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פותח על ידי קלירמאש פתרונות בע"מ -
Backbone cyclic peptide antagonists, derived from the insect pheromone biosynthesis activating neuropeptide, inhibit sex pheromone biosynthesis in moths
Year:
1999
Source of publication :
Journal of Biological Chemistry
Authors :
אלטשטיין, מרים
;
.
בן-עזיז, אורנה
;
.
דניאל, שי
;
.
זלצר, אירנה
;
.
שפלר, אירית
;
.
Volume :
274
Co-Authors:
Altstein, M., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Ben-Aziz, O., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Daniel, S., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Schefler, I., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Zeltser, I., Department of Organic Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Gilon, C., Department of Organic Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Facilitators :
From page:
17573
To page:
17579
(
Total pages:
7
)
Abstract:
We describe an application of the backbone cyclization and cycloscan concept for the design and synthesis of pheromone biosynthesis activating neuropeptide (PBAN) antagonists capable of inhibiting sex pheromone biosynthesis in Heliothis peltigera female moths. Two backbone cyclic (BBC) sub-libraries were designed and synthesized. The structure of the first sub- library ([Arg27]PBAN27-33NH2, termed the Ser sub-library) was based on the active C-terminal hexapeptide sequence (Tyr-Phe-Ser-Pro-Arg-Leu-NH2) of PBAN1-33NH2, which was found to comprise its active core. The second sublibrary ([Arg27,D-Phe30]PBAN27-33NH2, termed the D-Phe sub-library) was based on the sequence of the lead antagonist Arg-Tyr-Phe-(D)Phe-Pro-Arg-Leu- NH2. In both sub-libraries the Pro residue was replaced by an Nα(ω-amino- alkyl)Gly building unit having various lengths of the alkyl chain. All the cyclic peptides in each sub-library had the same primary sequence and the same location of the ring. The members of each library differed from each other by the bridge size and bridge chemistry. Screening of the two libraries for pheromonotropic antagonists resulted in the disclosure of four compounds that fully inhibited sex pheromone biosynthesis at 1 nmol and were devoid of agonistic activity. All antagonistic peptides originated from the D-Phe sub- library. Substitution of the D-Phe30 amino acid with a Ser resulted in a loss of antagonistic activity. Agonistic activities were exhibited by peptides from both sub-libraries.
Note:
Related Files :
Animals
animal tissue
biosynthesis
cyclopeptide
Female
Molecular structure
neuropeptide
Peptides, Cyclic
pheromones
עוד תגיות
תוכן קשור
More details
DOI :
10.1074/jbc.274.25.17573
Article number:
0
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
23258
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:58
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Scientific Publication
Backbone cyclic peptide antagonists, derived from the insect pheromone biosynthesis activating neuropeptide, inhibit sex pheromone biosynthesis in moths
274
Altstein, M., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Ben-Aziz, O., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Daniel, S., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Schefler, I., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Zeltser, I., Department of Organic Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Gilon, C., Department of Organic Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Backbone cyclic peptide antagonists, derived from the insect pheromone biosynthesis activating neuropeptide, inhibit sex pheromone biosynthesis in moths
We describe an application of the backbone cyclization and cycloscan concept for the design and synthesis of pheromone biosynthesis activating neuropeptide (PBAN) antagonists capable of inhibiting sex pheromone biosynthesis in Heliothis peltigera female moths. Two backbone cyclic (BBC) sub-libraries were designed and synthesized. The structure of the first sub- library ([Arg27]PBAN27-33NH2, termed the Ser sub-library) was based on the active C-terminal hexapeptide sequence (Tyr-Phe-Ser-Pro-Arg-Leu-NH2) of PBAN1-33NH2, which was found to comprise its active core. The second sublibrary ([Arg27,D-Phe30]PBAN27-33NH2, termed the D-Phe sub-library) was based on the sequence of the lead antagonist Arg-Tyr-Phe-(D)Phe-Pro-Arg-Leu- NH2. In both sub-libraries the Pro residue was replaced by an Nα(ω-amino- alkyl)Gly building unit having various lengths of the alkyl chain. All the cyclic peptides in each sub-library had the same primary sequence and the same location of the ring. The members of each library differed from each other by the bridge size and bridge chemistry. Screening of the two libraries for pheromonotropic antagonists resulted in the disclosure of four compounds that fully inhibited sex pheromone biosynthesis at 1 nmol and were devoid of agonistic activity. All antagonistic peptides originated from the D-Phe sub- library. Substitution of the D-Phe30 amino acid with a Ser resulted in a loss of antagonistic activity. Agonistic activities were exhibited by peptides from both sub-libraries.
Scientific Publication
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