A glycine-leucine-rich peptide structurally related to the plasticins from skin secretions of the frog Leptodactylus laticeps (Leptodactylidae)

J. Michael Conlon, Yasser Abdel-Wahab, Peter Flatt, Jerome Leprince, Hubert Vaudry, Thierry Jouenne, Eric Condamine

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Abstract

A glycine-leucine-rich peptide was isolated from norepinephrine-stimulated skin secretions of the Sante Fe frog Leptodactylus laticeps (Leptodactylidae) whose primary structure (Gly-Leu-Val-Asn-Gly-Leu-Leu-Ser-Ser-Val-Leu-Gly-Gly-Gly-Gln-Gly-Gly-Gly -Gly-Leu-Leu-Gly-Gly-Ile-Leu) contains the (GXXXG)(3) motif found in the plasticins, previously identified only in phyllomedusid frogs (Hylidae). Circular dichroism studies showed that the secondary structure of the peptide, termed plasticin-L1, was markedly solvent-dependent displaying a random coil conformation in water, a beta-sheet structure in methanol, and an alpha-helical conformation in 50% trifluoroethanol-water. A synthetic replicate of the peptide did not inhibit the growth of Escherichia coli or Staphylococcus aureus or lyse human erythrocytes at concentrations up to 500 mu M. At relatively high concentrations (> 1 microM), the peptide produced a significant (P <0.05), although modest (139% of basal rate at 3 mu M), increase in the rate of glucose-induced release of insulin from rat clonal BRIN-BD11 beta cells without increasing the rate of release of lactate dehydrogenase. A peptide, termed ocellatin-L2 was also identified in the skin secretion that was identical to the previously described ocellatin-L1 except for the substitution Asn(23) to Asp. Ocellatin-L2 was devoid of antimicrobial and hemolytic activity but also showed significant activity in stimulating insulin release from BRIN-BD11 cells (181% of basal rate at 3 microM). (C) 2009 Elsevier Inc. All rights reserved.
LanguageEnglish
Pages888-892
JournalPeptides
Volume30
Issue number5
DOIs
Publication statusPublished - May 2009

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glycine (amino acid)
skin (animal)
leucine
frogs
secretion
peptides
insulin
circular dichroism spectroscopy
synthetic peptides
Hylidae
norepinephrine
lactate dehydrogenase
Staphylococcus aureus
methanol
erythrocytes
anti-infective agents
water
cells
Escherichia coli
glucose

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@article{96f246e4d4f1437f89d42e400d8a1e99,
title = "A glycine-leucine-rich peptide structurally related to the plasticins from skin secretions of the frog Leptodactylus laticeps (Leptodactylidae)",
abstract = "A glycine-leucine-rich peptide was isolated from norepinephrine-stimulated skin secretions of the Sante Fe frog Leptodactylus laticeps (Leptodactylidae) whose primary structure (Gly-Leu-Val-Asn-Gly-Leu-Leu-Ser-Ser-Val-Leu-Gly-Gly-Gly-Gln-Gly-Gly-Gly -Gly-Leu-Leu-Gly-Gly-Ile-Leu) contains the (GXXXG)(3) motif found in the plasticins, previously identified only in phyllomedusid frogs (Hylidae). Circular dichroism studies showed that the secondary structure of the peptide, termed plasticin-L1, was markedly solvent-dependent displaying a random coil conformation in water, a beta-sheet structure in methanol, and an alpha-helical conformation in 50{\%} trifluoroethanol-water. A synthetic replicate of the peptide did not inhibit the growth of Escherichia coli or Staphylococcus aureus or lyse human erythrocytes at concentrations up to 500 mu M. At relatively high concentrations (> 1 microM), the peptide produced a significant (P <0.05), although modest (139{\%} of basal rate at 3 mu M), increase in the rate of glucose-induced release of insulin from rat clonal BRIN-BD11 beta cells without increasing the rate of release of lactate dehydrogenase. A peptide, termed ocellatin-L2 was also identified in the skin secretion that was identical to the previously described ocellatin-L1 except for the substitution Asn(23) to Asp. Ocellatin-L2 was devoid of antimicrobial and hemolytic activity but also showed significant activity in stimulating insulin release from BRIN-BD11 cells (181{\%} of basal rate at 3 microM). (C) 2009 Elsevier Inc. All rights reserved.",
author = "Conlon, {J. Michael} and Yasser Abdel-Wahab and Peter Flatt and Jerome Leprince and Hubert Vaudry and Thierry Jouenne and Eric Condamine",
year = "2009",
month = "5",
doi = "10.1016/j.peptides.2009.01.008",
language = "English",
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pages = "888--892",
number = "5",

}

A glycine-leucine-rich peptide structurally related to the plasticins from skin secretions of the frog Leptodactylus laticeps (Leptodactylidae). / Conlon, J. Michael; Abdel-Wahab, Yasser; Flatt, Peter; Leprince, Jerome; Vaudry, Hubert; Jouenne, Thierry; Condamine, Eric.

