Short hybrid peptides incorporating β- and γ-amino acids as antimicrobial agents

Wani, Naiem Ahmad; Singh, Gurpreet; Shankar, Sudha; Sharma, Aakanksha; Katoch, Meenu; Rai, Rajkishor

doi:10.1016/j.peptides.2017.09.016

Cited by 24 publications

(25 citation statements)

References 32 publications

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“…aeruginosa (MTCC 424), and E . coli (MTCC 118) bacteria according to previously reported method . The peptides were dissolved in phosphate‐buffered saline (PBS) with 50% aqueous DMSO at 1 mg/mL with continuous heating until it was dissolved completely.…”

Section: Methodsmentioning

confidence: 99%

“…The hemolytic assay was performed according to the method described in the literature with slight modifications. The hemolytic activity of the peptides was monitored as the amount of hemoglobin released from human erythrocytes due to their lysis.…”

Section: Methodsmentioning

confidence: 99%

“…26 The peptide and proteolytic enzymes (trypsin, reported method. 27 The peptides were dissolved in phosphatebuffered saline (PBS) with 50% aqueous DMSO at 1 mg/mL with continuous heating until it was dissolved completely. The solutions were kept overnight at room temperature.…”

Section: Enzymatic Stability Of Self-assembled Peptidesmentioning

confidence: 99%

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Investigation of α/γ hybrid peptide self‐assembled structures with antimicrobial and antibiofilm properties

Shankar

Singh

Rahim

et al. 2020

Journal of Peptide Science

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The present work describes the synthesis and characterization of α/γ hybrid peptides, Boc‐Phe‐γ4‐Phe‐Val‐OMe, P1; Boc‐Ala‐γ4‐Phe‐Val‐OMe, P2; and Boc‐Leu‐γ4‐Phe‐Val‐OMe, P3 together with the formation of self‐assembled structures formed by these hybrid peptides in dimethyl sulfoxide (DMSO)/water (1:1). The self‐assembled structures were characterized by infrared (IR) spectroscopy, circular dichroism (CD), and scanning electron microscopy (SEM). Further, α/γ hybrid peptide self‐assembled structures were evaluated for antibacterial properties. Among all, the self‐assembled peptide P1 exhibited the antimicrobial activity against Escherichia coli and Klebsiella pneumoniae, while self‐assembled peptide P3 inhibited the biofilms of Salmonella typhimurium and Pseudomonas aeruginosa. In this study, we have shown the significance of self‐assembled structures formed from completely hydrophobic α/γ hybrid peptides in exploring the antibacterial properties together with biofilm inhibition.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Investigation of α/γ hybrid peptide self‐assembled structures with antimicrobial and antibiofilm properties

Shankar

Singh

Rahim

et al. 2020

Journal of Peptide Science

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“…The antimicrobial activities of VIP and its analogues were tested against S. aureus ATCC 25923 and E. coli ATCC 25922 according to the method reported by Wani et al [ 32 ] with slight modification. The final peptide concentrations ranged from 0.5 to 256 μM.…”

Section: Methodsmentioning

confidence: 99%

“…Chemically-synthesized VIP8 and ampicillin were used as the positive control. The minimal inhibition concentration was determined by the method reported by Wani et al [ 32 ].…”

Section: Methodsmentioning

confidence: 99%

Design, Recombinant Fusion Expression and Biological Evaluation of Vasoactive Intestinal Peptide Analogue as Novel Antimicrobial Agent

Guo

Qiao

et al. 2017

Molecules

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Antimicrobial peptides represent an emerging category of therapeutic agents with remarkable structural and functional diversity. Modified vasoactive intestinal peptide (VIP) (VIP analogue 8 with amino acid sequence “FTANYTRLRRQLAVRRYLAAILGRR”) without haemolytic activity and cytotoxicity displayed enhanced antimicrobial activities against Staphylococcus aureus (S. aureus) ATCC 25923 and Escherichia coli (E. coli) ATCC 25922 than parent VIP even in the presence of 180 mM NaCl or 50 mM MgCl2, or in the range of pH 4–10. VIP analogue 8 was expressed as fusion protein thioredoxin (Trx)-VIP8 in E. coli BL21(DE) at a yield of 45.67 mg/L. The minimum inhibitory concentration (MIC) of the recombinant VIP analogue 8 against S. aureus ATCC 25923 and E. coli ATCC 25922 were 2 μM. These findings suggest that VIP analogue 8 is a promising candidate for application as a new and safe antimicrobial agent.

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Non‐canonical amino acid bioincorporation into antimicrobial peptides and its challenges

Enninful,

Kuppusamy,

Tiburu

et al. 2024

Journal of Peptide Science

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The rise of antimicrobial resistance and multi‐drug resistant pathogens has necessitated explorations for novel antibiotic agents as the discovery of conventional antibiotics is becoming economically less viable and technically more challenging for biopharma. Antimicrobial peptides (AMPs) have emerged as a promising alternative because of their particular mode of action, broad spectrum and difficulty that microbes have in becoming resistant to them. The AMPs bacitracin, gramicidin, polymyxins and daptomycin are currently used clinically. However, their susceptibility to proteolytic degradation, toxicity profile, and complexities in large‐scale manufacture have hindered their development. To improve their proteolytic stability, methods such as integrating non‐canonical amino acids (ncAAs) into their peptide sequence have been adopted, which also improves their potency and spectrum of action. The benefits of ncAA incorporation have been made possible by solid‐phase peptide synthesis. However, this method is not always suitable for commercial production of AMPs because of poor yield, scale‐up difficulties, and its non‐‘green’ nature. Bioincorporation of ncAA as a method of integration is an emerging field geared towards tackling the challenges of solid‐phase synthesis as a green, cheaper, and scalable alternative for commercialisation of AMPs. This review focusses on the bioincorporation of ncAAs; some challenges associated with the methods are outlined, and notes are given on how to overcome these challenges. The review focusses particularly on addressing two key challenges: AMP cytotoxicity towards microbial cell factories and the uptake of ncAAs that are unfavourable to them. Overcoming these challenges will draw us closer to a greater yield and an environmentally friendly and sustainable approach to make AMPs more druggable.

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Short hybrid peptides incorporating β- and γ-amino acids as antimicrobial agents

Cited by 24 publications

References 32 publications

Investigation of α/γ hybrid peptide self‐assembled structures with antimicrobial and antibiofilm properties

Investigation of α/γ hybrid peptide self‐assembled structures with antimicrobial and antibiofilm properties

Design, Recombinant Fusion Expression and Biological Evaluation of Vasoactive Intestinal Peptide Analogue as Novel Antimicrobial Agent

Non‐canonical amino acid bioincorporation into antimicrobial peptides and its challenges

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