Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides
Ocellatins are a family of antimicrobial peptides found exclusively in the <i>Leptodactylus</i> genus. To date, 10 species have been studied and more than 23 peptides described. Here we report the sequences of five new peptides from the skin of the frog <i>Leptodactylus latrans<...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-10-01
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| Series: | Antibiotics |
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| Online Access: | https://www.mdpi.com/2079-6382/9/11/751 |
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| author | Mariela M. Marani Silvana Aguilar Ana P. Cuzziol Boccioni Natalia L. Cancelarich Néstor G. Basso Fernando Albericio |
| author_facet | Mariela M. Marani Silvana Aguilar Ana P. Cuzziol Boccioni Natalia L. Cancelarich Néstor G. Basso Fernando Albericio |
| author_sort | Mariela M. Marani |
| collection | DOAJ |
| description | Ocellatins are a family of antimicrobial peptides found exclusively in the <i>Leptodactylus</i> genus. To date, 10 species have been studied and more than 23 peptides described. Here we report the sequences of five new peptides from the skin of the frog <i>Leptodactylus latrans</i> (Anura: Leptodactylidae) determined by cDNA cloning of the complete prepro-peptide structures. The mature peptides were characterized with in silico tools and compared with those previously described. With 21 amino acid residues, this new set of peptides not previously described in the <i>Leptodactylus</i> genus share between 100 and 76.2% similarity to ocellatin antimicrobial peptides. These novel peptides are cationic and their three-dimensional (3D) structure holds the highly conserved residues G<sup>1</sup>, D<sup>4</sup>, K<sup>7</sup>, and K<sup>11</sup> and a high theoretical amphipathic α-helix content. Furthermore, in silico analyses of these new peptides predicted antimicrobial activity. This study is framed in the context of previous work published about ocellatins, and therefore, provides a review of this intriguing family of peptides. |
| first_indexed | 2024-03-10T15:14:47Z |
| format | Article |
| id | doaj.art-576d6423ebc54e54a5077be4d15d690b |
| institution | Directory Open Access Journal |
| issn | 2079-6382 |
| language | English |
| last_indexed | 2024-03-10T15:14:47Z |
| publishDate | 2020-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antibiotics |
| spelling | doaj.art-576d6423ebc54e54a5077be4d15d690b2023-11-20T19:00:14ZengMDPI AGAntibiotics2079-63822020-10-0191175110.3390/antibiotics9110751Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing PeptidesMariela M. Marani0Silvana Aguilar1Ana P. Cuzziol Boccioni2Natalia L. Cancelarich3Néstor G. Basso4Fernando Albericio5IPEEC-CONICET, Consejo Nacional de Investigaciones Científicas y Técnicas, Bvd. Brown 2915, U9120ACD Puerto Madryn, ArgentinaIPEEC-CONICET, Consejo Nacional de Investigaciones Científicas y Técnicas, Bvd. Brown 2915, U9120ACD Puerto Madryn, ArgentinaIPEEC-CONICET, Consejo Nacional de Investigaciones Científicas y Técnicas, Bvd. Brown 2915, U9120ACD Puerto Madryn, ArgentinaIPEEC-CONICET, Consejo Nacional de Investigaciones Científicas y Técnicas, Bvd. Brown 2915, U9120ACD Puerto Madryn, ArgentinaIDEAus-CONICET, Consejo Nacional de Investigaciones Científicas y Técnicas, Bvd. Brown 2915, U9120ACD Puerto Madryn, ArgentinaPeptide Science Laboratory, School of Chemistry and Physics, University of KwaZulu-Natal, 4001 Durban, South AfricaOcellatins are a family of antimicrobial peptides found exclusively in the <i>Leptodactylus</i> genus. To date, 10 species have been studied and more than 23 peptides described. Here we report the sequences of five new peptides from the skin of the frog <i>Leptodactylus latrans</i> (Anura: Leptodactylidae) determined by cDNA cloning of the complete prepro-peptide structures. The mature peptides were characterized with in silico tools and compared with those previously described. With 21 amino acid residues, this new set of peptides not previously described in the <i>Leptodactylus</i> genus share between 100 and 76.2% similarity to ocellatin antimicrobial peptides. These novel peptides are cationic and their three-dimensional (3D) structure holds the highly conserved residues G<sup>1</sup>, D<sup>4</sup>, K<sup>7</sup>, and K<sup>11</sup> and a high theoretical amphipathic α-helix content. Furthermore, in silico analyses of these new peptides predicted antimicrobial activity. This study is framed in the context of previous work published about ocellatins, and therefore, provides a review of this intriguing family of peptides.https://www.mdpi.com/2079-6382/9/11/751in silico techniquesleptodactylidae<i>Leptodactylus latrans</i>natural productsbioprospection |
| spellingShingle | Mariela M. Marani Silvana Aguilar Ana P. Cuzziol Boccioni Natalia L. Cancelarich Néstor G. Basso Fernando Albericio Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides Antibiotics in silico techniques leptodactylidae <i>Leptodactylus latrans</i> natural products bioprospection |
| title | Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides |
| title_full | Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides |
| title_fullStr | Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides |
| title_full_unstemmed | Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides |
| title_short | Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides |
| title_sort | identification of new ocellatin antimicrobial peptides by cdna precursor cloning in the frame of this family of intriguing peptides |
| topic | in silico techniques leptodactylidae <i>Leptodactylus latrans</i> natural products bioprospection |
| url | https://www.mdpi.com/2079-6382/9/11/751 |
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