Peptaibols as a model for the insertions of chemical modifications

Das, Sanjit; Salah, Khoubaib Ben Haj; Djibo, Mahamadou; Inguimbert, Nicolas

doi:10.1016/j.abb.2018.09.016

Cited by 17 publications

(24 citation statements)

References 142 publications

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“…[1,2] In particular, the field of peptide-based foldamers has gained considerable interest in medicinal chemistry to circumvent some of the issues of short peptides by increasing their conformational stability and their stability towards proteolysis. [3,4] This feature makes peptidomimetic foldamer chemistry an important resource for the design of cell penetrating peptides (CPP), [5][6][7][8][9] antimicrobial peptides (AMP) [10][11][12] and inhibitors of protein-protein interactions (PPI). [13,14] Among the different types of foldamers, those constituted by several units of α-aminoisobutyric acid (Aib) have been widely investigated for their ability to form stable 3 10 -helices [15,16] and their similitude with peptaibols, a natural type of AMP.…”

Section: Introductionmentioning

confidence: 99%

“…In particular, the field of peptide‐based foldamers has gained considerable interest in medicinal chemistry to circumvent some of the issues of short peptides by increasing their conformational stability and their stability towards proteolysis [3,4] . This feature makes peptidomimetic foldamer chemistry an important resource for the design of cell penetrating peptides (CPP), [5–9] antimicrobial peptides (AMP) [10–12] and inhibitors of protein‐protein interactions (PPI) [13,14] …”

Section: Introductionmentioning

confidence: 99%

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Introducing the Chiral Constrained α‐Trifluoromethylalanine in Aib Foldamers to Control, Quantify and Assign the Helical Screw‐Sense**

Bodero

Guitot

Lensen

et al. 2022

Chemistry A European J

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Oligomers of α-aminoisobutyric acid (Aib) are achiral peptides that adopt 3 10 helical structures with equal population of left-and right-handed conformers. The screwsense preference of the helical chain may be controlled by a single chiral residue located at one terminus. 1 H and 19 F NMR, X-ray crystallography and circular dichroism studies on new Aib oligomers show that the incorporation of a chiral quaternary α-trifluoromethylalanine at their N-terminus induces a reversal of the screw-sense preference of the 3 10 -helix compared to that of a non-fluorinated analogue having an lα-methyl valine residue. This work demonstrates that, among the many particular properties of introducing a trifluoromethyl group into foldamers, its stereo-electronic properties are of major interest to control the helical screw sense. Its use as an easy-to-handle 19 F NMR probe to reliably determine both the magnitude of the screw-sense preference and its sign assignment is also of remarkable interest.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Introducing the Chiral Constrained α‐Trifluoromethylalanine in Aib Foldamers to Control, Quantify and Assign the Helical Screw‐Sense**

Bodero

Guitot

Lensen

et al. 2022

Chemistry A European J

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“…The images of all the samples treated with the prototype showed dehydrated hyphae with granules and an evident damage to the fungus wall. The action mechanism of P aib consists in the formation of permanent transmembrane pores due to their amphipathic nature, this causes the escape of cytoplasmic material and eventual cell death [11,14,32]. The endoplasmic material that exits through the pores accumulates on the surface of the hyphae, generating granulated surfaces as observed in hyphae treated with P aib .…”

Section: Resultsmentioning

confidence: 99%

“…The bioactivity of P aib against parasites, viruses, bacteria and pathogenic fungi has previously been reported (Das et al, 2018; Keswani et al, 2019; ; You et al, 2017). In addition, its bioactivity has been proved in therapies against cancer, Alzheimer, and some human and animal diseases thanks to their antifungal, antitrypanosomal and antihelmintic activity [11,13–15,20,21]. The activity of P aib has already been tested in vitro against some plant pathogens, such as Fusarium oxysporum, Botrytis cinerea, Rhizoctonia solani, Bipolaris sorokiniana, Colletotrichum lagenarium, Aspergillus niger, Sclerotium cepivorum, Mucor ramannianus, Moniliophthora perniciosa and Pseudomonas syringae pv.…”

Section: Introductionmentioning

confidence: 99%

Peptaibol Production and Characterization from Trichoderma asperellum and their Action as Biofungicide