Vol. 30, No. 5, 05.2009, p. 888-892.

Research output: Contribution to journalArticle

TY - JOUR

T1 - A glycine-leucine-rich peptide structurally related to the plasticins from skin secretions of the frog Leptodactylus laticeps (Leptodactylidae)

AU - Conlon, J. Michael

AU - Abdel-Wahab, Yasser

AU - Flatt, Peter

AU - Leprince, Jerome

AU - Vaudry, Hubert

AU - Jouenne, Thierry

AU - Condamine, Eric

PY - 2009/5

Y1 - 2009/5

N2 - A glycine-leucine-rich peptide was isolated from norepinephrine-stimulated skin secretions of the Sante Fe frog Leptodactylus laticeps (Leptodactylidae) whose primary structure (Gly-Leu-Val-Asn-Gly-Leu-Leu-Ser-Ser-Val-Leu-Gly-Gly-Gly-Gln-Gly-Gly-Gly -Gly-Leu-Leu-Gly-Gly-Ile-Leu) contains the (GXXXG)(3) motif found in the plasticins, previously identified only in phyllomedusid frogs (Hylidae). Circular dichroism studies showed that the secondary structure of the peptide, termed plasticin-L1, was markedly solvent-dependent displaying a random coil conformation in water, a beta-sheet structure in methanol, and an alpha-helical conformation in 50% trifluoroethanol-water. A synthetic replicate of the peptide did not inhibit the growth of Escherichia coli or Staphylococcus aureus or lyse human erythrocytes at concentrations up to 500 mu M. At relatively high concentrations (> 1 microM), the peptide produced a significant (P <0.05), although modest (139% of basal rate at 3 mu M), increase in the rate of glucose-induced release of insulin from rat clonal BRIN-BD11 beta cells without increasing the rate of release of lactate dehydrogenase. A peptide, termed ocellatin-L2 was also identified in the skin secretion that was identical to the previously described ocellatin-L1 except for the substitution Asn(23) to Asp. Ocellatin-L2 was devoid of antimicrobial and hemolytic activity but also showed significant activity in stimulating insulin release from BRIN-BD11 cells (181% of basal rate at 3 microM). (C) 2009 Elsevier Inc. All rights reserved.

AB - A glycine-leucine-rich peptide was isolated from norepinephrine-stimulated skin secretions of the Sante Fe frog Leptodactylus laticeps (Leptodactylidae) whose primary structure (Gly-Leu-Val-Asn-Gly-Leu-Leu-Ser-Ser-Val-Leu-Gly-Gly-Gly-Gln-Gly-Gly-Gly -Gly-Leu-Leu-Gly-Gly-Ile-Leu) contains the (GXXXG)(3) motif found in the plasticins, previously identified only in phyllomedusid frogs (Hylidae). Circular dichroism studies showed that the secondary structure of the peptide, termed plasticin-L1, was markedly solvent-dependent displaying a random coil conformation in water, a beta-sheet structure in methanol, and an alpha-helical conformation in 50% trifluoroethanol-water. A synthetic replicate of the peptide did not inhibit the growth of Escherichia coli or Staphylococcus aureus or lyse human erythrocytes at concentrations up to 500 mu M. At relatively high concentrations (> 1 microM), the peptide produced a significant (P <0.05), although modest (139% of basal rate at 3 mu M), increase in the rate of glucose-induced release of insulin from rat clonal BRIN-BD11 beta cells without increasing the rate of release of lactate dehydrogenase. A peptide, termed ocellatin-L2 was also identified in the skin secretion that was identical to the previously described ocellatin-L1 except for the substitution Asn(23) to Asp. Ocellatin-L2 was devoid of antimicrobial and hemolytic activity but also showed significant activity in stimulating insulin release from BRIN-BD11 cells (181% of basal rate at 3 microM). (C) 2009 Elsevier Inc. All rights reserved.

U2 - 10.1016/j.peptides.2009.01.008

DO - 10.1016/j.peptides.2009.01.008

M3 - Article

VL - 30

SP - 888

EP - 892

IS - 5

ER -