Bioavailability of β-amino acid and C-terminally derived PK/PBAN analogs

Hariton, Aliza; Ben-Aziz, Orna; Davidovitch, Michael; Zubrzak, Paweł; Nachman, Ronald J.; Altstein, Miriam

doi:10.1016/j.peptides.2009.05.011

Cited by 8 publications

(7 citation statements)

References 40 publications

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“…The structure and pheromone activity of PBAN of Helicoverpa zea was identified by Rain et al (1989) and subsequently the PBAN sequence of H. zea (34 amino acids), particularly the terminal sequence (24 -33) was synthesized to identify the pyrokinin/PBAN bioactivity of other insects. The neuropeptide activity was studied by injecting the synthetic peptide into the brain of insects or used as an antibody in ELISA (Jurenka et al, 1995;Altstein et al, 1999;Rain et al, 2003, Hariton et al, 2009. In the present study, we could not find the immunoreactivity of PBAN-like peptide in the head of another psocid L. bostrychophia female.…”

Section: Discussioncontrasting

confidence: 62%

Identification and sequence analysis of pyrokinin/PBAN peptide of psocids, Liposcelis entomophila

Lu¹,

Guo²,

Li³

et al. 2011

Afr. J. Biotechnol.

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Using an antiserum against Helicoverpa zea pheromone biosynthesis activating neuropeptide (PBAN), pyrokinin/PBAN-like immunoreactivity in the head and body of female of Liposcelis entomophila was detected by competitive ELISA. Pyrokinin/PBAN peptides were extracted and purified by reverse-phase HPLC, and the sequence were elucidated by a matrix-assisted laser desorption ionization time of flight mass spectrometer (MALDI-MS-TOF). The results showed that pyrokinin/PBAN neuropeptide was expressed in the heads of L. entomophila females. Meanwhile, it was not found in the abdomen of L. entomophila females and the head of Liposcelis bostrychophila. These results indicated that the peptide perhaps had the functions to regulate sex pheromone releasing. The sequence pyrokinin/PBAN family peptide in L. entomophila was SAGMFTPRL-NH 2. The result of BLASTp in NCBI web showed that its sequence had largely homologous sequences with other PBAN/pyrokinin peptides sequence in other insects that were published and share a highly conserved sequence FXPRLamide in the C terminal. This result indicated that the identified peptide in L. entomophila belong to the pyrokinin/PBAN family. The purification and identification of this peptide have an important instructional meaning for cloning the gene of pyrokinin/PBAN and elucidating the release mechanism of the sex pheromone of L. entomophila.

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Section: Discussioncontrasting

confidence: 62%

Identification and sequence analysis of pyrokinin/PBAN peptide of psocids, Liposcelis entomophila

Lu¹,

Guo²,

Li³

et al. 2011

Afr. J. Biotechnol.

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“…Increased knowledge on neuropeptide actions, and their associated regulatory roles, may reveal suitable targets for design of environmentally benign control compounds to eradicate and/or control these medically relevant pest species (Scherkenbeck and Zdobinsky, 2009). Development of peptidomimetics, which are synthetic analogs that can match or exceed activity of the native peptides and can have increased biostability (Hariton et al, 2009;Zubrzak et al, 2007), is increasingly needed as the protozoan parasites develop resistance to the front line drugs used to treat Chagas' disease (Wilkinson et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Identification, spatial expression analysis and functional characterization of a pyrokinin-1 receptor in the Chagas’ disease vector, Rhodnius prolixus

Paluzzi

O’Donnell

2012

Molecular and Cellular Endocrinology

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“…Recently, we demonstrated, for the first time, that native, unmodified linear peptides of various lengths belonging to the PK/PBAN family (PBAN, leucopyrokinin, pheromonotropin and myotropin), as well as small, linear synthetic β‐substituted peptides (Ac‐YFT[β 3 P]RLa, Ac‐Y[β 2 homoF]TPRLa, Ac‐Y[β 3 F]TPRLa and Ac‐[β 3 F]FT[β 3 P]RLa) and two analogs (YFTPRLa and the acylated peptide Ac‐YFTPRLa) were highly bioavailable, i.e. they could penetrate the cuticle very efficiently and reach and activate their target organ following topical application to the female moth abdomen, at a dose of 1 nmol in either double‐distilled water (DDW) or dimethylsulfoxide [19,20].…”

Section: Introductionmentioning

confidence: 99%

“…and two analogs (YFTPRLa and the acylated peptide Ac-YFTPRLa) were highly bioavailable, i.e. they could penetrate the cuticle very efficiently and reach and activate their target organ following topical application to the female moth abdomen, at a dose of 1 nmol in either double-distilled water (DDW) or dimethylsulfoxide [19,20].…”

Section: Introductionmentioning

confidence: 99%

Bioavailability of backbone cyclic PK/PBAN neuropeptide antagonists – inhibition of sex pheromone biosynthesis elicited by the natural mechanism in Heliothis peltigera females

et al. 2010

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The bioavailability (i.e. ability to penetrate the insect cuticle, to reach the target organ and to exert bioactivity) of two backbone cyclic (BBC) pyrokinin/pheromone biosynthesis‐activating neuropeptide (PK/PBAN) antagonistic peptides was tested by applying them topically to Heliothis peltigera females and monitoring the resulting inhibition of sex pheromone production elicited by the natural (endogenous) mechanism during scotophase. Peptides were applied at various time points before the onset of scotophase, in aqueous or organic solvents, and pheromone content was examined at the 5th or 6th hour of scotophase. Both peptides penetrated the cuticle very efficiently and inhibited sex pheromone biosynthesis elicited by the natural mechanism for up to 8 or 9 h after application. The degree of inhibition differed between solvents: those applied in double‐distilled water (DDW) were more active than those applied in dimethylsulfoxide (inhibition by 53–73% and 15–38%, respectively, for BBC‐25, and 46–67% and 36–40%, respectively for BBC‐28). Peptides applied in dimethylsulfoxide and hexane exhibited slightly more persistent inhibitory activity than those applied in DDW. The solvents themselves did not affect sex pheromone production. Multiple applications (at −2, 0, +2 and +4 h) resulted in almost complete (87%) inhibition of sex pheromone biosynthesis, compared with 52% inhibition following a single application. The present study is the first demonstration of the ability of topically applied PK/PBAN antagonists to inhibit sex pheromone biosynthesis elicited by the natural mechanism in female moths, and provides important information on the bioavailability of BBC peptides and the mechanism responsible for sex pheromone production in these insects.

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Bioavailability of β-amino acid and C-terminally derived PK/PBAN analogs

Cited by 8 publications

References 40 publications

Identification and sequence analysis of pyrokinin/PBAN peptide of psocids, Liposcelis entomophila

Identification and sequence analysis of pyrokinin/PBAN peptide of psocids, Liposcelis entomophila

Identification, spatial expression analysis and functional characterization of a pyrokinin-1 receptor in the Chagas’ disease vector, Rhodnius prolixus

Bioavailability of backbone cyclic PK/PBAN neuropeptide antagonists – inhibition of sex pheromone biosynthesis elicited by the natural mechanism in Heliothis peltigera females

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