Antimicrobial activity and self-assembly behavior of antimicrobial peptide chensinin-1b with lipophilic alkyl tails

Dong, Weibing; Liu, Ziang; Sun, Liying; Wang, Cui; Guan, Yue; Mao, Xiaoman; Shang, Dejing

doi:10.1016/j.ejmech.2018.03.025

Cited by 23 publications

(14 citation statements)

References 41 publications

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“…For example, the GL13K peptide (the sequence shown in Table S1) is obtained by replacing three amino acid residues with lysine residues in GL13NH 2 , which is the bacteria-agglutinating prototype derived from the parotid secretory protein. − Such modification makes GL13K a more cationic peptide and thus makes GL13K bactericidal against many types of bacteria such as E. coli . Furthermore, recent studies have shown that self-assembly can enhance the effects of AMPs by achieving more specific and stronger interactions with microbial membranes, − and nanomaterials (such as gold nanodots) serve as a desirable vehicle for the self-assembly of AMPs …”

Section: Resultsmentioning

confidence: 99%

Tetrahedral Framework Nucleic Acids Deliver Antimicrobial Peptides with Improved Effects and Less Susceptibility to Bacterial Degradation

Liu

Sun

et al. 2020

Nano Lett.

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Antimicrobial peptides (AMPs) have been an attractive alternative to traditional antibiotics. However, considerable efforts are needed to further enhance their antimicrobial effects and stability against bacterial degradation. Tetrahedral framework nucleic acids (tFNAs), a new class of three-dimensional nanostructures, have been utilized as a delivery vehicle. In this study, tFNAs were combined for the first time with an antimicrobial peptide GL13K, and the effects of the resultant complexes against Escherichia coli (sensitive to GL13K) and Porphyromonas gingivalis (capable of degrading GL13K) were investigated. tFNA-based delivery enhanced the effects of GL13K against E. coli. The tFNA vehicle both increased bacterial uptake and promoted membrane destabilization. Moreover, it enhanced the effects of GL13K against P. gingivalis by protecting the peptide against degradation in the protease-rich extracellular environment. Therefore, tFNA provides a delivery vehicle for AMPs targeting a broad range of disease.

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Section: Resultsmentioning

confidence: 99%

Tetrahedral Framework Nucleic Acids Deliver Antimicrobial Peptides with Improved Effects and Less Susceptibility to Bacterial Degradation

Liu

Sun

et al. 2020

Nano Lett.

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“…Moreover, these same lipidated helical peptides inserted into the liposomes most effectively, demonstrating that the α-helical structure of a lipopeptide is clearly correlated to the ability to disrupt a bacterial membrane. Furthermore, conjugates with longer acyl chains may lead to a decrease in the activity due to aggregation and self-assembly [38,48,50,58]. Indeed, Sikorska et al showed that the monomeric forms of short arginine-rich HDPs were responsible for the disruption of the bacterial membrane as opposed to aggregated forms [58].…”

Section: Length Of Acyl Chainmentioning

confidence: 99%

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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“…While lipid carriers are a generally cytocompatibile platform that can be readily formulated with various biomolecular cargo [189], tailored chemical modifications and large-scale manufacture can be limited in comparison. However, a major advantage of liposomal-based drug carriers is the ability of membranolytic AMPs to intercalate into the bilayer to effectively turn 'on' their transition to a bioactive α-helical or β-sheet conformation [97,[190][191][192]. This is in addition to the ability of liposomal particles to improve the systemic stability and circulation time of the loaded therapeutic.…”

Section: Peptide-excipient Co-formulationsmentioning

confidence: 99%

Supramolecular Peptide Assemblies as Antimicrobial Scaffolds

2020

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Antimicrobial discovery in the age of antibiotic resistance has demanded the prioritization of non-conventional therapies that act on new targets or employ novel mechanisms. Among these, supramolecular antimicrobial peptide assemblies have emerged as attractive therapeutic platforms, operating as both the bactericidal agent and delivery vector for combinatorial antibiotics. Leveraging their programmable inter- and intra-molecular interactions, peptides can be engineered to form higher ordered monolithic or co-assembled structures, including nano-fibers, -nets, and -tubes, where their unique bifunctionalities often emerge from the supramolecular state. Further advancements have included the formation of macroscopic hydrogels that act as bioresponsive, bactericidal materials. This systematic review covers recent advances in the development of supramolecular antimicrobial peptide technologies and discusses their potential impact on future drug discovery efforts.

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Antimicrobial activity and self-assembly behavior of antimicrobial peptide chensinin-1b with lipophilic alkyl tails

Cited by 23 publications

References 41 publications

Tetrahedral Framework Nucleic Acids Deliver Antimicrobial Peptides with Improved Effects and Less Susceptibility to Bacterial Degradation

Tetrahedral Framework Nucleic Acids Deliver Antimicrobial Peptides with Improved Effects and Less Susceptibility to Bacterial Degradation

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

Supramolecular Peptide Assemblies as Antimicrobial Scaffolds

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