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פותח על ידי קלירמאש פתרונות בע"מ -
An amphiphilic, PK/PBAN analog is a selective pheromonotropic antagonist that penetrates the cuticle of a heliothine insect
Year:
2009
Source of publication :
peptides (מקור פרסום )
Authors :
אלטשטיין, מרים
;
.
דוידוביץ', מיכאל
;
.
Volume :
30
Co-Authors:
Nachman, R.J., Areawide Pest Management Research, Southern Plains Agricultural Research Center, U.S. Department of Agriculture, College Station, TX 77845, United States
Teal, P.E.A., Center for Medical, Agricultural and Veterinary Entomology, U.S. Department of Agriculture, Gainesville, FL 32604, United States
Aziz, O.B., Department of Entomology, The Volcani Center, Bet Dagan, 50250, Israel
Davidovitch, M., Department of Entomology, The Volcani Center, Bet Dagan, 50250, Israel
Zubrzak, P., Areawide Pest Management Research, Southern Plains Agricultural Research Center, U.S. Department of Agriculture, College Station, TX 77845, United States
Altstein, M., Department of Entomology, The Volcani Center, Bet Dagan, 50250, Israel
Facilitators :
From page:
616
To page:
621
(
Total pages:
6
)
Abstract:
A linear pyrokinin (PK)/pheromone biosynthesis activating neuropeptide (PBAN) antagonist lead (RYF[dF]PRLa) was structurally modified to impart amphiphilic properties to enhance its ability to transmigrate the hydrophobic cuticle of noctuid moth species and yet retain aqueous solubility in the hemolymph to reach target PK/PBAN receptors within the internal insect environment. The resulting novel PK/PBAN analog, Hex-Suc-A[dF]PRLa (PPK-AA), was synthesized and evaluated as an antagonist in a pheromonotropic assay in Heliothis peltigera against 4 natural PK/PBAN peptide elicitors (PBAN; pheromonotropin, PT; myotropin, MT; leucopyrokinin, LPK) and in a melanotropic assay in Spodoptera littoralis against 3 natural PK/PBAN peptide elicitors (PBAN, PT, LPK). The analog proved to be a potent and efficacious inhibitor of sex pheromone biosynthesis elicited by PBAN (84% at 100 pmol) and PT (54% at 100 pmol), but not by MT and LPK. PPK-AA is a selective pure antagonist (i.e., does not exhibit any agonistic activity) as it failed to inhibit melanization elicited by any of the natural PK/PBAN peptides. The analog was shown to transmigrate isolated cuticle dissected from adult female Heliothis virescens moths to a high extent of 25-30% (130-150 pmol), representing physiologically significant quantities. PPK-AA represents a significant addition to the arsenal of tools available to arthropod endocrinologists studying the endogenous mechanisms of PK/PBAN regulated processes, and a prototype for the development of environmentally friendly pest management agents capable of disrupting the critical process of reproduction. © 2008 Elsevier Inc.
Note:
Related Files :
animal experiment
Animals
Female
Lepidoptera
Peltigera
pest management
Reproduction
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.peptides.2008.09.024
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
28809
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:42
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Scientific Publication
An amphiphilic, PK/PBAN analog is a selective pheromonotropic antagonist that penetrates the cuticle of a heliothine insect
30
Nachman, R.J., Areawide Pest Management Research, Southern Plains Agricultural Research Center, U.S. Department of Agriculture, College Station, TX 77845, United States
Teal, P.E.A., Center for Medical, Agricultural and Veterinary Entomology, U.S. Department of Agriculture, Gainesville, FL 32604, United States
Aziz, O.B., Department of Entomology, The Volcani Center, Bet Dagan, 50250, Israel
Davidovitch, M., Department of Entomology, The Volcani Center, Bet Dagan, 50250, Israel
Zubrzak, P., Areawide Pest Management Research, Southern Plains Agricultural Research Center, U.S. Department of Agriculture, College Station, TX 77845, United States
Altstein, M., Department of Entomology, The Volcani Center, Bet Dagan, 50250, Israel
An amphiphilic, PK/PBAN analog is a selective pheromonotropic antagonist that penetrates the cuticle of a heliothine insect
A linear pyrokinin (PK)/pheromone biosynthesis activating neuropeptide (PBAN) antagonist lead (RYF[dF]PRLa) was structurally modified to impart amphiphilic properties to enhance its ability to transmigrate the hydrophobic cuticle of noctuid moth species and yet retain aqueous solubility in the hemolymph to reach target PK/PBAN receptors within the internal insect environment. The resulting novel PK/PBAN analog, Hex-Suc-A[dF]PRLa (PPK-AA), was synthesized and evaluated as an antagonist in a pheromonotropic assay in Heliothis peltigera against 4 natural PK/PBAN peptide elicitors (PBAN; pheromonotropin, PT; myotropin, MT; leucopyrokinin, LPK) and in a melanotropic assay in Spodoptera littoralis against 3 natural PK/PBAN peptide elicitors (PBAN, PT, LPK). The analog proved to be a potent and efficacious inhibitor of sex pheromone biosynthesis elicited by PBAN (84% at 100 pmol) and PT (54% at 100 pmol), but not by MT and LPK. PPK-AA is a selective pure antagonist (i.e., does not exhibit any agonistic activity) as it failed to inhibit melanization elicited by any of the natural PK/PBAN peptides. The analog was shown to transmigrate isolated cuticle dissected from adult female Heliothis virescens moths to a high extent of 25-30% (130-150 pmol), representing physiologically significant quantities. PPK-AA represents a significant addition to the arsenal of tools available to arthropod endocrinologists studying the endogenous mechanisms of PK/PBAN regulated processes, and a prototype for the development of environmentally friendly pest management agents capable of disrupting the critical process of reproduction. © 2008 Elsevier Inc.
Scientific Publication
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