CD and NMR structural characterization of ceratotoxins, natural peptides with antimicrobial activity

Ragona, Laura; Molinari, Henríette; Zetta, Lucia; Longhi, Renato; Marchini, Daniela; Dallai, Romano; Bernini, L. F.; Lozzi, Luisa; Scarselli, María; Niccolai, Neri

doi:10.1002/(sici)1097-0282(199611)39:5<653::aid-bip4>3.0.co;2-v

Cited by 4 publications

(1 citation statement)

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“…The remarkable feature of AMPs with broad spectrum of activity is a 3D sorting of cationic and hydrophobic amino acid side chains during supramolecular interactions with negatively charged phospholipids distributed on the microbial surface. As revealed by structural studies of AMP’s, performed by NMR, − circular dichroism (CD), − and X-ray studies, − in the presence of membrane models the majority of the studied linear 10–50-peptides undergo conformational conversion to protein-like secondary structures (helical, β-sheet, etc. ), resulting in perturbation of microbial membrane and at least inhibition of microbial growth.…”

Section: Introductionmentioning

confidence: 99%

Bioinspired Amphiphilic Peptide Dendrimers as Specific and Effective Compounds against Drug Resistant Clinical Isolates of E. coli

et al. 2018

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Evolution-derived natural compounds have been inspirational for design of numerous pharmaceuticals, e.g., penicillins and tetracyclines. Herein, we present a bioinspired strategy to design peptide dendrimers for the effective therapy of E. coli infections where the selection of appropriate amino acids and the mode of their assembly are based on the information gained from research on membranolytic natural antimicrobial peptides (AMP's). On the molecular level two opposite effects were explored: the effect of multiple positive charges necessary for membrane disintegration was equilibrated by the anchoring role of tryptophanes. Indeed, a series of Trp-terminated dendrimers exhibited high potency against clinical isolates of antibiotic resistant ESBL E. coli strains, stability in human plasma along with very low hemo-and genotoxicity. Investigation of the underlying antimicrobial mechanism indicated that the dendrimers studied at minimal inhibitory concentration showed weak permeability toward membranes. Solid-state 2D NMR studies revealed their presence on and inside the model membranes. Therefore, their biological properties might be explained by targeting of extra-or intracellular receptors. Our results point to a new approach to design novel branched antimicrobials with high therapeutic index.

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Section: Introductionmentioning

confidence: 99%

Bioinspired Amphiphilic Peptide Dendrimers as Specific and Effective Compounds against Drug Resistant Clinical Isolates of E. coli

et al. 2018

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Amphipathic, α-helical antimicrobial peptides

2000

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Development of Antimicrobial Peptides as Therapeutic Agents

Hodges

Jiang

Whitehurst

et al. 2011

Pharmaceutical Sciences Encyclopedia

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Classical antibiotics work by inhibiting bacterial cell wall synthesis, protein synthesis, DNA (deoxyribonucleic acid) replication, or by modifying metabolism. Bacteria can resist antibiotics as a result of chromosomal changes (mutation or inductive expression of a latent chromosomal gene) or the exchange of genetic material via plasmids and transposons. As this chapter will discuss, antibiotics are rendered inactive by three major mechanisms: (1) antibiotic inactivation by destruction or modification, (2) prevention of access of the antibiotic to the target, and (3) alteration of the target site of the antibiotic. Bacteria have a remarkable ability to overcome each new reagent synthesized as a potential classical antibiotic. Consequently, the current priority is the development of alternative drugs and/or the isolation of native molecules that would allow the consistent and proper control of pathogen‐caused diseases.

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CD and NMR structural characterization of ceratotoxins, natural peptides with antimicrobial activity

Cited by 4 publications

References 35 publications

Bioinspired Amphiphilic Peptide Dendrimers as Specific and Effective Compounds against Drug Resistant Clinical Isolates of E. coli

Bioinspired Amphiphilic Peptide Dendrimers as Specific and Effective Compounds against Drug Resistant Clinical Isolates of E. coli

Amphipathic, α-helical antimicrobial peptides

Development of Antimicrobial Peptides as Therapeutic Agents

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