Structure and function of cationic hylin bioactive peptides from the tree frog Boana pulchella in interaction with lipid membranes

Aguilar, Silvana; Brunetti, Andrés E.; Garay, Aisel Valle; Santos, Liem Canet; Pérez, Luis E.; Moreira, Daniel C.; Cancelarich, Lorena; Barbosa, Éder Alves; Basso, Néstor Guillermo; Freitas, Sonia María de; Faivovich, Julián; Brand, Guilherme; Cabrera, Gabriela M.; Leite, J. R.; Marani, Mariela M.

doi:10.1016/j.peptides.2022.170900

Cited by 9 publications

(14 citation statements)

References 41 publications

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“…Hylins Are Hypervariable Peptides with a Conserved Motif. The analysis of new hylins' sequences reported here, along with those reported in previous studies 25,[27][28][29]34,35 (see Supporting Information for nomenclature comments of hylins), showed that peptides within this family possess 18− 20 amino acids and variable sequences that share common patterns (Figure 1). Most have Phe at the N-terminus and a positively charged amino acid, either Lys or Arg, at the Cterminus.…”

Section: ■ Results and Discussionsupporting

confidence: 76%

“…However, unlike hylins, Pro from maculatins is close to the C-terminus, suggesting a convergent evolution related to the role of this amino acid in peptide−membrane interactions. In addition, previous studies on hylins 25,28,35 demonstrate they are unstructured in solution but adopt a secondary structure with α-helix content in membrane-mimetic environments. This ability can be associated with the amphipathic structure characteristic of several helical AMPs by which the hydrophobic region interacts with the lipids on the membrane, and the polar residues are oriented first toward the surface environment and finally to the pore lumen.…”

Section: ■ Results and Discussionmentioning

confidence: 91%

“…Peptides sequenced de novo for this study present Leu/Ile uncertainty. Therefore, the assignation depicted here is tentative and was based on comparison with available transcriptomes 34 and cDNA sequences 25 or following a parsimonious criterion (see Supporting Information for details). The sequence logo with the letter size for each amino acid representing the frequency in the total number of hylins is depicted on the top graph.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…Marques ( 2016) is an unpublished thesis. Because previous studies 25,28 showed that hylins adopt an αhelical conformation under natural biological conditions, we interpreted their sequences using a helical wheel representation. In this scenario, hylins have a clear amphipathic arrangement where almost all the hydrophobic residues (i.e., Leu, Iso, Val, Phe, and Ala) are in the nonpolar face (Figures 2, S1).…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…This situation is more notorious when studying species for which sequence comparisons are limited to distantly related taxa, as it occurs with the subfamily Hylinae. Indeed, though being the largest hylid subfamily (∼745 species), the analysis of AMPs in Hylinae is restricted to very few species, − with the description of nine peptide families.…”

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confidence: 99%

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The Significance of Hypervariability and Conserved Motifs in Antimicrobial Peptides from Tree Frogs

et al. 2023

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Amphibians' skin is a rich source of natural antimicrobial peptides (AMPs). These AMPs exhibit marked inter-and intraspecific sequence divergence linked to the arms race between host and pathogens. Here, we combine peptidomics, molecular modeling, and phylogenetic analyses to understand the evolution of AMPs in Cophomantini, a diverse clade of neotropical tree frogs, and to investigate their interaction with bacterial membranes. Consistent with results in other amphibians, all species of Cophomantini secrete a mixture of peptides. We selected the hylin peptide family to survey sequence variability and the presence of common amino acid motifs. We found that most species secrete a unique set of hylins that, though variable, share the conserved motif Gly-X-X-X-Pro-Ala-X-X-Gly, with Gly and Pro colocalizing with charged or polar residues. Our modeling revealed that Pro curves the peptide through a hinge, facilitating its insertion into the bacterial membrane and, once inserted, contributes to stabilizing the pore structure. The phylogenetic inference using hylid prepropeptides showed the need to classify new AMPs using the full-length sequence of the prepro-peptide region and highlighted the complex relationships between peptide families. Our findings revealed that conserved motifs occurred independently in distinct AMP families, suggesting a convergent evolution and a significant role in peptide−membrane interactions.

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