A family of acyclic brevinin-1 peptides from the skin of the Ryukyu brown frog Rana okinavana
| Autor: | J. Michael Conlon, David Cosquer, Hubert Vaudry, Laurent Coquet, Thierry Jouenne, Shawichi Iwamuro, Agnes Sonnevend |
|---|---|
| Přispěvatelé: | University of Ulster, Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Tohoku University [Sendai] |
| Jazyk: | angličtina |
| Rok vydání: | 2005 |
| Předmět: |
Staphylococcus aureus
Ranidae Physiology [SDV]Life Sciences [q-bio] Molecular Sequence Data Peptide Microbial Sensitivity Tests Biology medicine.disease_cause Biochemistry Amphibian Proteins 03 medical and health sciences Cellular and Molecular Neuroscience Residue (chemistry) 0302 clinical medicine Endocrinology Salientia Escherichia coli Consensus sequence medicine Animals Amino Acid Sequence Cysteine ComputingMilieux_MISCELLANEOUS Skin 030304 developmental biology chemistry.chemical_classification 0303 health sciences Tissue Extracts Proteins biology.organism_classification Anti-Bacterial Agents Amino acid Molecular Weight chemistry Glycine Female Peptides Frog Skin 030217 neurology & neurosurgery Antimicrobial Cationic Peptides |
| Zdroj: | Peptides Peptides, Elsevier, 2005, 26 (2), pp.185-190. ⟨10.1016/j.peptides.2004.08.008⟩ |
| ISSN: | 0196-9781 |
| DOI: | 10.1016/j.peptides.2004.08.008⟩ |
| Popis: | The 24 amino-acid residue antimicrobial peptide, brevinin-1 is synthesized in the skins of a wide range of species of Eurasian and North American frogs belonging to the genus Rana . All previously characterized brevinin-1 peptides contain the cyclic heptapeptide domain Cys 18 -(Xaa) 4 -Lys-Cys 24 at the COOH-terminus of the molecule. Four structurally related peptides were isolated from an extract of the skin of the Ryukyu brown frog Rana okinavana. The amino acid sequences of the peptides [Phe-(Xaa) 4 -Ile-(Xaa) 2 -Leu-Ala-Lys-Gly-Leu-Pro-Ser-Leu-Ile-Xaa-Leu-Xaa-Lys-Lys·NH 2 ] identified them as members of the brevinin-1 family that lacked the COOH-terminal cyclic domain but contained a C-terminally α-amidated residue. It is suggested, as one possibility, that the Cys 18 in the brevinin-1 consensus sequence has been deleted and the Cys 24 residue has mutated to a glycine that acts as substrate for peptidyl-glycine α-amidating monooxygenase. The peptides potently inhibited the growth of Escherichia coli and Staphylococcus aureus confirming that a cyclic domain is not necessary for antimicrobial activity. A fifth peptide (SFLNFFKGAA 10 KNLLAAGLDK 20 LKCKISGTQC 30 ), that also displayed broad-spectrum antimicrobial activity, was isolated from the skin extract and showed structural similarity with members of the ranatuerin-2 family previously isolated from the skin of North American ranid frogs. |
| Databáze: | OpenAIRE |
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