Sarconesin II, a New Antimicrobial Peptide Isolated from Sarconesiopsis magellanica Excretions and Secretions

Díaz-Roa, Andrea; Espinoza-Culupú, Abraham; Torres, Orlando; Borges, Monamaris Marques; Avino, Ivan N.; Alves, Flávio Lopes; Miranda, Antônio; Patarroyo, Manuel A.; Silva, Pedro I. da; Bello, Felio J.

doi:10.3390/molecules24112077

Cited by 23 publications

(21 citation statements)

References 134 publications

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“…In another analysis, the ability of Mygalin to disrupt the cellular membranes of E. coli was evidenced since the treated bacteria incorporated PI, similar to that visualized with ampicillin. DNA damage has been described in the treatment of bacteria with antibiotics (Kohanski et al, 2010), toxic metals (Espirito Santo et al, 2011) and antimicrobial peptides (Farkas et al, 2017;Diaz-Roa et al, 2019), which led to bacterial death. Inhibition of DNA synthesis was confirmed by light microscopy (Alfred et al, 2013) during the treatment of E. coli with Mygalin and ciprofloxacin, a high bacterial stress-inducing antibiotic (Goswami et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

Mygalin: An Acylpolyamine With Bactericidal Activity

Espinoza-Culupú¹,

Mendes²,

Vitorino³

et al. 2020

Front. Microbiol.

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Inappropriate use of antibiotics favors the selection and spread of resistant bacteria. To reduce the spread of these bacteria, finding new molecules with activity is urgent and necessary. Several polyamine analogs have been constructed and used to control microorganisms and tumor cells. Mygalin is a synthetic acylpolyamine, which are analogs of spermidine, derived from the hemolymph of the spider Acanthoscurria gomesiana. The effective activity of polyamines and their analogs has been associated with their structure. The presence of two acyl groups in the Mygalin structure may give this molecule a specific antibacterial activity. The aim of this study was to identify the mechanisms involved in the interaction of Mygalin with Escherichia coli to clarify its antimicrobial action. The results indicated that Mygalin exhibits intense dose and time-dependent bactericidal activity. Treatment of E. coli with this molecule caused membrane rupture, inhibition of DNA synthesis, DNA damage, and morphological changes. The esterase activity increased along with the intracellular production of reactive oxygen species (ROS) after treatment of the bacteria with Mygalin. In addition, this molecule was able to sequester iron and bind to LPS. We have shown that Mygalin has bactericidal activity with underlying mechanisms involving ROS generation and chelation of iron ions that are necessary for bacterial metabolism, which may contribute to its microbicidal activity. Taken together, our data suggest that Mygalin can be explored as a new alternative drug with antimicrobial potential against Gram-negative bacteria or other infectious agents.

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Section: Discussionmentioning

confidence: 99%

Mygalin: An Acylpolyamine With Bactericidal Activity

Espinoza-Culupú¹,

Mendes²,

Vitorino³

et al. 2020

Front. Microbiol.

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“…The minimum signal required for selecting an ion for a fragmentation event (MS2) was set at 5,000 cps. (8,9) Bioinformatics analysis -MS/MS spectra were selected from a database constructed from the Lucilia UniProt protein databank (17) and the National Centre for Biotechnology Information (NCBI) GenBank database (18) for determining the amino acid (aa) sequences; Proteome Discoverer 1.4 software (Thermo Fisher Scientific Inc) was used as search machine for protein identification. The ProtParam (Expasy) tool was used for calculating the physicochemical parameters, (19) is provided as a service to the life science community by a multidis- ciplinary team at the Swiss Institute of Bioinformatics (SIB ClustalW 2.0 for aligning the sequences (20) and the PEP-FOLD3 server for predicting tertiary structure.…”

Section: Methodsmentioning

confidence: 99%

“…Our previous studies have shown that S. magellanica-derived larval ES have proved effective in treating diabetic rabbits' wounds and as potential therapy against bacterial pathogens. (8,9,15) Such situation becomes even more drastic regarding hard-to-heal wounds in patients having an underlying disease, including diabetes or cardiovascular failure, often involving polymicrobial colonisation by different bacterial strains, such as P. aeruginosa, S. pyogenes, Clostridium perfringens, Corynebacterium spp., Propionibacterium spp., S. aureus and methicillin-resistant S. aureus (MRSA), or in patients in intensive care units (ICU) who have developed a health-care associated-infection (HAI). (16) These ideas have been addressed regarding the detection of new biological properties in S. magellanica-derived AMPs.…”

