Buforin I an alternative to conventional antibiotics: Evaluation of the antimicrobial properties, stability, and safety

Roshanak, Sahar; Shahidi, Fakhri; Yazdi, Farideh Tabatabaei; Javadmanesh, Ali; Movaffagh, Jebraeil

doi:10.1016/j.micpath.2021.105301

Cited by 12 publications

(13 citation statements)

References 42 publications

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“…In addition, histone H2A has been shown to be synthesized in excess, in amounts required for DNA packaging, and accumulates in cytoplasmic granules in gastric gland cells. Upon secretion into the gastric lumen, it is processed by pepsin C isozymes to yield buforin I [ 46 , 47 ], and proteasomal degradation of histone proteins increases after oxidative damage [ 48 ]. The peptide buforin II (TRSSRAGLQFPVGRVHRLLRK) derived from buforin I demonstrates a potent antimicrobial activity, killing the bacteria without cell lysis and having affinity with nucleic acids, apparently inhibiting the cellular function by binding to DNA and/or RNA [ 49 ].…”

Section: Discussionmentioning

confidence: 99%

Revealing Natural Intracellular Peptides in Gills of Seahorse Hippocampus reidi

et al. 2023

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The seahorse is a marine teleost fish member of the Syngnathidae family that displays a complex variety of morphological and reproductive behavior innovations and has been recognized for its medicinal importance. In the Brazilian ichthyofauna, the seahorse Hippocampus reidi is among the three fish species most used by the population in traditional medicine. In this study, a protocol was performed based on fast heat inactivation of proteases plus liquid chromatography coupled to mass spectrometry to identify native peptides in gills of seahorse H. reidi. The MS/MS spectra obtained from gills allowed the identification of 1080 peptides, of which 1013 peptides were present in all samples and 67 peptide sequences were identified in an additional LC-MS/MS run from an alkylated and reduced pool of samples. The majority of peptides were fragments of the internal region of the amino acid sequence of the precursor proteins (67%), and N- and C-terminal represented 18% and 15%, respectively. Many peptide sequences presented ribosomal proteins, histones and hemoglobin as precursor proteins. In addition, peptide fragments from moronecidin-like protein, described with antimicrobial activity, were found in all gill samples of H. reidi. The identified sequences may reveal new bioactive peptides.

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Section: Discussionmentioning

confidence: 99%

Revealing Natural Intracellular Peptides in Gills of Seahorse Hippocampus reidi

et al. 2023

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“…In our previous study, the antimicrobial effect of native buforin I was assessed against same microbial strains (MIC for L. monocytogenes, S. aureus, A. niger, C. albicans, P. aeruginosa, S. aureus (MRSA), E. coli O157:H7, S. Typhi, K. pneumonia and C. perfringens was 4, 10, 10, 10, 12, 14, 14, 14, 6, and 16 (µg/mL) of buforin I, respectively) 7 . As the difference in MICs value for the buforin I and recombinant buforin I for all microbial strains were less than two-fold, the sensitivity levels were considered equal, therefore, there is no significant difference between the antimicrobial effect of recombinant buforin I and synthetic buforin I.…”

Section: Discussionmentioning

confidence: 99%

“…A purified and characterized buforin I from an Asian toad's stomach demonstrated strong antimicrobial activity against Gram-positive and Gram-negative bacteria and fungal strains 6 . Our previous studies showed that buforin I has high and board spectrum antimicrobial 6 , 7 , biofilm formation and biofilm radiation activities with high therapeutic index. Buforin I's safety is confirmed by the lack of cell cytotoxicity and hemolytic activity 7 .…”

Section: Introductionmentioning

confidence: 99%

“…Our previous studies showed that buforin I has high and board spectrum antimicrobial 6 , 7 , biofilm formation and biofilm radiation activities with high therapeutic index. Buforin I's safety is confirmed by the lack of cell cytotoxicity and hemolytic activity 7 . Accordingly, Cationic antimicrobial peptides like buforin I, are being developed as a promising class of antimicrobial substances 2 .…”

Section: Introductionmentioning

confidence: 99%

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Effects of adding poly-histidine tag on stability, antimicrobial activity and safety of recombinant buforin I expressed in periplasmic space of Escherichia coli

