Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys18]-substituted analogue

@inproceedings{AbdelWahab2008InsulinreleasingPO,
  title={Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys18]-substituted analogue},
  author={Yasser H A Abdel-Wahab and Gavin J. Power and Ming T. Ng and Peter R. Flatt and J. Michael Conlon},
  booktitle={Biological chemistry},
  year={2008}
}
Abstract Pseudin-2 is a cationic α-helical peptide that was first isolated from the skin of the paradoxical frog Pseudis paradoxa on the basis of its antimicrobial activity. We have investigated the insulin-releasing properties and cytotoxicity of the peptide, together with selected analogues with increased cationicity and hydrophobicity. At concentrations in the range 10-9–10-6 m, pseudin-2, and its [Lys18], [Phe8], and [d-Lys3,d-Lys10,d-Lys14] derivatives, stimulated insulin release from the… Expand
Insulin-releasing and cytotoxic properties of the frog skin peptide, tigerinin-1R: a structure–activity study
TLDR
The claim that tigerinin-1R shows potential for development into novel therapeutic agents for treatment of type 2 diabetes mellitus is supported. Expand
Esculentin-2CHa(1-30) and its analogues: stability and mechanisms of insulinotropic action.
TLDR
The insulin-releasing effects, cellular mechanisms of action and anti-hyperglycaemic activity of 10 analogues of esculentin-2CHa lacking the cyclic C-terminal domain (CKISKQC) were evaluated, suggesting that multi-acting analoguesof esculentin-1-30 may prove useful for glycaemic control in obesity-diabetes. Expand
Brevinin-2-related peptide and its [D4K] analogue stimulate insulin release in vitro and improve glucose tolerance in mice fed a high fat diet.
TLDR
Administration of [D4K]B2RP to mice fed a high fat diet to induce obesity and insulin-resistance significantly enhanced insulin release and improved glucose tolerance during the 60-minute period following an intraperitoneal glucose load, and shows potential for development into an agent for the treatment of type 2 diabetes. Expand
In vitro and in vivo insulinotropic properties of the multifunctional frog skin peptide hymenochirin-1B: a structure–activity study
TLDR
Intraperitoneal administration of the [P5K] and [D9k] analogues to high-fat-fed mice with insulin resistance significantly enhanced glucose tolerance with a concomitant increase in insulin secretion and it is concluded that Hym-1B and D9k show potential for development into anti-diabetic agents. Expand
Investigation of cationicity and structure of pseudin-2 analogues for enhanced bacterial selectivity and anti-inflammatory activity
TLDR
It is found that Ps analogues produced much higher membrane depolarization than Ps-P analogues, whereas Ps-F analogues may penetrate bacterial cell membranes, and the bent structure provided by Pro substitution plays an important role in enhancing bacterial cell selectivity and cell penetration. Expand
Insulinotropic activity of the host-defense peptide frenatin 2D: Conformational, structure-function and mechanistic studies.
TLDR
It is concluded that the insulinotropic activity of frenatin 2D is mediated predominantly, if not exclusively, by the KATP channel-independent pathway. Expand
Insulinotropic Actions of the Frog Skin Host‐Defense Peptide Alyteserin‐2a: A Structure–Activity Study
TLDR
Administration of [G11k]alyteserin‐2a (75 nmol/kg body weight) to high‐fat‐fed mice with obesity and insulin resistance significantly enhanced insulin release and improved glucose tolerance during the 60‐min period following an intraperitoneal glucose load. Expand
Activity optimization of an undecapeptide analogue derived from a frog-skin antimicrobial peptide
TLDR
Given its relatively shorter length and simpler amino acid composition, the sequence-optimized GA-K4AL peptide may be a potentially useful antimicrobial peptide agent. Expand
Caerulein precursor fragment (CPF) peptides from the skin secretions of Xenopus laevis and Silurana epitropicalis are potent insulin-releasing agents.
TLDR
Ten peptides with the ability to stimulate the release of insulin from the rat BRIN-BD11 clonal β cell line are identified and show potential for development into agents for the treatment of Type 2 diabetes. Expand
Research progress of insulin-releasing function of antimicrobial peptides from frog skin
TLDR
The sequence features of antibacterial peptides which have insulin-releasing activities and the advance in insulinotropic secretion mechanism are summarized to provide the reference for further research about insulinotropic peptide from the skin secretions of frog. Expand
...
1
2
3
4
...

