A potent antibacterial activity of new short d-enantiomeric lipopeptide against multi drug resistant bacteria

Lee, Jae-Ho; Kim, Shanghyeon; Sim, Ji-Yeong; Lee, Daeun; Kim, Ha Hyung; Hwang, Jae Sam; Lee, Dong Gun; Park, Chul–Seung; Kim, Jae Il

doi:10.1016/j.bbamem.2018.10.014

Cited by 23 publications

(11 citation statements)

References 37 publications

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“…The resulting cyclic lipopeptides with a D-amino acid were as active as their L-counterparts and, interestingly, they were not hemolytic at concentrations 10- to 80-fold higher than their MIC values. Other studies have also shown that the combination of D-amino acids and a lipidic chain in a peptide constitutes an effective strategy to obtain sequences with improved biological activity [ 29 , 42 , 43 , 44 , 45 ].…”

Section: Introductionmentioning

confidence: 99%

D-Amino Acid-Containing Lipopeptides Derived from the Lead Peptide BP100 with Activity against Plant Pathogens

Oliveras

Moll

Riesco-Llach

et al. 2021

IJMS

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From a previous collection of lipopeptides derived from BP100, we selected 18 sequences in order to improve their biological profile. In particular, analogues containing a D-amino acid at position 4 were designed, prepared, and tested against plant pathogenic bacteria and fungi. The biological activity of these sequences was compared with that of the corresponding parent lipopeptides with all L-amino acids. In addition, the influence of the length of the hydrophobic chain on the biological activity was evaluated. Interestingly, the incorporation of a D-amino acid into lipopeptides bearing a butanoyl or a hexanoyl chain led to less hemolytic sequences and, in general, that were as active or more active than the corresponding all L-lipopeptides. The best lipopeptides were BP475 and BP485, both incorporating a D-Phe at position 4 and a butanoyl group, with MIC values between 0.8 and 6.2 µM, low hemolysis (0 and 24% at 250 µM, respectively), and low phytotoxicity. Characterization by NMR of the secondary structure of BP475 revealed that the D-Phe at position 4 disrupts the α-helix and that residues 6 to 10 are able to fold in an α-helix. This secondary structure would be responsible for the high antimicrobial activity and low hemolysis of this lipopeptide.

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Section: Introductionmentioning

confidence: 99%

D-Amino Acid-Containing Lipopeptides Derived from the Lead Peptide BP100 with Activity against Plant Pathogens

Oliveras

Moll

Riesco-Llach

et al. 2021

IJMS

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“…Bacteria are single celled, fast reproducing microorganisms that have the ability to adapt quickly to the changes in their environment. Antibiotics, on the other hand, are very clinically important drugs which are used in the treatment of infectious diseases caused by microorganisms which prevent the growth of bacteria [1]. However, new antibiotic discoveries have recently slowed down considerably, while the incidence of multiple antibiotic-resistant microorganisms has increased dramatically and a future in which antibiotics have lost their influence has begun to appear soon [2].…”

Section: Introductionmentioning

confidence: 99%

Moleküler Docking Yöntemi ile Bazı Azo Bileşiklerinin Potansiyel Antibakteriyel Özelliklerinin İncelenmesi

Atay

Tilki

Dede

2019

Süleyman Demirel Üniversitesi Fen Edebiyat Fakültesi Fen Dergisi

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In this study, molecular docking studies were applied to three azo dyes, 2- [(3,5diamino-1H-pyrazol-4-yl)diazenyl]-5-nitrobenzoic acid (A), 2- [(3,5-dimethyl-1H-pyrazol-4yl)diazenyl]-5-nitrobenzoic acid (B) and 2-[(5-amino-3-methyl-1H-pyrazol-4-yl)diazenyl]-5nitrobenzoic acid (C), which synthesized in our previous studies, to investigate their potential antibacterial properties. Modelling was performed on SwissDock web server using EADock DSS algorithm. Docking simulations of ligands (A, B and C) were performed into the E. coli betaketoacyl-acyl carrier protein synthase III (KAS III) active site to determine the probable binding conformations and inhibitory effects. Docking results were also compared with triclosan used as a commercial antibacterial agent and it was found that compound B had the best antibacterial property.

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“…However, the conjugation of acyl chains to the peptide containing d-enantiomers improved the antibacterial activity better than the parent peptide, and in addition, resulted in better stability against proteases. Another study conducted by Lee et al on peptide CopW demonstrated that exchanging all l-amino acids for d-amino acids increased the antibacterial activity against some bacterial strains [65]. The antibacterial activity was further improved when acyl chains were conjugated to the N-terminus.…”

Section: Combining Lipidation With Other Methods To Increase Biocompatibility Stability Activity and Specificitymentioning

confidence: 98%

Lipidation of Antimicrobial Peptides as a Design Strategy for Future Alternatives to Antibiotics

Rounds¹,

Straus²

2020

IJMS

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Multi-drug-resistant bacteria are becoming more prevalent, and treating these bacteria is becoming a global concern. One alternative approach to combat bacterial resistance is to use antimicrobial (AMPs) or host-defense peptides (HDPs) because they possess broad-spectrum activity, function in a variety of ways, and lead to minimal resistance. However, the therapeutic efficacy of HDPs is limited by a number of factors, including systemic toxicity, rapid degradation, and low bioavailability. One approach to circumvent these issues is to use lipidation, i.e., the attachment of one or more fatty acid chains to the amine groups of the N-terminus or a lysine residue of an HDP. In this review, we examined lipidated analogs of 66 different HDPs reported in the literature to determine: (i) whether there is a link between acyl chain length and antibacterial activity; (ii) whether the charge and (iii) the hydrophobicity of the HDP play a role; and (iv) whether acyl chain length and toxicity are related. Overall, the analysis suggests that lipidated HDPs with improved activity over the nonlipidated counterpart had acyl chain lengths of 8–12 carbons. Moreover, active lipidated peptides attached to short HDPs tended to have longer acyl chain lengths. Neither the charge of the parent HDP nor the percent hydrophobicity of the peptide had an apparent significant impact on the antibacterial activity. Finally, the relationship between acyl chain length and toxicity was difficult to determine due to the fact that toxicity is quantified in different ways. The impact of these trends, as well as combined strategies such as the incorporation of d- and non-natural amino acids or alternative approaches, will be discussed in light of how lipidation may play a role in the future development of antimicrobial peptide-based alternatives to current therapeutics.

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A potent antibacterial activity of new short d-enantiomeric lipopeptide against multi drug resistant bacteria

Cited by 23 publications

References 37 publications

D-Amino Acid-Containing Lipopeptides Derived from the Lead Peptide BP100 with Activity against Plant Pathogens

D-Amino Acid-Containing Lipopeptides Derived from the Lead Peptide BP100 with Activity against Plant Pathogens

Moleküler Docking Yöntemi ile Bazı Azo Bileşiklerinin Potansiyel Antibakteriyel Özelliklerinin İncelenmesi

Lipidation of Antimicrobial Peptides as a Design Strategy for Future Alternatives to Antibiotics

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