Editorial: Community series in antimicrobial peptides: Molecular design, structure function relationship and biosynthesis optimization

Yang, Na; Aminov, Rustam; Franco, Octávio Luiz; Fuente-Núñez, César de la; Wang, Jianhua

doi:10.3389/fmicb.2023.1125426

Cited by 8 publications

(8 citation statements)

References 51 publications

(69 reference statements)

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“…More and better new AMPs could be created quickly by means of these AMP databases and they could play an important role in the struggle to alleviate the threat posed by AMRs to the health ecosystem. We believe that the integrative approach, proposed in this paper, will lead to the improvement of AMP databases, allowing wide coverage and balance among those three essential key principles, and final goals ranging from druggability, activity, safety, stability, resistance, and cost [ 97 ].…”

Section: Discussionmentioning

confidence: 99%

Thinking on the Construction of Antimicrobial Peptide Databases: Powerful Tools for the Molecular Design and Screening

Zhang

Teng

Mao

et al. 2023

IJMS

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With the accelerating growth of antimicrobial resistance (AMR), there is an urgent need for new antimicrobial agents with low or no AMR. Antimicrobial peptides (AMPs) have been extensively studied as alternatives to antibiotics (ATAs). Coupled with the new generation of high-throughput technology for AMP mining, the number of derivatives has increased dramatically, but manual running is time-consuming and laborious. Therefore, it is necessary to establish databases that combine computer algorithms to summarize, analyze, and design new AMPs. A number of AMP databases have already been established, such as the Antimicrobial Peptides Database (APD), the Collection of Antimicrobial Peptides (CAMP), the Database of Antimicrobial Activity and Structure of Peptides (DBAASP), and the Database of Antimicrobial Peptides (dbAMPs). These four AMP databases are comprehensive and are widely used. This review aims to cover the construction, evolution, characteristic function, prediction, and design of these four AMP databases. It also offers ideas for the improvement and application of these databases based on merging the various advantages of these four peptide libraries. This review promotes research and development into new AMPs and lays their foundation in the fields of druggability and clinical precision treatment.

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Section: Discussionmentioning

confidence: 99%

Thinking on the Construction of Antimicrobial Peptide Databases: Powerful Tools for the Molecular Design and Screening

Zhang

Teng

Mao

et al. 2023

IJMS

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“…This number is expected to reach 10 million deaths per year worldwide by 2050 [ 53 ], if not sooner, partly due to the widespread over-prescription of antimicrobials to COVID-19 patients in recent years [ 54 , 55 ]. Compared to conventional antimicrobials, AMPs possess certain advantages, such as high permeabilisation and internalisation in microbial cell membranes and, consequently, lower likelihood of developing bacterial MDR pathogens, broad-spectrum antibacterial activity, lower effect of accumulation in tissues, ability to neutralise virulence, lack of generation of active waste that can contaminate the environment and ability to modulate the host immune response [ 5 , 56 , 57 ].…”

Section: Pharmacological Proprietiesmentioning

confidence: 99%

Jelleine, a Family of Peptides Isolated from the Royal Jelly of the Honey Bees (Apis mellifera), as a Promising Prototype for New Medicines: A Narrative Review

Lima,

Brito,

Verly

et al. 2024

Toxins

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The jelleine family is a group of four peptides (jelleines I–IV) originally isolated from the royal jelly of honey bee (Apis mellifera), but later detected in some honey samples. These oligopeptides are composed of 8–9 amino acid residues, positively charged (+2 to +3 at pH 7.2), including 38–50% of hydrophobic residues and a carboxamide C-terminus. Jelleines, generated by processing of the C-terminal region of major royal jelly proteins 1 (MRJP-1), play an important biological role in royal jelly conservation as well as in protecting bee larvae from potential pathogens. Therefore, these molecules present numerous benefits for human health, including therapeutic purposes as shown in preclinical studies. In this review, we aimed to evaluate the biological effects of jelleines in addition to characterising their toxicities and stabilities. Jelleines I–III have promising antimicrobial activity and low toxicity (LD50 > 1000 mg/Kg). However, jelleine-IV has not shown relevant biological potential. Jelleine-I, but not the other analogues, also has antiparasitic, healing, and pro-coagulant activities in addition to indirectly modulating tumor cell growth and controlling the inflammatory process. Although it is sensitive to hydrolysis by proteases, the addition of halogens increases the chemical stability of these molecules. Thus, these results suggest that jelleines, especially jelleine-I, are a potential target for the development of new, effective and safe therapeutic molecules for clinical use.

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“…Antimicrobial peptides (AMPs) are a group of short peptides widely distributed in almost all forms of life [ 13 ]. Due to the high sensitivity and low resistance properties, AMPs have become one of the potential novel drug candidates during the 21st century; our team has recently proposed the iron triangle theory of health protection from AMPs, antibiotics, and vaccines and a frame of AMPs development for the post-antibiotic era [ 14 , 15 ]. In a special scope, AMPs show a potential to replace traditional antibiotics; but in a higher and broader scope, they actually belong to one of the new types of antimicrobials.…”

Section: Introductionmentioning

confidence: 99%

Molecular Modification of Kex2 P1’ Site Enhances Expression and Druggability of Fungal Defensin

et al. 2023

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Pichia pastoris is the widely used expression system for producing recombinant secretory proteins. It is known that Kex2 protease plays a vital role in the process of protein secretion, in which the P1’ site affects its cleavage efficiency. To enhance the expression level of fungal defensin-derived peptide NZ2114, this work attempts to optimize the P1’ site of Kex2 by replacing it with 20 amino acids in turn. The results showed that when the amino acid of the P1’ site was changed to Phe (F), the yield of target peptide significantly increased from 2.39 g/L to 4.81 g/L. Additionally, the novel peptide F-NZ2114 (short for FNZ) showed strong antimicrobial activity against Gram-positive (G+) bacteria, especially for Staphylococcus aureus and Streptococcus agalactiae (MIC: 4–8 μg/mL). The FNZ was very stable and retained high activity in various conditions; in addition, a low cytotoxicity and no hemolysis were observed even at a high concentration of 128 μg/mL, and a longer postantibiotic effect was reached. The above results indicate that this engineering strategy provided a feasible optimization scheme for enhancing the expression level and druggability of this antimicrobial peptide from fungal defensin and other similar targets by this updated recombinant yeast.

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Editorial: Community series in antimicrobial peptides: Molecular design, structure function relationship and biosynthesis optimization

Cited by 8 publications

References 51 publications

Thinking on the Construction of Antimicrobial Peptide Databases: Powerful Tools for the Molecular Design and Screening

Thinking on the Construction of Antimicrobial Peptide Databases: Powerful Tools for the Molecular Design and Screening

Jelleine, a Family of Peptides Isolated from the Royal Jelly of the Honey Bees (Apis mellifera), as a Promising Prototype for New Medicines: A Narrative Review

Molecular Modification of Kex2 P1’ Site Enhances Expression and Druggability of Fungal Defensin

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