Roshanak

Yarabbi

Shahidi

et al. 2023

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The lack of cost-effective methods for producing antimicrobial peptides has made it impossible to use their high potential as a new and powerful class of antimicrobial agents. In recent years, extensive research has been conducted to decrease the cost of recombinant proteins production through microorganisms, transgenic animals, and plants. Well-known genetic and physiological characteristics, short-term proliferation, and ease of manipulation make E. coli expression system a valuable host for recombinant proteins production. Expression in periplasmic space is recommended to reduce the inherently destructive behavior of antimicrobial peptides against the expressing microorganism and to decline susceptibility to proteolytic degradation. In this study, a pET-based expression system was used to express buforin I at E. coli periplasmic space, and its antimicrobial, hemolytic, and cell toxicity activities as well as structural stability were evaluated. The hemolysis activity and cytotoxicity of His-tagged buforin I were negligible and its antimicrobial activity did not show a significant difference compared to synthetic buforin I. In addition, in silico investigating of stability of native and His-tagged buforin I showed that RMSF, RMSD and Rg curves had followed a similar trend during 150 ns simulation. Furthermore, evaluating the modelled structures, FTIR and X-ray methods of both peptides indicated an insignificant structural difference. It was concluded that the recombinant buforin I could be a viable alternative to some currently used antibiotics by successfully expressing it in the pET-based expression system.

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“…The residues with the most interactions with this phospholipid are ARG6 and ARG9. Thus, the residue that contributes the most to the formation of intermolecular interactions is arginine, which has a greater affinity to bind to the phosphate groups in the bacterial membrane due to the greater number of hydrogen bonds and exactly five donor stabilizer groups [43]. In fact, ARG attracts water molecules in the polar head of the membrane in addition to being electrostatically attracted by phosphate [44], which may be related to the C=O dehydration discussed above.…”

Section: Interaction Between Peptides and Membranesmentioning

confidence: 99%

Integrating In Vitro and In Silico Analysis of a Cationic Antimicrobial Peptide Interaction with Model Membranes of Colistin-Resistant Pseudomonas aeruginosa Strains

et al. 2022

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Bacterial antibiotic resistance is a serious global public health concern. Infections caused by colistin-resistant Pseudomonas aeruginosa (CRPa) strains represent a serious threat due to their considerable morbidity and mortality rates, since most of the current empirical antibiotic therapies are ineffective against these strains. Accordingly, cationic antimicrobial peptides (CAMPs) have emerged as promising alternatives to control resistant bacteria. In this study, the interaction of a CAMP derived from cecropin D-like (∆M2) with model membranes mimicking bacterial biomembranes of wild-type (WTPa) strains of P. aeruginosa and CRPa was evaluated through in vitro and in silico approaches. In vitro interaction was determined by infrared spectroscopy, whereas in silico molecular dynamics was performed to predict specific interactions between amino acids of ∆M2 and lipids of model membrane systems. Experimental analysis showed this peptide interacted with the lipids of bacterial-like model membranes of WTPa and CRPa. In both cases, an increase in the concentration of peptides induced an increase in the phase transition temperature of the lipid systems. On the other hand, the peptides in solution underwent a transition from a random to a helical secondary structure after interacting with the membranes mostly favored in the CRPa system. The α-helix structure percentage for ΔM2 interacting with WTPa and CRPa lipid systems was 6.4 and 33.2%, respectively. Finally, molecular dynamics showed ∆M2 to have the most affinities toward the phospholipids palmitoyl-oleyl-phosphatidylglycerol (POPG) and palmitoyl-oleoyl-phosphatidylethanolamine (POPE) that mimic membranes of WTPa and CRPa, respectively. This work provides clues for elucidating the membrane-associated mechanism of action of ∆M2 against colistin-susceptible and -resistant strains of Pseudomonas aeruginosa.

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Buforin I an alternative to conventional antibiotics: Evaluation of the antimicrobial properties, stability, and safety

Cited by 12 publications

References 42 publications

Revealing Natural Intracellular Peptides in Gills of Seahorse Hippocampus reidi

Revealing Natural Intracellular Peptides in Gills of Seahorse Hippocampus reidi

Effects of adding poly-histidine tag on stability, antimicrobial activity and safety of recombinant buforin I expressed in periplasmic space of Escherichia coli

Integrating In Vitro and In Silico Analysis of a Cationic Antimicrobial Peptide Interaction with Model Membranes of Colistin-Resistant Pseudomonas aeruginosa Strains

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