Peptaibols: Diversity, bioactivity, and biosynthesis

Hou, Xuewen; Sun, Runyuan; Feng, Yue; Zhang, Runfang; Zhu, Tianjiao; Che, Qian; Zhang, Guojian; Li, Dehai

doi:10.1016/j.engmic.2022.100026

Cited by 22 publications

(35 citation statements)

References 116 publications

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“…32 While the peptaibiotics encompass Nacylated linear peptides of between five and 22 amino acid residues with a high occurrence of Aib and other nonproteinogenic amino acids, the peptaibols are characterized by the additional presence of a C-terminal amino alcohol and represent the largest subclass of peptaibiotics. 32,33 Peptaibols that contain a lipophilic N-acyl moiety (typically octanoyl to pentadecenoyl chains) are further classified as lipopeptaibols, 34 with 16 members of this class having been isolated from insect pathogens or soil/sediment-inhabiting fungal species congeneric with our Tolypocladium sp. isolate (order Hypocreales, family Ophiocordycipitaceae): LP237-F5, LP237-F7, LP237-F8, 17,18 the dakwaabakains A−E, 16 and the tolypocladamides A−H.…”

Section: ■ Results and Discussionmentioning

confidence: 84%

Tolypocaibols: Antibacterial Lipopeptaibols from a Tolypocladium sp. Endophyte of the Marine Macroalga Spongomorpha arcta

et al. 2023

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Two new lipopeptaibols, tolypocaibols A (1) and B (2), and the mixed NRPS-polyketide-shikimate natural product maximiscin [(P/M)-3)] were isolated from a Tolypocladium sp. fungal endophyte of the marine alga Spongomorpha arcta. Analysis of NMR and mass spectrometry data revealed the amino acid sequences of the lipopeptaibols, which both comprise 11 residues with a valinol C-terminus and a decanoyl acyl chain at the N-terminus. The configuration of the amino acids was determined by Marfey’s analysis. Tolypocaibols A (1) and B (2) showed moderate, selective inhibition against Gram-positive and acid-fast bacterial strains, while maximiscin [(P/M)-3)] showed moderate, broad-spectrum antibiotic activity.

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Section: ■ Results and Discussionmentioning

confidence: 84%

Tolypocaibols: Antibacterial Lipopeptaibols from a Tolypocladium sp. Endophyte of the Marine Macroalga Spongomorpha arcta

et al. 2023

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“…Their three-dimensional structures consist of α -helix and β -bend patterns [ 52 ]. They are classified based on sequence length as “long” (18−20 residues), “short” (11−16 amino acids) ( Figure 4 ), and founded on modification types on the terminal groups, “lipo” peptaibols (i.e., N -terminal acylated by decanoic) [ 53 ]. Different mechanisms have been proposed to describe their action.…”

Section: Antimicrobial Peptides’ Natural Sourcementioning

confidence: 99%

An Overview of the Potentialities of Antimicrobial Peptides Derived from Natural Sources

2022

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Antimicrobial peptides (AMPs) are constituents of the innate immune system in every kind of living organism. They can act by disrupting the microbial membrane or without affecting membrane stability. Interest in these small peptides stems from the fear of antibiotics and the emergence of microorganisms resistant to antibiotics. Through membrane or metabolic disruption, they defend an organism against invading bacteria, viruses, protozoa, and fungi. High efficacy and specificity, low drug interaction and toxicity, thermostability, solubility in water, and biological diversity suggest their applications in food, medicine, agriculture, animal husbandry, and aquaculture. Nanocarriers can be used to protect, deliver, and improve their bioavailability effectiveness. High cost of production could limit their use. This review summarizes the natural sources, structures, modes of action, and applications of microbial peptides in the food and pharmaceutical industries. Any restrictions on AMPs’ large-scale production are also taken into consideration.

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“…Indeed, some medium-length peptaibols were reported to display antitumor activity. 9 The medium-length heptaibin showed also selectivity towards negative-charged liposomes, a simple model for cancer cell membranes, over zwitterionic ones that mimic healthy cells/erythrocytes. 7 Further studies on such a promising class of natural bioactive peptides are hampered by a lack of effective synthetic procedures, because the presence of several Aib residues in a row often results in unsuccessful couplings and the production of deleted sequences.…”

Section: Introductionmentioning

confidence: 99%

“…Their wavering between mechanisms suggests a kind of selective bioactivity, which is promising for their application as antimicrobial or antitumor agents. Indeed, some medium-length peptaibols were reported to display antitumor activity [9]. The medium-length heptaibin showed also selectivity towards negative-charged liposomes, a simple model for cancer cell membranes, over zwitterionic ones that mimic healthy cells/erythrocytes [7].…”

Section: Introductionmentioning

confidence: 99%

Total synthesis of the natural, medium‐length, peptaibol pentadecaibin and study of the chemical features responsible for its membrane activity

Morbiato

Haneen

Formaggio

et al. 2023

Journal of Peptide Science

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Peptaibols are naturally-occurring, antimicrobial peptides endowed with well-defined helical conformations and resistance to proteolysis. Both features stem from the presence in their sequence of several, C α -tetrasubstituted, α-aminoisobutyric acid (Aib) residues. Peptaibols interact with biological membranes, usually causing their leakage. All of the peptaibolmembrane interaction mechanisms proposed so far begin with peptide aggregation or accumulation. The long-length alamethicin, the most studied peptaibol, acts by forming pores in the membranes. Conversely, the carpet mechanism has been claimed for shortlength peptaibols, such as trichogin. The mechanism of medium-length peptaibols is far less studied and this is partly due to the difficulties of their synthesis. They are believed to perturb membrane permeability in different ways, depending on the membrane properties. The present work focuses on pentadecaibin, a recently discovered, medium-length peptaibol. In contrast to the majority of its family members, its sequence does not comprise hydroxyprolines or prolines, and its helix is not kinked. A reliable and effective synthesis procedure is described that allowed us to produce also two shorter analogs. By a combination of techniques, we were able to establish a 3D-structure-activity relationship. In particular, the membrane activity of pentadecaibin heavily depends on the presence of three consecutive Aib residues that are responsible for the clear, albeit modest, amphiphilic character of its helix. The shortest analog, devoid of two of these three Aib residues, preserves a well-defined helical conformation, but not its amphipathicity, and loses almost completely the ability to cause membrane leakage. We conclude that pentadecaibin amphiphilicity is probably needed for the peptide ability to perturb model membranes.

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Peptaibols: Diversity, bioactivity, and biosynthesis

Cited by 22 publications

References 116 publications

Tolypocaibols: Antibacterial Lipopeptaibols from a Tolypocladium sp. Endophyte of the Marine Macroalga Spongomorpha arcta

Tolypocaibols: Antibacterial Lipopeptaibols from a Tolypocladium sp. Endophyte of the Marine Macroalga Spongomorpha arcta

An Overview of the Potentialities of Antimicrobial Peptides Derived from Natural Sources

Total synthesis of the natural, medium‐length, peptaibol pentadecaibin and study of the chemical features responsible for its membrane activity

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