibol Antibiotic Zervamicin IIB

2000 ◽  
Vol 28 (5) ◽  
pp. A207-A207
Author(s):  
T. V. Ovchinnikova ◽  
M. B. Baru ◽  
E. Yu. Gorbunova ◽  
I. V. Vagenina ◽  
L. G. Mustaeva ◽  
...  
Keyword(s):  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Total Solid ◽  
Biologically Active ◽  
Phase Synthesis

A new strategy for total solid-phase synthesis of polymyxins

2015 ◽  
Vol 56 (33) ◽  
pp. 4796-4799 ◽  
Author(s):  
Wei-Liang Xu ◽  
A-Long Cui ◽  
Xin-Xin Hu ◽  
Xue-Fu You ◽  
Zhuo-Rong Li ◽  
...  
Keyword(s):  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Total Solid ◽  
Phase Synthesis ◽  
New Strategy

Total solid-phase synthesis, purification and characterization of human parathyroid hormone-(1-84)

Biochemistry ◽  
1983 ◽  
Vol 22 (11) ◽  
pp. 2691-2697 ◽  
Author(s):  
T. Fairwell ◽  
A. V. Hospattankar ◽  
R. Ronan ◽  
H. B. Brewer ◽  
J. K. Chang ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Total Solid ◽  
Human Parathyroid Hormone ◽  
Purification And Characterization ◽  
Phase Synthesis

Total solid phase synthesis of ubiquitin. Comparison of different coupling procedures

Peptides 1990 ◽  
1991 ◽  
pp. 80-81 ◽  
Author(s):  
J. P. Briand ◽  
J. Coste ◽  
A. Van Dorsselaer ◽  
B. Raboy ◽  
J. Neimark ◽  
...  
Keyword(s):  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Total Solid ◽  
Phase Synthesis

Total solid-phase synthesis of human cholecystokinin (CCK)-39

2005 ◽  
pp. 295-296
Author(s):  
K. Kitagawa ◽  
C. Aida ◽  
H. Fujiwara ◽  
T. Yagami ◽  
S. Futaki
Keyword(s):  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Total Solid ◽  
Phase Synthesis

Total solid-phase synthesis of porcine gut gastrin releasing peptide (GRP), a mammalian bombesin

1981 ◽  
Vol 103 (11) ◽  
pp. 3178-3185 ◽  
Author(s):  
W. Maerki ◽  
J. Spiess ◽  
Y. Tache ◽  
M. Brown ◽  
J. E. Rivier
Keyword(s):  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Total Solid ◽  
Phase Synthesis ◽  
Gastrin Releasing Peptide

scholarly journals Total Solid-Phase Synthesis of Biologically Active Drosophila Insulin-Like Peptide 2 (DILP2)

2017 ◽  
Vol 70 (2) ◽  
pp. 208 ◽  
Author(s):  
Feng Lin ◽  
Mohammed Akhter Hossain ◽  
Stephanie Post ◽  
Galina Karashchuk ◽  
Marc Tatar ◽  
...  
Keyword(s):  
Solid Phase ◽  
Cell Signalling ◽  
Fruit Fly ◽  
Total Solid ◽  
Biologically Active ◽  
Loss Of Function ◽  
Phase Synthesis ◽  
Function Relationship ◽  
G Protein Coupled ◽  
Synthesis Protocol

In the fruit fly Drosophila melanogaster, there are eight insulin-like peptides (DILPs) with DILPs 1–7 interacting with a sole insulin-like receptor tyrosine kinase (DInR) while DILP8 interacts with a single G protein-coupled receptor (GPCR), Lgr3. Loss-of-function dilp mutation studies show that the neuropeptide DILP2 has a key role in carbohydrate and lipid metabolism as well as longevity and reproduction. A better understanding of the processes whereby DILP2 mediates its specific actions is required. Consequently we undertook to prepare DILP2 as part of a larger, detailed structure–function relationship study. Use of our well established insulin-like peptide synthesis protocol that entails separate solid-phase assembly of each of the A- and B-chains with selective cysteine S-protection followed by sequential S-deprotection and simultaneous disulfide bond formation produced DILP2 in good overall yield and high purity. The synthetic DILP2 was shown to induce significant DInR phosphorylation and downstream signalling, with it being more potent than human insulin. This peptide will be a valuable tool to provide further insights into its binding to the insulin receptor, the subsequent cell signalling, and role in insect metabolism.

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