Kassinatuerin-1

A peptide with broad-spectrum antimicrobial activity isolated from the skin of the hyperoliid frog, kassina senegalensis

Beverly Mattute, Floyd C. Knoop, J. Michael Conlon

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Kassinatuerin-1 (GFMKYIGPLI10PHAVKAISDL20I.NH2) was isolated in high yield (75 nmol/g) from an extract of the skin of a Hyperoliid frog, the African running frog Kassina senegalensis and its sequence was confirmed by total synthesis. The peptide inhibited growth of the gram-negative bacterium Escherichia coli (minimum inhibitory concentration, MIC = 4 μM), the gram-positive bacterium Staphylococcus aureus (MIC = 8 μM), and the yeast Candida albicans (MIC = 70 μM). A structurally related peptide, kassinatuerin-2 (FIQYLAPLI10PHAVKAISDL20I.NH2) was also isolated in high yield (96 nmol/g) from the extract but was devoid of antimicrobial activity against these microrganisms. Kassinatuerin-1 may be classified with other linear, cationic antimicrobial peptides that can potentially adopt an amphipathic α-helical conformation but it contains almost no amino acid sequence identity with previously characterized bioactive peptides from frog skin. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)433-436
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume268
Issue number2
DOIs
StatePublished - Feb 16 2000

Fingerprint

Anura
Skin
Peptides
Bacteria
Antimicrobial Cationic Peptides
Candida
Gram-Positive Bacteria
Microbial Sensitivity Tests
Gram-Negative Bacteria
Candida albicans
Yeast
Escherichia coli
Conformations
Staphylococcus aureus
Amino Acid Sequence
Yeasts
Amino Acids
Growth
kassinatuerin-1

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Kassinatuerin-1 : A peptide with broad-spectrum antimicrobial activity isolated from the skin of the hyperoliid frog, kassina senegalensis. / Mattute, Beverly; Knoop, Floyd C.; Conlon, J. Michael.

In: Biochemical and Biophysical Research Communications, Vol. 268, No. 2, 16.02.2000, p. 433-436.

Research output: Contribution to journalArticle

@article{a25a50216525443f97e99834a43f40c4,
title = "Kassinatuerin-1: A peptide with broad-spectrum antimicrobial activity isolated from the skin of the hyperoliid frog, kassina senegalensis",
abstract = "Kassinatuerin-1 (GFMKYIGPLI10PHAVKAISDL20I.NH2) was isolated in high yield (75 nmol/g) from an extract of the skin of a Hyperoliid frog, the African running frog Kassina senegalensis and its sequence was confirmed by total synthesis. The peptide inhibited growth of the gram-negative bacterium Escherichia coli (minimum inhibitory concentration, MIC = 4 μM), the gram-positive bacterium Staphylococcus aureus (MIC = 8 μM), and the yeast Candida albicans (MIC = 70 μM). A structurally related peptide, kassinatuerin-2 (FIQYLAPLI10PHAVKAISDL20I.NH2) was also isolated in high yield (96 nmol/g) from the extract but was devoid of antimicrobial activity against these microrganisms. Kassinatuerin-1 may be classified with other linear, cationic antimicrobial peptides that can potentially adopt an amphipathic α-helical conformation but it contains almost no amino acid sequence identity with previously characterized bioactive peptides from frog skin. (C) 2000 Academic Press.",
author = "Beverly Mattute and Knoop, {Floyd C.} and Conlon, {J. Michael}",
year = "2000",
month = "2",
day = "16",
doi = "10.1006/bbrc.2000.2136",
language = "English (US)",
volume = "268",
pages = "433--436",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Kassinatuerin-1

T2 - A peptide with broad-spectrum antimicrobial activity isolated from the skin of the hyperoliid frog, kassina senegalensis

AU - Mattute, Beverly

AU - Knoop, Floyd C.

AU - Conlon, J. Michael

PY - 2000/2/16

Y1 - 2000/2/16

N2 - Kassinatuerin-1 (GFMKYIGPLI10PHAVKAISDL20I.NH2) was isolated in high yield (75 nmol/g) from an extract of the skin of a Hyperoliid frog, the African running frog Kassina senegalensis and its sequence was confirmed by total synthesis. The peptide inhibited growth of the gram-negative bacterium Escherichia coli (minimum inhibitory concentration, MIC = 4 μM), the gram-positive bacterium Staphylococcus aureus (MIC = 8 μM), and the yeast Candida albicans (MIC = 70 μM). A structurally related peptide, kassinatuerin-2 (FIQYLAPLI10PHAVKAISDL20I.NH2) was also isolated in high yield (96 nmol/g) from the extract but was devoid of antimicrobial activity against these microrganisms. Kassinatuerin-1 may be classified with other linear, cationic antimicrobial peptides that can potentially adopt an amphipathic α-helical conformation but it contains almost no amino acid sequence identity with previously characterized bioactive peptides from frog skin. (C) 2000 Academic Press.

AB - Kassinatuerin-1 (GFMKYIGPLI10PHAVKAISDL20I.NH2) was isolated in high yield (75 nmol/g) from an extract of the skin of a Hyperoliid frog, the African running frog Kassina senegalensis and its sequence was confirmed by total synthesis. The peptide inhibited growth of the gram-negative bacterium Escherichia coli (minimum inhibitory concentration, MIC = 4 μM), the gram-positive bacterium Staphylococcus aureus (MIC = 8 μM), and the yeast Candida albicans (MIC = 70 μM). A structurally related peptide, kassinatuerin-2 (FIQYLAPLI10PHAVKAISDL20I.NH2) was also isolated in high yield (96 nmol/g) from the extract but was devoid of antimicrobial activity against these microrganisms. Kassinatuerin-1 may be classified with other linear, cationic antimicrobial peptides that can potentially adopt an amphipathic α-helical conformation but it contains almost no amino acid sequence identity with previously characterized bioactive peptides from frog skin. (C) 2000 Academic Press.

UR - http://www.scopus.com/inward/record.url?scp=0034673291&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034673291&partnerID=8YFLogxK

U2 - 10.1006/bbrc.2000.2136

DO - 10.1006/bbrc.2000.2136

M3 - Article

VL - 268

SP - 433

EP - 436

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -