Structure activity studies of PBAN of Helicoverpa zea (Lepidoptera:noctuidae)

Raina, Ashok K.; Kempe, Thomas G.

doi:10.1016/0965-1748(92)90058-m

Cited by 70 publications

(38 citation statements)

References 12 publications

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“…The family, therefore, is grouped together based on a common Cterminal five-amino-acid sequence, with this sequence being the minimal sequence required for activity. The family members are cross-reactive in that each peptide can be active in all physiological functions (Kuniyoshi et al 1992;Nachman et al 1993aNachman et al , 1993bRaina and Kempe 1992). In addition, adult male and female insects contain members of this family of peptides.…”

Section: Introductionmentioning

confidence: 99%

Pyrokinin/PBAN-like peptides in the central nervous system of Drosophila melanogaster

2001

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The pyrokinin/pheromone biosynthesis activating neuropeptide (PBAN) family of peptides found in insects is characterized by a 5-amino-acid C-terminal sequence, FXPRLamide. The pentapeptide is the active core required for diverse physiological functions, including stimulation of pheromone biosynthesis in female moths, stimulation of muscle contraction, induction of embryonic diapause in Bombyx mori, and stimulation of melanization in some larval moths. Recently, this family of peptides has been implicated in accelerating the formation of the puparium in a dipteran. Using bioassay and immunocytochemical techniques, we demonstrate the presence of pyrokinin/PBAN-like peptides in the central nervous system of Drosophila melanogaster. Pheromonotropic activity was shown in the moths Helicoverpa zeaand Helicoverpa armigera by using dissected larval nervous systems and adult heads and bodies of D. melanogaster. Polyclonal antisera against the C-terminal ending of PBAN revealed the location of cell bodies and axons in the central nervous systems of larval and adult flies. Immunoreactive material was detected in at least three groups of neurons in the subesophageal ganglion of 3rd instar larvae, pupae, and adults. The ring gland of both larvae and adults contained immunoreactivity. Adult brain-subesophageal ganglion complex possessed additional neurons. The fused ventral ganglia of both larvae and adults contained three pairs of neurons that sent their axons to a neurohemal organ connected to the abdominal nervous system. These results indicate that the D. melanogasternervous system contains pyrokinin/PBAN-like peptides and that these peptides could be released into the hemolymph.

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Section: Introductionmentioning

confidence: 99%

Pyrokinin/PBAN-like peptides in the central nervous system of Drosophila melanogaster

2001

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“…SAR studies, using synthetic Hez-PBAN and shorter peptides derived from its sequence, revealed that the C-terminal pentapeptide/PBAN that is common to all members of the pyrokinin/PBAN family comprises the active core required for biological activity (22)(23)(24)(25)(26)(27)(28)(29)(30)(31). Furthermore, studies performed in our laboratory indicated that, under certain conditions, the hexapeptide sequence derived from Hez-PBAN (PBAN28 -33NH 2 : Tyr-Phe-Ser-Pro-Arg-Leu-NH 2 , MINI-PBAN) is as active as the full-length PBAN (22) Fig.…”

Section: Design Of Bbc Pban-derived Sub-libraries-detailedmentioning

confidence: 99%

“…Detailed structure-activity relationship studies (SAR), using synthetic PBAN and shorter peptides derived from its sequence, have revealed that the C-terminal pentapeptide, PheXxx-Pro-Arg-Leu-NH 2 (Xxx ϭ Ser), which is identical in all PBAN molecules, is the active core required for biological activity (22)(23)(24)(25)(26)(27)(28)(29)(30)(31). In addition, it has been found that this C-terminal pentapeptide (where Xxx ϭ Ser, Gly, Thr, Val) is homologous with the C-terminal pentapeptide sequence of other families of insect neuropeptides: the pyrokinins (PK) and the myotropins (MT) (myotropic peptides isolated from Leucophaea maderae and Locusta migratoria) (32)(33)(34)(35)(36)(37)(38)(39), and also with the C-terminal region of Pseudaletia separata pheromonotropin (Pss-PT) (40) and Bombyx mori diapause hormone (Bom-DH) (41).…”

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confidence: 99%

Backbone Cyclic Peptide Antagonists, Derived from the Insect Pheromone Biosynthesis Activating Neuropeptide, Inhibit Sex Pheromone Biosynthesis in Moths