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confidence: 99%

Characterising four Sarconesiopsis magellanica (Diptera: Calliphoridae) larval fat body-derived antimicrobial peptides

Pérez

Díaz-Roa

Bernal

et al. 2021

Mem. Inst. Oswaldo Cruz

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BACKGROUND The inappropriate use of antibiotics has led to the accelerated growth of resistance to antibiotics. The search for new therapeutic strategies (i.e., antimicrobial peptides-AMPs) has thus become a pressing need.OBJECTIVE Characterising and evaluating Sarconesiopsis magellanica larval fat body-derived AMPs.METHODS Fat body extracts were analysed by reversed-phase high-performance liquid chromatography (RP-HPLC); mass spectrometry was used for characterising the primary structure of the AMPs so found. ProtParam (Expasy) was used for analysing the AMPs' physico-chemical properties. Synthetic AMPs' antibacterial activity was evaluated.FINDINGS Four new AMPs were obtained and called sarconesin III, IV, V and VI. Sarconesin III had an α-helix structure and sarconesins IV, V and VI had linear formations. Oligomer prediction highlighted peptide-peptide interactions, suggesting that sarconesins III, V and VI could form self-aggregations when in contact with the microbial membrane. AMPs synthesised from their native molecules' sequences had potent activity against Gram-positive bacteria and, to a lesser extent, against Gram-negative and drug-resistant bacteria. Sarconesin VI was the most efficient AMP. None of the four synthetic AMPs had a cytotoxic effect. MAIN CONCLUSIONS S. magellanica larval fat body-derived antimicrobial peptides are an important source of AMPs and could be used in different antimicrobial therapies and overcoming bacterial resistance.

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“…Antimicrobial peptides and proteins show a wide distribution and have been isolated from nearly all living organisms. [8][9][10][11][12][13][14][15][16][17][18][19][20][21] Beyond their antimicrobial effects, several AMPs have been shown to have other biological activities. 11,[22][23][24][25] One such protein group that represents the duplicity of activities for the same molecules is the tachykinin family.…”

Section: Introductionmentioning

confidence: 99%

“…Antimicrobial peptides and proteins show a wide distribution and have been isolated from nearly all living organisms. 8 - 21 …”

Section: Introductionmentioning

confidence: 99%

Two Tachykinin-Related Peptides with Antimicrobial Activity Isolated from Triatoma infestans Hemolymph

et al. 2020

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Antimicrobial peptides and proteins (AMPs) are molecules that can interact with microbial cells and lead to membrane disruption or intracellular molecule interactions and death. Several molecules with antimicrobial effects also present other biological activities. One such protein group representing the duplicity of activities is the tachykinin family. Tachykinins (TKs) form a family of neuropeptides in vertebrates with a consensus C-terminal region (F-X-G-Y-R-NH2). Invertebrate TKs and TK-related peptides (TKRPs) are subfamilies found in invertebrates that present high homology with TKs and have similar biological effects. Several of these molecules have already been described but reports of TKRP in Hemiptera species are limited. By analyzing the Triatoma infestans hemolymph by reversed-phase high-performance liquid chromatography, biological assays, and mass spectrometry, two antimicrobial molecules were isolated and identified as TKRPs, which we named as TRP1-TINF and TRP2-TINF (tachykinin-related peptides I and II from T. infestans). TRP1-TINF is a random secondary structure peptide with 9 amino acid residues. It is susceptible to aminopeptidases degradation and is active mainly against Micrococcus luteus (32 μM). TRP2-TINF is a 10-amino acid peptide with a 310 helix secondary structure and is susceptible to carboxypeptidases degradation. It has major antimicrobial activity against both Pseudomonas aeruginosa and Escherichia coli (45 μM). Neither molecule is toxic to human erythrocytes and both present minor toxicity toward Vero cells at a concentration of 1000 μM. As the first description of TKRPs with antimicrobial activity in T. infestans, this work contributes to the wider comprehension of the insects’ physiology and describes pharmacological relevant molecules.

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Sarconesin II, a New Antimicrobial Peptide Isolated from Sarconesiopsis magellanica Excretions and Secretions

Cited by 23 publications

References 134 publications

Mygalin: An Acylpolyamine With Bactericidal Activity

Mygalin: An Acylpolyamine With Bactericidal Activity

Characterising four Sarconesiopsis magellanica (Diptera: Calliphoridae) larval fat body-derived antimicrobial peptides

Two Tachykinin-Related Peptides with Antimicrobial Activity Isolated from Triatoma infestans Hemolymph

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