Cinerascetins, New Peptides from<i>Hypsiboas cinerascens</i>: MALDI LIFT-TOF-MS/MS<i>de novo</i>Sequence and Imaging Analysis

Almeida, Richardson Alves de; Gordo, Marcelo; Silva, Felipe M. A. da; Araújo, Rafael Canonenco de; Ramada, Marcelo Henrique Soller; Abrão, Fernando Yano; Costa, Túlio O. G.; Koolen, Héctor H. F.; Souza, Afonso Duarte Leão de; Bloch, Carlos

doi:10.5935/0103-5053.20150219

Cited by 6 publications

(15 citation statements)

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“… Amino acid sequence alignment of three of the peptides identified in situ by MALDI IMS in the transverse section of dorsal and lateral skin samples of B. punctata ( B. punctata _2367, B. punctata _1976, and B. punctata _1683) and similar or identical peptides identified in the gland secretion of B. punctata [ B. punctata _P11, B. punctata _P12, and B. punctata _P13 (this article); B. punctata _Hsp9 and B. punctata _Psp10 and B. cinerascens _Crs]. 15 Arrows indicate putative proteolytic cleavage site based on sequence identities between peptides identified by in situ MALDI IMS and peptides identified in the gland secretion. …”

Section: Resultsmentioning

confidence: 83%

“…The specific sequences included were the following: eight peptides of B. raniceps (raniseptins), 18 peptides of Boana albopunctata (hylin-1a and Ctx-Ha), 16 peptides of Boana lundii (hylin-b1 and hylin-b2), 17 one peptide of Boana semilineata (Hs-1), 40 and one peptide of B. cinerascens (Cinerascetin-01). 15 For comparison, uncertainties (X) in the peptide sequence identified in our study in B. punctata were either left as Leu or were tentatively assigned to Leu or to Ile based on similarities with the amino acid sequence identified in the same or related species and also on comparisons with synthetic analogues ( Table S4 ).…”

Section: Methodsmentioning

confidence: 99%

“…punctata is a very interesting model to investigate peptides in anurans from morphological, functional, and evolutionary perspectives because the structure and ultrastructure of the skin has been well-characterized . Moreover, the skin secretion has at least two peptides, one with antimicrobial activity (hylaseptin P1; HSP1), which may actually be a cleavage form of a larger peptide, , and a second one, which is likely related to an antipredatory function (phenylseptin). , …”

Section: Introductionmentioning

confidence: 99%

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Cleavage of Peptides from Amphibian Skin Revealed by Combining Analysis of Gland Secretion and in Situ MALDI Imaging Mass Spectrometry

et al. 2018

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Peptides from skin secretions of amphibians are considered important components of their immune system and also play a relevant role in their defense mechanism against predators. Herein, by using mass spectrometry (MS), we characterize the sequence of 13 peptides from the gland secretion of the hylid tree frog, Boana punctata. Using in situ matrix-assisted laser desorption ionization imaging MS of a transverse section of the skin tissue, we show that some peptides are stored as longer molecules that are cleaved after being secreted, whereas others do not undergo any modification. Sequence comparison with peptides from other Boana species and analysis of the three-dimensional theoretical structure indicate that this cleavage depends on both the presence of a specific sequence motif and the secondary structure. The fact that peptides undergo a rapid cleavage upon secretion suggests that stored and secreted peptides may have distinct roles for anuran survival, including defense against pathogens and predators.

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Section: Resultsmentioning

confidence: 83%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cleavage of Peptides from Amphibian Skin Revealed by Combining Analysis of Gland Secretion and in Situ MALDI Imaging Mass Spectrometry

et al. 2018

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“…From the skin secretions of different species of the genus Hypsiboas , currently reclassified as Boana [ 8 ], several broad-spectrum antimicrobial peptides have been isolated [ 9 , 10 , 11 , 12 ]. Our research group originally found a new class of peptides named Hylins from the skin secretion of Hyla biobeba (now Boana lundii ) with hemolytic activity [ 13 ] and, later, Hylin a1 from Hypsiboas albopunctatus (now Boana albopunctata ) with a broad spectrum of activity against Gram-positive and Gram-negative bacteria and fungi, in addition to strong hemolytic activity [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

