The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent
Open accessAbstract
The rise in antimicrobial resistant bacteria threatens the current methods utilized to treat bacterial infections. The development of novel therapeutic agents is crucial in avoiding a post-antibiotic era and the associated deaths from antibiotic resistant pathogens. The human antimicrobial peptide LL-37 has been considered as a potential alternative to conventional antibiotics as it displays broad spectrum antibacterial and anti-biofilm activities as well as immunomodulatory functions. While LL-37 has shown promising results, it has yet to receive regulatory approval as a peptide antibiotic. Despite the strong antimicrobial properties, LL-37 has several limitations including high cost, lower activity in physiological environments, susceptibility to proteolytic degradation, and high toxicity to human cells. This review will discuss the challenges associated with making LL-37 into a viable antibiotic treatment option, with a focus on antimicrobial resistance and cross-resistance as well as adaptive responses to sub-inhibitory concentrations of the peptide. The possible methods to overcome these challenges, including immobilization techniques, LL-37 delivery systems, the development of LL-37 derivatives, and synergistic combinations will also be considered. Herein, we describe how combination therapy and structural modifications to the sequence, helicity, hydrophobicity, charge, and configuration of LL-37 could optimize the antimicrobial and anti-biofilm activities of LL-37 for future clinical use.
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Nakatsuji, T., Chen, T. H., Narala, S., Chun, K. A., Two, A. M., Yun, T., Shafiq, F., Kotol, P. F., Bouslimani, A., Melnik, A. V., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aah4680 · Cited by 1,095
The antimicrobial peptide SAAP-148 combats drug-resistant bacteria and biofilms
de Breij, A., Riool, M., Cordfunke, R. A., Malanovic, N., de Boer, L., Koning, R. I., Ravensbergen, E., Franken, M., van der Heijde, T., Boekema, B. K., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aan4044 · Cited by 555
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“To kill bacteria, chlorhexidine targets membrane fluidity, which results in the loss of structural integrity of the membrane [96].”
BackgroundBacterial proteases, untapped antimicrobial drug targets
Culp, E., & Wright, G. D. (2017) · The Journal of Antibiotics · doi:10.1038/ja.2016.138 · Cited by 244
Wang, G., Mishra, B., Epand, R. F., & Epand, R. M. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.01.016 · Cited by 184
Sakoulas, G., Bayer, A. S., Pogliano, J., Tsuji, B. T., Yang, S.-J., Mishra, N. N., Nizet, V., Yeaman, M. R., & Moise, P. A. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.05551-11 · Cited by 176
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“DAP exhibits antibacterial effects against heterogeneous VAN-intermediate S. aureus (hVISA), VISA [208], MRSA and vancomycin-resistant enterococci (VRE) [207].”
BackgroundInfluentialSakoulas, G., Rose, W., Nonejuie, P., Olson, J., Pogliano, J., Humphries, R., & Nizet, V. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02274-13 · Cited by 94 · cited 1×
“One study found that the combination of DAP and CPT increased the amount of LL-37 binding to the surface of VRE, and therefore sensitizes the bacteria to LL-37 [209].”
BackgroundSakoulas, G., Nonejuie, P., Nizet, V., Pogliano, J., Crum-Cianflone, N., & Haddad, F. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02481-12 · Cited by 65
Cited by
Sharma, S., Mohler, J., Mahajan, S. D., Schwartz, S. A., Bruggemann, L., & Aalinkeel, R. (2023) · Microorganisms · doi:10.3390/microorganisms11061614 · Cited by 993
Bostanghadiri, N., Kouhzad, M., Taki, E., Elahi, Z., Khoshbayan, A., Navidifar, T., & Darban-Sarokhalil, D. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1431785 · Cited by 61
Antimicrobial peptides for bone tissue engineering: Diversity, effects and applications
Hao, Z., Chen, R., Chai, C., Wang, Y., Chen, T., Li, H., Hu, Y., Feng, Q., & Li, J. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.1030162 · Cited by 47
Brown, A. N., Anderson, M. T., Smith, S. N., Bachman, M. A., & Mobley, H. L. T. (2023) · mBio · doi:10.1128/mbio.01448-23 · Cited by 14
Metadata
- Authors
- Ridyard, K. E., & Overhage, J.
- Venue
- Antibiotics
- Publisher
- MDPI AG
- Published
- 2021-05-29
- Volume
- 10
- Issue
- 6
- Pages
- 650
- ISSN
- 2079-6382 (ISSN-L)
- OpenAlex
- W3164122911
- Cited by
- 270
- References
- 9
- FWCI
- 18.31
- Type
- journal article
- Language
- en
- Open access
- gold
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