Altstein¹,

Ben-Aziz²,

Daniel³

et al. 1999

Journal of Biological Chemistry

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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 ([Arg 27 ]PBAN27-33NH 2 , termed the Ser sub-library) was based on the active C-terminal hexapeptide sequence (Tyr-Phe-Ser-Pro-Arg-Leu-NH 2 ) of PBAN1-33NH 2 , which was found to comprise its active core. It is well established that the activation of multiple receptors by the same peptide arises from the ability of a given peptide to exist in different interchangeable bioactive conformations (1). To attain receptor selectivity it is, therefore, essential to restrict the conformational space of a peptide so it can attain one bioactive conformation.Cyclization is an important and attractive way to restrict the conformational space of peptidic structures (1). Conformationally restricted peptides containing medium and long range cyclizations have been mainly prepared following the same modes of cyclization of naturally occurring peptides. These include end-to-end, side-chain-to-side-chain, and side-chain-toend (2). These modes of cyclization involve modifications of side chains and ends which in many cases are essential for bioactivity, and therefore their modification causes loss of activity. Also, these modes of cyclization are not sufficient to screen effectively the conformational space available for a linear peptide with a given sequence. To overcome these limitations, we have introduced two methods called backbone cyclization (2) and cycloscan (3).Backbone cyclization is a general method by which a conformational constraint is imposed on peptides through the connection of the N ␣ and/or C ␣ atoms in the peptide backbone to each other or to side chains or to the carboxyl and amino ends (2). Thus, the cyclization can be performed while retaining the functionality and the activity of the side chains. Backbone cyclization allows nine new modes of cyclization in addition to the four modes in naturally occurring peptides. Preparation of backbone cyclic (BBC) 1 peptides involves the use of a large variety of orthogonally protected N ␣ and C ␣ (-amino-, -carboxy-, and -thio-alkyl) amino acids building units (4 -6). Synthetic procedures have been developed to incorporate these building units into peptides using the solid phase methodology (7,8).The advantages of backbone cyclization over the naturally occurring modes of cyclization are because of the immense variability of spatial orientation of the constitute residues which result from the multiple anchoring points within a chain or between chains. This allows us to screen the conformational space of a given peptide in an extremely efficient manner. Furthermore, most of the modes of backbone cyclization do not involve chemical modifications of side chains which are essential for biological activity. Ba...

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“…Pyrokinin (PK)/pheromone biosynthesis activating neuropeptides (PBAN) are a large family of insect neuropeptides characterized by a common C-terminal pentapeptide, FXPRLamide (Raina and G. Kempe, 1992). A variety of physiological functions for this family of peptides have been described including stimulation of pheromone biosynthesis in female moths (Raina et al 1989), induction of melanization in moth larvae (Matsumoto et al 1990), induction of embryonic diapause in the silkworm moth (Suwan et al 1994), stimulation of visceral muscle contraction (Predel and Nachman 2001), and termination of pupal diapause development in heliothine moths (Xu and Denlinger 2003), among others.…”

Section: Introductionmentioning

confidence: 99%

Pyrokinin/PBAN-like peptides in the central nervous system of mosquitoes

2014

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The pyrokinin/pheromone biosynthesis activating neuropeptide (PBAN) family of peptides is characterized by a common C-terminal pentapeptide, FXPRLamide, which is required for diverse physiological functions in various insects. Polyclonal antisera against the C-terminus was utilized to determine the location of cell bodies and axons in the central nervous systems of larval and adult mosquitoes. Immunoreactive material was detected in three groups of neurons in the subesophageal ganglion of larvae and adults. The corpora cardiaca of both larvae and adults contained immunoreactivity indicating potential release into circulation. The adult and larval brains had at least one pair of immunoreactive neurons in the protocerebrum with the adult brain having additional immunoreactive neurons in the dorsal medial part of the protocerebrum. The ventral ganglia of both larvae and adults each contained one pair of neurons that sent their axons to a perisympathetic organ associated with each abdominal ganglion. These results indicate that the mosquito nervous system contains pyrokinin/PBAN-like peptides and that these peptides could be released into the hemolymph. The peptides in insects and mosquitoes are produced by two genes, capa and pk/pban. Utilizing PCR protocols, we demonstrate that products of the capa gene could be produced in the abdominal ventral ganglia and the products of the pk/pban gene could be produced in the subesophageal ganglion. Two receptors for pyrokinin peptides were differentially localized to various tissues. Abstract Pyrokinin/pheromone biosynthesis activating neuropeptide (PBAN) family of peptides is characterized by a common C-terminal pentapeptide, FXPRLamide, that is required for diverse physiological functions in various insects. Polyclonal antisera against the C-terminus was utilized to determine the location of cell bodies and axons in the central nervous systems of larval and adult mosquitoes. Immunoreactive material was detected in three groups of neurons in the subesophageal ganglion of larvae and adults. The corpora cardiaca of both larvae and adults contained immunoreactivity indicating potential release into circulation. The adult and larval brains had at least one pair of immunoreactive neurons in the protocerebrum with the adult brain having additional immunoreactive neurons in the dorsal medial part of the protocerebrum. The ventral ganglia of both larvae and adults each contained one pair of neurons that sent their axons to a perisympathetic organ associated with each abdominal ganglion. These results indicate that the mosquito nervous system contains pyrokinin/PBAN-like peptides and that these peptides could be released into the hemolymph. The peptides in insects and mosquitoes are produced by two genes, capa and pk/pban. Utilizing PCR protocols we demonstrate that products of the capa gene could be produced in the abdominal ventral ganglia and the products of the pk/pban gene could be produced in the subesophageal ganglion. Two receptors for pyrokinin peptides were differ...

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Structure activity studies of PBAN of Helicoverpa zea (Lepidoptera:noctuidae)

Cited by 70 publications

References 12 publications

Pyrokinin/PBAN-like peptides in the central nervous system of Drosophila melanogaster

Pyrokinin/PBAN-like peptides in the central nervous system of Drosophila melanogaster

Backbone Cyclic Peptide Antagonists, Derived from the Insect Pheromone Biosynthesis Activating Neuropeptide, Inhibit Sex Pheromone Biosynthesis in Moths

Pyrokinin/PBAN-like peptides in the central nervous system of mosquitoes

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