Alfaro-Vargas¹,

Bastos-Salas

Muñoz-Arrieta³

et al. 2022

Preprint

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Peptaibols (Paib), are a class of biologically active peptides isolated from soil, fungi and molds, which have interesting properties as antimicrobial agents. Paib production was optimized in flasks by adding sucrose as a carbon source, Aib as an additive amino acid, and F. oxysporum cell debris as an elicitor. Paib were purified, sequenced and identified by HPLC coupled to mass spectrometry. Af-terward, a Paib prototype was prepared with the extracts obtained from the optimized fermenta-tions. The biological activity of these prototypes was evaluated using in vitro and in vivo methods. The prototype inhibited the growth of specific plant pathogens, and it showed inhibition rates similar to those from commercially available fungicides. Growth inhibition rates were 92.2, 74.2, 58.4 and 36.2 % against Colletotrichum gloeosporioides, Botrytis cinerea, Alternaria alternata and Fusarium oxysporum, respectively. Furthermore, the antifungal activity was tested in tomatoes inoculated with A. alternata, the incidence of the disease in tomatoes treated with the prototype was 0%, while the untreated fruit showed a 92.5% of infection. Scanning electron microscopy images showed structural differences between fungi treated with or without Paib. The most visual altera-tions were sunk and shriveled morphology in spores, while the hyphae appeared to be fractured, rough, and dehydrated.

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“…The main characteristic of this type of AMP is the presence of non-proteinogenic amino acids which are not encoded by DNA, such as α-aminobutyric acid (Aib) and isovaline (Iva). This class of amino acids is often used in peptides of pharmacological interest since they are not recognized by hydrolytic enzymes, improving their biodegradability and increasing their bioavailability [7,8]. One of the most unique AMPs in this family is Peptaibolin because it is the smallest in the peptaibol family but at the same time, it has a three-dimensional structure comparable to the larger peptaibols.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of Peptaibolin, an Antimicrobial Peptide

Ribeiro

Felgueiras

Costa

et al. 2020

The 1st International Electronic Conference on Pharmaceutics

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To tackle one of the biggest global health problems, the resistance of microorganisms to antibiotics, a collective effort in the search for more effective agents against bacteria was required. Peptides with antimicrobial activity have been raising much attention as a promising alternative for antibiotics. Peptaibols, for instance, are a family of antimicrobial peptides (AMPs) with great biomedical potential, in which the Peptaibolin can be highlighted. This peptide has gained relevance due to its small amino acids content, only four, and its acetyl group and a phenylalaninol residue (Phol) at the N-terminal and C-terminal, respectively. Here, we report the synthesis of Peptaibolin through Solid Phase Peptide Synthesis assisted by Microwave heating (MW-SPPS) in a pre-loaded Phe-Wang resin. Starting from a loading of 0.51 mmol/g, two syntheses were made, using two different combinations of coupling reagents. The best option was DIC/Oxima, achieving a yield of 50.0%. Proton Nuclear Magnetic Resonance (1H-NMR) studies confirmed the peptide structure, while High Performance Liquid Chromatography (HPLC) verified the peptide purity. The peptide solubility was examined against several combinations of solvents. Peptaibolin was not soluble in water, only in organic solvents or in the combination of both. Antimicrobial testing was conducted using Staphylococcus aureus, Staphylococcus epidermidis, Escherichia coli, and Pseudomonas aeruginosa. Minimum inhibitory concentration studies demonstrated the resistance of bacteria to the peptide action and the peptide instability in bacterial growth conditions.

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Peptaibols as a model for the insertions of chemical modifications

Cited by 17 publications

References 142 publications

Introducing the Chiral Constrained α‐Trifluoromethylalanine in Aib Foldamers to Control, Quantify and Assign the Helical Screw‐Sense**

Introducing the Chiral Constrained α‐Trifluoromethylalanine in Aib Foldamers to Control, Quantify and Assign the Helical Screw‐Sense**

Peptaibol Production and Characterization from Trichoderma asperellum and their Action as Biofungicide

Synthesis of Peptaibolin, an Antimicrobial Peptide

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