Enhancing the antibacterial activity of PMAP‐37 by increasing its hydrophobicity

Zhou, Jiangfei; Liu, Yongqing; Shen, Tengfei; Chen, Liangliang; Zhao, Cong; Cai, Kairui; Liu, Zhixin; Meng, Xiangmiao; Zhang, Ling; Liao, Chengshui; Wang, Chen

doi:10.1111/cbdd.13601

Cited by 16 publications

(10 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Numerous studies have been devoted to improving the cell selectivity and antibacterial activity of AMPs [ 9 , 19 ]. Although the specific mechanism of action is unclear, moderate net positive charge and hydrophobicity are essential for the antimicrobial activity of AMPs [ 12 , 20 ]. Net positive charge can facilitate the interactions of peptides with the negatively charged plasma membrane phospholipid molecules of the bacterial cell; after interactions, hydrophobicity could impart membrane insertion to destroy the ordered structure of the bacterial cell membrane and form pores, resulting in a loss of control over ion flows across the membrane and bacterial death [ 21 ].…”

Section: Discussionmentioning

confidence: 99%

Enhancing the antibacterial activity of antimicrobial peptide PMAP-37(F34-R) by cholesterol modification

et al. 2020

Self Cite

View full text Add to dashboard Cite

Background The problem of increasing resistance against conventional antibiotics has drawn people’s attention. Therefore, the development of novel antibacterial agents with effective and safe therapeutic effects is imminent. Antimicrobial peptides (AMPs) are considered a promising class of antibacterial agents due to their broad antibacterial spectrum. Results In this study, on the basis of our previously studied peptide PMAP-37(F34-R), a novel antimicrobial peptide Chol-37(F34-R) was developed by N-terminal cholesterol modification to increase hydrophobicity. We observed that the N-terminal cholesterol-modified Chol-37(F34-R) showed higher antimicrobial activity than PMAP-37(F34-R) in vitro. Chol-37(F34-R) also exhibited effective anti-biofilm activity and may kill bacteria by improving the permeability of their membranes. Chol-37(F34-R) exerted high stability in different pH, salt, serum, and boiling water environments. Chol-37(F34-R) also showed no hemolytic activity and substantially low toxicity. Furthermore, Chol-37(F34-R) exhibited good potency of bacteria eradication and promoted wound healing and abscess reduction in infected mice. Meanwhile, in S. aureus ATCC25923-infected peritonitis model, Chol-37(F34-R) exhibited an impressive therapeutic effect by reducing the decrease in systemic bacterial burden and alleviating organ damage. Conclusions Our findings suggested that the N-terminal cholesterol modification of PMAP-37(F34-R) could improve antibacterial activity. Chol-37(F34-R) displayed excellent bactericidal efficacy and impressive therapeutic effect in vivo. Thus, Chol-37(F34-R) may be a candidate for antimicrobial agents against microbial infection in the clinic.

show abstract

Section: Discussionmentioning

confidence: 99%

Enhancing the antibacterial activity of antimicrobial peptide PMAP-37(F34-R) by cholesterol modification

et al. 2020

Self Cite

View full text Add to dashboard Cite

show abstract

“…In recent years, our group has performed research on the structural modification and antimicrobial activity of PMAPs. According to the structure and mechanism of PMAPs, many scholars have designed multiple novel modified peptides with increased stability and antimicrobial activity (43)(44)(45)(46)(47)(48)(49)(50). This review mainly summarizes the research progress on the structural characteristics and biological activities of PMAPs in recent years.…”

Section: Antimicrobial Peptidesmentioning

confidence: 99%

“…Although monomers and dimers show rapid and effective bactericidal activity against most microorganisms, dimeric peptides have a more stable conformation, longer bacteriostatic time, and lower medium sensitivity (34,62). PMAP-37 is an amphiphilic antimicrobial peptide that contains 37 amino acid residues with a molecular weight of 4365.02 Da (38,50), and the amino acid sequence of PMAP-37 is GLLSRLRDFLSDRGRRLGEKIERIGQKIKDLSEFFQS (48,49). PMAP-37 has the highest hydrophobicity and the lowest net charge (22).…”

Section: Porcine Myeloid Antimicrobial Peptidesmentioning

confidence: 99%

“…The sensitivity of Gram-negative bacteria to PMAP-37 and its analogs is higher than that of Grampositive bacteria, and the MIC of PMAP-37 (R13-I) for Gramnegative bacteria is lower than that of PMAP-37. Moreover, PMAP-37 (K20/27-I) has antimicrobial activity against Shigella flexneri CICC 21534, especially S. typhimurium SL1344, with ∼4-fold increases in antimicrobial activity, and it has obvious therapeutic effects on mice infected with S. aureus ATCC 25923 and S. typhimurium SL1344 (48). The antimicrobial activity can be enhanced by increasing the net charge of the polypeptide to a certain range (89).…”

