Journal of Peptide Science · 1998 · 76 citations · 16 references
Life SciencesBiochemistryMicrobiologyAntimicrobial PharmacologyProtein BiochemistrySequence AnalysisAntimicrobial PeptidesPeptide AnalysisPeptide ChemistryPeptide IdentificationAntibacterial PeptidesAntimicrobial Peptide ActivityFast Atom BombardmentPeptide Structure-activity Relationships
Six peptides have been isolated and characterized from the dorsal glands of the tree frog Litoria genimaculata. One of these is the known hypotensive peptide caerulein; the others have been named maculatins. The amino acid sequences of the maculatin peptides have been determined using a combination of fast atom bombardment mass spectrometry and automated Edman sequencing. Four of the maculatin peptides show antibiotic activity, with maculatin 1.1 [GLFGVLAKVAAHVVPAIAEHF(NH2)] showing the most pronounced activity, particularly against gram-positive organisms. Maculatin 1.1 resembles the known caerin 1 antibiotic peptides, except that four of the central amino acid residues (of the caerin 1 system) are missing in maculatin 1.1. A comparison of the antibiotic activity of maculatin 1.1 with those of caerin 1.1 is reported.
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Bergey's Manual of Systematic Bacteriology
Annals of Internal Medicine · 1990 · 15.7K citations
Bergey's manual of systematic bacteriology
Renzo Bazzo, Michael J. Tappin, Annalisa Pastore et al. · European Journal of Biochemistry · 1988 · 334 citations · Full text