Figainin 1, a Novel Amphibian Skin Peptide with Antimicrobial and Antiproliferative Properties

et al. 2020

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Amphibian skin secretions are abundant in bioactive compounds, especially antimicrobial peptides. These molecules are generally cationic and rich in hydrophobic amino acids, have an amphipathic structure and adopt an α-helical conformation when in contact with microorganisms membranes. In this work, we purified and characterized Figainin 1, a novel antimicrobial and antiproliferative peptide from the cutaneous secretion of the frog Boana raniceps. Figainin 1 is a cationic peptide with eighteen amino acid residues—rich in leucine and isoleucine, with an amidated C-terminus—and adopts an α-helical conformation in the presence of trifluoroethanol (TFE). It displayed activity against Gram-negative and especially Gram-positive bacteria, with MIC values ranging from 2 to 16 µM, and showed an IC50 value of 15.9 µM against epimastigote forms of T. cruzi; however, Figanin 1 did not show activity against Candida species. This peptide also showed cytolytic effects against human erythrocytes with an HC50 of 10 µM, in addition to antiproliferative activity against cancer cells and murine fibroblasts, with IC50 values ranging from 10.5 to 13.7 µM. Despite its adverse effects on noncancerous cells, Figainin 1 exhibits interesting properties for the development of new anticancer agents and anti-infective drugs against pathogenic microorganisms.

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“…Antimicrobial peptides are a group of molecules conserved during evolution that can be found in a wide range of organisms [ 3 , 4 ]. Most of these peptides have similar characteristics: (a) they are cationic with two or more positive charges, (b) contain from ten to fifty amino acid residues, (c) have 50% hydrophobic residues, and (d) form α-amphipathic helix [ 5 , 6 ].…”

Section: Introductionmentioning

confidence: 99%

Evaluation of cytotoxicity features of antimicrobial peptides with potential to control bacterial diseases of citrus

et al. 2018

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Antimicrobial peptides (AMPs) can be found in various organisms, and could be considered an alternative for pesticides used to control plant pathogens, including those affecting citrus. Brazil is the largest producer and exporter of frozen concentrated orange juice in the world. However, the citrus industry has been affected by several diseases such as citrus canker and huanglongbing (HLB), caused by the bacteria Xanthomonas citri subsp. citri (X.citri) and Candidatus Liberibacter asiaticus (CaLas), respectively. In order to control these pathogens, putative AMPs were prospected in databases containing citrus sequences. Furthermore, AMPs already reported in the literature were also used for in vitro and in vivo assays against X.citri. Since CaLas cannot be cultivated in vitro, surrogates as Sinorhizobium meliloti and Agrobacterium tumefaciens were used. This study reports the evaluation of six AMPs obtained from different sources, two of them from Citrus spp. (citrus-amp1 and citrus-amp2), three from amphibians (Hylin-a1, K0-W6-Hy-a1 and Ocellatin 4-analogue) and one from porcine (Tritrpticin). Peptides K0-W6-Hy-a1, Ocellatin 4-analogue, and citrus-amp1 showed bactericidal activity against X.citri and S. meliloti and bacteriostatic effect on A. tumefaciens. These results were confirmed for X.citri in planta. In addition cytotoxicity evaluations of these molecules were performed. The AMPs that showed the lowest hemolytic activities were Triptrpticin, citrus-amp1 and citrus-amp2. Citrus-amp1 and citrus-amp2 not presented toxicity in experiments using in vivo model, G. mellonella and U87 MG cells. To verify the interaction of these AMPs with bacteria and erythrocyte cell membranes, vesicles mimicking these cells were built. Citrus-amp1 and Tritrpticin exhibited higher affinity to bacterial membranes, while Ocellatin 4-analogue and Hylin-a1 showed higher affinity to erythrocyte membranes; exclude their use in citrus. This work demonstrates an essential alternative, trough AMPs obtained from Citrus spp., which can be feasibly used to control bacterial pathogens.

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Cinerascetins, New Peptides fromHypsiboas cinerascens: MALDI LIFT-TOF-MS/MSde novoSequence and Imaging Analysis

Cited by 6 publications

References 0 publications

Cleavage of Peptides from Amphibian Skin Revealed by Combining Analysis of Gland Secretion and in Situ MALDI Imaging Mass Spectrometry

Cleavage of Peptides from Amphibian Skin Revealed by Combining Analysis of Gland Secretion and in Situ MALDI Imaging Mass Spectrometry

Figainin 1, a Novel Amphibian Skin Peptide with Antimicrobial and Antiproliferative Properties

Evaluation of cytotoxicity features of antimicrobial peptides with potential to control bacterial diseases of citrus

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