Tryptophan- and arginine-rich antimicrobial peptides: Anti-infectives with great potential

Straus, Suzana K.

doi:10.1016/j.bbamem.2023.184260

Cited by 8 publications

(7 citation statements)

References 90 publications

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“…The suggested alteration for this peptide was based on the relationship between tryptophan and antimicrobial activity. This amino acid plays a crucial role in proteins and peptides interacting with membranes. , In addition, several studies show a relationship between this amino acid and increased antimicrobial activity without increasing hemolytic activity. − …”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

“…This amino acid is crucial for proteins and peptides to interact with membranes. 13,14 This simple exchange vastly increased the activity against Gram-negative bacteria, highlighting the importance of the structure−activity relationship.…”

Section: ■ Introductionmentioning

confidence: 98%

“…This amino acid plays a crucial role in proteins and peptides interacting with membranes. 13,14 In addition, several studies show a relationship between this amino acid and increased antimicrobial activity without increasing hemolytic activity. 14−17 The initial assessment of the newly synthesized peptide was its comparison with its previously evaluated analogue for antibacterial activity and cytotoxicity.…”

Section: ■ Introductionmentioning

confidence: 99%

“…An image providing the location of p-BthTX-I in the protein Bothropstoxin-I is provided in Figure , as well as the alignment between the previously studied peptide and the new analogue p-BthW. This amino acid is crucial for proteins and peptides to interact with membranes. , This simple exchange vastly increased the activity against Gram-negative bacteria, highlighting the importance of the structure–activity relationship.…”

Section: Introductionmentioning

confidence: 99%

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Optimizing Bothropstoxin-I-Derived Peptides: Exploring the Antibacterial Potential of p-BthW

Marinho Righetto,

Alves Santos-Filho,

Oliveira Catarin Nunes

et al. 2024

ACS Omega

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Antimicrobial peptides are an emerging class of antibiotics that present a series of advantageous characteristics such as wide structural variety, broad spectrum of activity, and low propensity to select for resistance. They are found in all classes of life as defense molecules. A group of peptides derived from the protein Bothropstoxin-I has been previously studied as an alternative treatment against multi-drug-resistant bacteria. The peptide p-BthTX-I (sequence: KKYRYHLKPFCKK) and its homodimer, linked by disulfide oxidation through the residues of Cys11 and the serum degradation product [sequence: (KKYRYHLKPFC)2], were evaluated and showed similar antimicrobial activity. In this study, we synthesized an analogue of p-BthTX-I that uses the strategy of Fmoc-Lys(Fmoc)-OH in the C-terminal region for dimerization and tryptophan for all aromatic amino acids to provide better membrane interactions. This analogue, named p-BthW, displayed potent antibacterial activity at lower concentrations and maintained the same hemolytic levels as the original molecule. Our assessment revealed that p-BthW has a quick in vitro bactericidal action and prolonged post-antibiotic effect, comparable to the action of polymyxin B. The mode of action of p-BthW seems to rely not only on membrane depolarization but also on necrosis-like effects, especially in Gram-negative bacteria. Overall, the remarkable results regarding the propensity to develop resistance reaffirmed the great potential of the developed molecule.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 98%

Section: ■ Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Optimizing Bothropstoxin-I-Derived Peptides: Exploring the Antibacterial Potential of p-BthW

Marinho Righetto,

Alves Santos-Filho,

Oliveira Catarin Nunes

et al. 2024

ACS Omega

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Current scenario of indole hybrids with antibacterial potential against Acinetobacter baumannii pathogens: A mini‐review

Chen

2024

Archiv der Pharmazie

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Acinetobacter baumannii with the capability to “escape” almost all currently available antibacterials is eroding the safety of basic medical interventions and is an increasing cause of mortality globally, prompting a substantial requirement for new classes of antibacterial agents. Indoles participate in the regulation of persistent bacterial formation, biofilm formation, plasmid stability, and drug resistance. In particular, indole hybrids demonstrated promising antibacterial activity against both drug‐sensitive and drug‐resistant A. baumannii pathogens, representing a fertile source for the discovery of novel therapeutic agents for clinical deployment in controlling A. baumannii infections. This mini‐review outlines the current innovations of indole hybrids with antibacterial activity against A. baumannii pathogens, covering articles published from 2020 to the present, to open new avenues for exploring novel anti‐A. baumannii candidates.

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Chemically Peptide Synthesis and Role of Arginine and Lysine in the Antimicrobial and Antiviral Activity of Synthetic Peptides: A Comprehensive Review

Sunar,

Acar,

Sahin

2024

Peptide Science

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This review examines the potential applications of peptides in biotechnology, medicine, and pharmacy, while highlighting the important antibacterial and antiviral properties of peptides. Peptides and chemical peptide synthesis have become a field of study that is gaining great momentum today. Some of the main reasons for this are high specificity, biodegradability and versatility of peptides. Peptides also have some specific properties that make them attractive for pharmaceutical development. As a case study, it can be used to create peptides that can be used to replace or fix damaged proteins in the body by mimicking the action of naturally occurring proteins. Delivering drugs or other therapeutic agents to specific cells or tissues is another method that can help increase the effectiveness of treatment and reduce unwanted effects. Various types of antimicrobial peptides (AMPs), such as defensins and cathelicidins, and their anti‐infective properties are also discussed. Finally, peptides (melittin, lactoferricin, etc.) can be used to trigger an immune response against certain infections, such as COVID‐19 and Zika virus, by acting as vaccines. In our study, a comprehensive review was made on antiviral and AMPs, and especially peptides containing arginine and lysine were mentioned. The properties of these peptides, examples of these peptides and their developments in the pharmaceutical field are emphasized.

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Tryptophan- and arginine-rich antimicrobial peptides: Anti-infectives with great potential

Cited by 8 publications

References 90 publications

Optimizing Bothropstoxin-I-Derived Peptides: Exploring the Antibacterial Potential of p-BthW

Optimizing Bothropstoxin-I-Derived Peptides: Exploring the Antibacterial Potential of p-BthW

Current scenario of indole hybrids with antibacterial potential against Acinetobacter baumannii pathogens: A mini‐review

Chemically Peptide Synthesis and Role of Arginine and Lysine in the Antimicrobial and Antiviral Activity of Synthetic Peptides: A Comprehensive Review

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