A Novel Ocellatin-P1 Isoform from Leptodactylus labyrinthicus Frog Skin Secretion: Purification, Biological Properties and Three-Dimensional Structure

, which remains largely preserved even at 95 °C. NMR Hydrogen/Deuterium (H/D) exchange experiments suggest that ocellatin-LB3 adopts a preferential orientation when interacting with SDS micelles. Based on the similarity among ocellatins, and on the physicochemical and structural properties of this peptide, a possible membrane-mediated mode of action is proposed, although this remains to be experimentally validated.

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Publication Details

Journal
International Journal of Molecular Sciences
Published
2026-04-20
DOI
https://doi.org/10.3390/ijms27083658
Primary Topic
Antimicrobial Peptides and Activities
Type
article
Field-Weighted Citation Impact
0.00

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article

A Novel Ocellatin-P1 Isoform from Leptodactylus labyrinthicus Frog Skin Secretion: Purification, Biological Properties and Three-Dimensional Structure

Alice da Cunha Morales Álvares, César Augusto Prías-Márquez, Wagner Fontes, Ricardo Bentes Azevedo et al.
International Journal of Molecular Sciences
Antimicrobial Peptides and Activities
article

A Novel Ocellatin-P1 Isoform from Leptodactylus labyrinthicus Frog Skin Secretion: Purification, Biological Properties and Three-Dimensional Structure

Alice da Cunha Morales Álvares, César Augusto Prías-Márquez, Wagner Fontes, Ricardo Bentes Azevedo, E.S.F. Alves, Osmindo Rodrigues Pires Júnior, Rafael Marques Porto, Luciano M. Lião, Alexandra Maria dos Santos Carvalho, Mariana S. Castro, Fabiano José Queiroz Costa, Eduardo Maffud Cilli, Aline Oliveira, Sônia Maria de Freitas, Carlos José Correia de Santana, Izabela Marques Dourado Bastos, Isabel de Fátima Correia Batista, Isabelle S. Luz, Felipe da Silva Mendonça de Melo, Henrique de Oliveira Noronha, João Paulo Stawiarski Miranda, Marco Antônio Damasceno Faustino
article en

Abstract

, which remains largely preserved even at 95 °C. NMR Hydrogen/Deuterium (H/D) exchange experiments suggest that ocellatin-LB3 adopts a preferential orientation when interacting with SDS micelles. Based on the similarity among ocellatins, and on the physicochemical and structural properties of this peptide, a possible membrane-mediated mode of action is proposed, although this remains to be experimentally validated.

International Journal of Molecular SciencesVol. 27(8)
Universidade de Brasília (BR), Instituto Butantan (BR), Instituto de Saúde (BR), Rede de Química e Tecnologia (PT), Universidade Federal de Goiás (BR), Universidade Estadual Paulista (Unesp) (BR)
Fundação de Amparo à Pesquisa do Estado de São Paulo, Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Conselho Nacional de Desenvolvimento Científico e Tecnológico, Fundação de Empreendimentos Científicos e Tecnológicos
Openalex Percentile: Top 23%
Antimicrobial Peptides and Activities
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