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פותח על ידי קלירמאש פתרונות בע"מ -
Evaluation of a PK/PBAN analog with an (E)-alkene, trans-Pro isostere identifies the Pro orientation for activity in four diverse PK/PBAN bioassays
Year:
2009
Source of publication :
peptides (מקור פרסום )
Authors :
אלטשטיין, מרים
;
.
בן-עזיז, אורנה
;
.
דוידוביץ', מיכאל
;
.
Volume :
30
Co-Authors:
Nachman, R.J., Areawide Pest Management Research, Southern Plains Agricultural Research Center, USDA, 2881 F/B Road, College Station, TX 77845, United States
Wang, X.J., Department of Chemistry, Virginia Tech, MC 0212, Blacksburg, VA 24061, United States
Etzkorn, F.A., Department of Chemistry, Virginia Tech, MC 0212, Blacksburg, VA 24061, 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
Kaczmarek, K., Areawide Pest Management Research, Southern Plains Agricultural Research Center, USDA, 2881 F/B Road, College Station, TX 77845, United States, Institute of Organic Chemistry, Technical University of Lodz, 90-924 Lodz, Poland
Zabrocki, J., Areawide Pest Management Research, Southern Plains Agricultural Research Center, USDA, 2881 F/B Road, College Station, TX 77845, United States, Institute of Organic Chemistry, Technical University of Lodz, 90-924 Lodz, Poland
Strey, A., Areawide Pest Management Research, Southern Plains Agricultural Research Center, USDA, 2881 F/B Road, College Station, TX 77845, United States
Pryor, N., Areawide Pest Management Research, Southern Plains Agricultural Research Center, USDA, 2881 F/B Road, College Station, TX 77845, United States
Altstein, M., Department of Entomology, The Volcani Center, Bet Dagan, 50250, Israel
Facilitators :
From page:
1254
To page:
1259
(
Total pages:
6
)
Abstract:
The pyrokinin/pheromone biosynthesis activating neuropeptide (PK/PBAN) family plays a multifunctional role in an array of important physiological processes in a variety of insects. An active core analog containing an (E)-alkene, trans-Pro isosteric component was evaluated in four disparate PK/PBAN bioassays in four different insect species. These bioassays include pheromone biosynthesis in the moth Heliothis peltigera, melanization in the larval Spodoptera littoralis, pupariation acceleration in the larval fly Neobellieria bullata, and hindgut contraction in the cockroach Leucophaea maderae. The conformationally constrained analog demonstrated activity equivalent to parent PK/PBAN peptides of equal length in all four PK/PBAN bioassays, and matched and/or approached the activity of peptides of natural length in three of them. In the melanization bioassay, the constrained analog exceeded the efficacy (maximal response) of the natural PBAN1-33 by a factor of 2 (at 1 nmol). The results provide strong evidence for the orientation of Pro and the core conformation adopted by PK/PBAN neuropeptides during interaction with receptors associated with a range of disparate PK/PBAN bioassays. The work further identifies a scaffold with which to design mimetic PK/PBAN analogs as potential leads in the development of environmentally favorable pest management agents capable of disrupting PK/PBAN-regulated systems.
Note:
Related Files :
Animals
Lepidoptera
Molecular structure
Peltigera
peptides
pest management
pheromones
Sarcophaga bullata
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.peptides.2009.04.017
Article number:
0
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
18814
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:24
Scientific Publication
Evaluation of a PK/PBAN analog with an (E)-alkene, trans-Pro isostere identifies the Pro orientation for activity in four diverse PK/PBAN bioassays
30
Nachman, R.J., Areawide Pest Management Research, Southern Plains Agricultural Research Center, USDA, 2881 F/B Road, College Station, TX 77845, United States
Wang, X.J., Department of Chemistry, Virginia Tech, MC 0212, Blacksburg, VA 24061, United States
Etzkorn, F.A., Department of Chemistry, Virginia Tech, MC 0212, Blacksburg, VA 24061, 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
Kaczmarek, K., Areawide Pest Management Research, Southern Plains Agricultural Research Center, USDA, 2881 F/B Road, College Station, TX 77845, United States, Institute of Organic Chemistry, Technical University of Lodz, 90-924 Lodz, Poland
Zabrocki, J., Areawide Pest Management Research, Southern Plains Agricultural Research Center, USDA, 2881 F/B Road, College Station, TX 77845, United States, Institute of Organic Chemistry, Technical University of Lodz, 90-924 Lodz, Poland
Strey, A., Areawide Pest Management Research, Southern Plains Agricultural Research Center, USDA, 2881 F/B Road, College Station, TX 77845, United States
Pryor, N., Areawide Pest Management Research, Southern Plains Agricultural Research Center, USDA, 2881 F/B Road, College Station, TX 77845, United States
Altstein, M., Department of Entomology, The Volcani Center, Bet Dagan, 50250, Israel
Evaluation of a PK/PBAN analog with an (E)-alkene, trans-Pro isostere identifies the Pro orientation for activity in four diverse PK/PBAN bioassays
The pyrokinin/pheromone biosynthesis activating neuropeptide (PK/PBAN) family plays a multifunctional role in an array of important physiological processes in a variety of insects. An active core analog containing an (E)-alkene, trans-Pro isosteric component was evaluated in four disparate PK/PBAN bioassays in four different insect species. These bioassays include pheromone biosynthesis in the moth Heliothis peltigera, melanization in the larval Spodoptera littoralis, pupariation acceleration in the larval fly Neobellieria bullata, and hindgut contraction in the cockroach Leucophaea maderae. The conformationally constrained analog demonstrated activity equivalent to parent PK/PBAN peptides of equal length in all four PK/PBAN bioassays, and matched and/or approached the activity of peptides of natural length in three of them. In the melanization bioassay, the constrained analog exceeded the efficacy (maximal response) of the natural PBAN1-33 by a factor of 2 (at 1 nmol). The results provide strong evidence for the orientation of Pro and the core conformation adopted by PK/PBAN neuropeptides during interaction with receptors associated with a range of disparate PK/PBAN bioassays. The work further identifies a scaffold with which to design mimetic PK/PBAN analogs as potential leads in the development of environmentally favorable pest management agents capable of disrupting PK/PBAN-regulated systems.
Scientific Publication
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