References

SHOWING 1-10 OF 27 REFERENCES
Design of potent, non-toxic antimicrobial agents based upon the structure of the frog skin peptide, pseudin-2
TLDR
Increasing the hydrophobicity of pseudin-2, while maintaining the amphipathic character of the molecule, by substitution of neutral amino acids on the Hydrophobic face of the alpha-helix by L-phenylalanine had only minor effects on antimicrobial and hemolytic activities. Expand
Pseudin-2: an antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog.
TLDR
Four structurally related peptides (pseudins 1-4) with antimicrobial activity were isolated from an extract of the skin of the paradoxical frog Pseudis paradoxa and Circular dichroism studies showed that the pseudins belong to the class of cationic, amphipathic alpha-helical antimicrobial peptides. Expand
Brevinin-1 and multiple insulin-releasing peptides in the skin of the frog Rana palustris.
TLDR
The skin secretions of R. palustris frogs contain a novel class of peptides with insulin-releasing activity that merit further investigation, and these peptides are determined by mass spectrometry and N-terminal amino acid sequencing. Expand
Novel Insulin-Releasing Peptides in the Skin of Phyllomedusa trinitatis Frog Include 28 Amino Acid Peptide From Dermaseptin BIV Precursor
TLDR
These data demonstrate that the defensive skin secretions of P. trinitatis contain biologically active peptides, which may have mammalian counterparts and merit further investigation as insulin secretagogues. Expand
Characterization of naturally occurring peptides in the skin secretion of Rana pipiens frog reveal pipinin-1 as the novel insulin-releasing agent.
TLDR
The skin secretions of Rana pipiens frogs are revealed to be a rich source of insulin-releasing peptides and the discovery of insulinotropic activity for pipinin-1, initially characterized as an antimicrobial is interesting and merits further investigation. Expand
Insulin releasing properties of the temporin family of antimicrobial peptides.
TLDR
The temporins at 10(-7) M had no effect on intracellular calcium concentrations suggesting that they stimulate insulin release via a K(ATP) channel- independent pathway. Expand
Isolation and characterisation of an unexpected class of insulinotropic peptides in the skin of the frog Agalychnis litodryas
TLDR
Data indicate that the skin secretions of A. litodryas frogs contain biologically active peptides which merit further evaluation as a new class of insulin secretagogues. Expand
Isolation and structural characterization of novel Rugosin A-like insulinotropic peptide from the skin secretions of Rana saharica frog
TLDR
Skin secretions of Rana saharica frogs contain novel peptides with insulin-releasing activity, and mass spectrometry analysis of two peaks indicated the molecular masses of 1892.6 and 2930.8Da. Expand
The therapeutic potential of antimicrobial peptides from frog skin
TLDR
Despite showing broad-spectrum activity against strains of antibiotic-resistant bacteria and potent activity against certain pathogenic fungi and protozoa, the frog skin antimicrobial peptides have received particular attention and their therapeutic potential remains to be realized. Expand
Skin secretions of Rana saharica frogs reveal antimicrobial peptides esculentins-1 and -1B and brevinins-1E and -2EC with novel insulin releasing activity.
TLDR
Data indicate that the skin secretions of Rana saharica frogs contain bioactive molecules with significant insulin-releasing activity and relatives of the brevinin/esculentin peptide family merit further investigation as novel insulin secretagogues. Expand
...
1
2
3
...