Section: Antibacterial Activity Of Pmap-37mentioning

confidence: 99%

See 1 more Smart Citation

Porcine Myeloid Antimicrobial Peptides: A Review of the Activity and Latest Advances

et al. 2021

Self Cite

View full text Add to dashboard Cite

Traditional antibiotics have made great contributions to human health and animal husbandry since the discovery of penicillin in 1928, but bacterial resistance and drug residues are growing threats to global public health due to the long-term uncontrolled application of antibiotics. There is a critical need to develop new antimicrobial drugs to replace antibiotics. Antimicrobial peptides (AMPs) are distributed in all kingdoms of life, presenting activity against pathogens as well as anticancer, anti-inflammatory, and immunomodulatory activities; consequently, they have prospects as new potential alternatives to antibiotics. Porcine myeloid antimicrobial peptides (PMAPs), the porcine cathelicidin family of AMPs, have been reported in the literature in recent years. PMAPs have become an important research topic due to their strong antibacterial activity. This review focuses on the universal trends in the biochemical parameters, structural characteristics and biological activities of PMAPs.

show abstract

“…24 Therefore, the combined use of an AP and CdSe QDs (such as conventional antibiotics) definitely has the potential to improve the effectiveness of the two groups of compounds. [25][26][27] In this study, an AP, used as a stabilizer and active group, was modified on the surface of CdSe QDs to form fluorescent AP NPs (AP-CdSe NPs) with high antibacterial activity. 28 The AP-CdSe NPs showed strong antibacterial activity against MDR Escherichia coli (E. coli) and Staphylococcus aureus (S. aureus) in vitro and in vivo.…”

Section: Introductionmentioning

confidence: 99%

The Effects of Luminescent CdSe Quantum Dot-Functionalized Antimicrobial Peptides Nanoparticles on Antibacterial Activity and Molecular Mechanism

Song

Xin

et al. 2021

IJN

View full text Add to dashboard Cite

Background With the development of bacterial resistance, the range of effective antibiotics is increasingly becoming more limited. The effective use of nanoscale antimicrobial peptides (AP) in therapeutic and diagnostic methods is a strategy for new antibiotics. Methods Combining both AP and cadmium selenide (CdSe) into a composite material may result in a reagent with novel properties, such as enhanced antibacterial activity, fluorescence and favorable stability in aqueous solution. Results AP-loaded CdSe NPs (AP-CdSe NPs) showed strong antibacterial activity against multidrug-resistant (MDR) Escherichia coli ( E. coli ) and Staphylococcus aureus ( S. aureus ) in vitro and in vivo. Colony-forming unit (CFU) and minimum inhibitory concentration (MIC) assays showed that AP-CdSe NPs have highly effective antibacterial activity. The quantitative analysis of apoptosis by flow cytometry analysis further confirmed that MDR E. coli and S. aureus treated with AP-CdSe NPs had death rates of 98.76% and 99.13%, respectively. Also, AP-CdSe NPs was found to inhibit bacterial activity in an in vivo bacteremia model in mice infected with S. aureus . In addition, the antibacterial mechanism of AP-CdSe NPs was determined by RNA sequencing analysis. Gene ontology (GO) analysis and Kyoto encyclopedia of genes and genomes (KEGG) pathway analysis revealed the molecular mechanism of the antibacterial effect of AP-CdSe NPs. Importantly, histopathology analysis, and hematological toxicity analysis indicated that AP-CdSe NPs had few side effects. Conclusion These results demonstrate that AP loaded on CdSe NPs had a higher water solubility, bioavailability and antibacterial effect compared with raw AP. This study reports findings that are helpful for the design and development of antibacterial treatment strategies based on AP.

show abstract

Enhancing the antibacterial activity of PMAP‐37 by increasing its hydrophobicity

Cited by 16 publications

References 54 publications

Enhancing the antibacterial activity of antimicrobial peptide PMAP-37(F34-R) by cholesterol modification

Enhancing the antibacterial activity of antimicrobial peptide PMAP-37(F34-R) by cholesterol modification

Porcine Myeloid Antimicrobial Peptides: A Review of the Activity and Latest Advances

The Effects of Luminescent CdSe Quantum Dot-Functionalized Antimicrobial Peptides Nanoparticles on Antibacterial Activity and Molecular Mechanism

Contact Info

Product

Resources

About