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Altstein, M., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
Dunkelblum, E., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
Gabay, T., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
Aziz, O.B., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
Schafler, I., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
Gazit, Y., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
A structure‐activity relationship study of Hez‐PBAN was performed with respect to its pheromonotropic activity, using Heliothis peltigera as the test animal. The activity of N‐ and C‐terminally derived sequences was examined in a time‐ and dose‐dependent mode. Using a variety of Hez‐PBAN‐derived fragments at two doses (1 and 10 pmol) and at different times post‐injection (5–120 min), we were able to demonstrate that peptides lacking 12 and 16 amino acids from their N‐terminus are as potent as the full length PBAN, and that the C‐terminally derived hexapeptide was capable of stimulating sex pheromone production to a similar extent as PBAN 1–33NH2, when its activity was analyzed at shorter post‐injection times. Within the C‐terminal sequence, the amide was found to play a crucial role. In addition, it was observed that the region between amino acids 9 and 13 is important for the biological activity of the full length PBAN. The fact that the pheromonotropic activity of the hexapeptide was similar to that of the full length PBAN, under specific conditions, suggests that this sequence constitutes the biologically active site of the neuropeptide. The discovery that PBAN‐derived peptides reacted in a time‐ and dose‐dependent mode, strengthens the assumption that proteolytic enzymes interfere with the pheromonotropic activity of the PBAN‐derived fragments. The ability of a variety of peptides to stimulate sex pheromone biosynthesis suggests two possible mechanisms: (1) Existence of multiple pheromonotropic mechanisms which may be mediated by multiple PBAN receptors that are activated at different kinetics; (2) Existence of only one mechanism mediated by short C‐terminally derived peptides. In the first case, the C‐terminally derived sequences fulfill the conformational requirement of only one class of receptors, and other regions in the PBAN molecule (e.g., 9–13) fulfill the conformational requirements of a second (or other) class of receptors. In the second case, the C‐terminally derived sequence is the only conformationally important sequence, and other sequences, which were found to be essential for the biological activity, serve other non‐conformational purposes (e.g., protection against proteolytic degradation). © 1995 Wiley‐Liss, Inc. Copyright © 1995 Wiley‐Liss, Inc.
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PBAN‐induced sex pheromone biosynthesis in Heliothis peltigera: Structure, dose, and time dependent analysis
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Altstein, M., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
Dunkelblum, E., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
Gabay, T., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
Aziz, O.B., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
Schafler, I., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
Gazit, Y., Institute of Plant Protection, ARO, The Volcani Center, Bet Dagan, Israel
PBAN‐induced sex pheromone biosynthesis in Heliothis peltigera: Structure, dose, and time dependent analysis
A structure‐activity relationship study of Hez‐PBAN was performed with respect to its pheromonotropic activity, using Heliothis peltigera as the test animal. The activity of N‐ and C‐terminally derived sequences was examined in a time‐ and dose‐dependent mode. Using a variety of Hez‐PBAN‐derived fragments at two doses (1 and 10 pmol) and at different times post‐injection (5–120 min), we were able to demonstrate that peptides lacking 12 and 16 amino acids from their N‐terminus are as potent as the full length PBAN, and that the C‐terminally derived hexapeptide was capable of stimulating sex pheromone production to a similar extent as PBAN 1–33NH2, when its activity was analyzed at shorter post‐injection times. Within the C‐terminal sequence, the amide was found to play a crucial role. In addition, it was observed that the region between amino acids 9 and 13 is important for the biological activity of the full length PBAN. The fact that the pheromonotropic activity of the hexapeptide was similar to that of the full length PBAN, under specific conditions, suggests that this sequence constitutes the biologically active site of the neuropeptide. The discovery that PBAN‐derived peptides reacted in a time‐ and dose‐dependent mode, strengthens the assumption that proteolytic enzymes interfere with the pheromonotropic activity of the PBAN‐derived fragments. The ability of a variety of peptides to stimulate sex pheromone biosynthesis suggests two possible mechanisms: (1) Existence of multiple pheromonotropic mechanisms which may be mediated by multiple PBAN receptors that are activated at different kinetics; (2) Existence of only one mechanism mediated by short C‐terminally derived peptides. In the first case, the C‐terminally derived sequences fulfill the conformational requirement of only one class of receptors, and other regions in the PBAN molecule (e.g., 9–13) fulfill the conformational requirements of a second (or other) class of receptors. In the second case, the C‐terminally derived sequence is the only conformationally important sequence, and other sequences, which were found to be essential for the biological activity, serve other non‐conformational purposes (e.g., protection against proteolytic degradation). © 1995 Wiley‐Liss, Inc. Copyright © 1995 Wiley‐Liss, Inc.
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