Abstract
The increasing onset of multidrug-resistant bacteria has propelled microbiology research towards antimicrobial peptides as new possible antibiotics from natural sources. Antimicrobial peptides are short peptides endowed with a broad range of activity against both Gram-positive and Gram-negative bacteria and are less prone to trigger resistance. Besides their activity against planktonic bacteria, many antimicrobial peptides also show antibiofilm activity. Biofilms are ubiquitous in nature, having the ability to adhere to virtually any surface, either biotic or abiotic, including medical devices, causing chronic infections that are difficult to eradicate. The biofilm matrix protects bacteria from hostile environments, thus contributing to the bacterial resistance to antimicrobial agents. Biofilms are very difficult to treat, with options restricted to the use of large doses of antibiotics or the removal of the infected device. Antimicrobial peptides could represent good candidates to develop new antibiofilm drugs as they can act at different stages of biofilm formation, on disparate molecular targets and with various mechanisms of action. These include inhibition of biofilm formation and adhesion, downregulation of quorum sensing factors, and disruption of the pre-formed biofilm. This review focuses on the proprieties of antimicrobial and antibiofilm peptides, with a particular emphasis on their mechanism of action, reporting several examples of peptides that over time have been shown to have activity against biofilm.
Highlights
In 1922, Alexander Fleming identified lysozyme from nasal mucus [1], which was considered the first human antimicrobial protein
Anunthawan et al studied KT2 and RT2, two synthetic tryptophan-rich cationic peptides, which showed activity against multidrug-resistant E. coli biofilms at sub-minimum inhibitory concentration (MIC) levels [96]. Another peptide known as CRAMP is able to inhibit fungal biofilm formation [97], but surprisingly, it was demonstrated that AS10, a CRAMP shorter fragment, was able to inhibit biofilm growth of Candida albicans, E. coli, and P. aeruginosa [98]
The high concentrations of antibiotics used in order to disrupt or prevent biofilm formation could be associated with poor prognosis and cytotoxicity
Summary
In 1922, Alexander Fleming identified lysozyme from nasal mucus [1], which was considered the first human antimicrobial protein. This discovery was overshadowed when in 1928, Fleming discovered penicillin, which, together with streptomycin, in 1943, led to the beginning of the so-called “Golden Age of Antibiotics”. With the advent of the “Golden Age of Antibiotics”, there was a loss of interest in the therapeutic potential of natural antimicrobial peptides (AMPs), such as lysozyme [2,3]. Since the discovery of the first groups of AMPs, the magainins from the skin of the African clawed frog Xenopus laevis by Zasloff et al [10,11,12] and the first antimicrobial peptides. MplanyktAonMicPscsohuonwterapnatirbtisofi[1lm7].acMtiavnityy aAgMaiPnst smhuolwtidarnutgi-brieosfiisltmantabctaicvtietryiaa, gaactiinnsgt amt udilfftiedrreungt-srteasgisetsaonft biaocfitelmriaf,oarmctiantgiona,t odnifdfeisrpenatrastteamgeosleocfublaior ftialmrgeftosramnadtiwonit,hovnardioisupsamraetechmanoilsemcus.lar targets and with varioTuhsismercehvaienwismfso.cuses on antimicrobial peptides and their mechanism of action against biofilTmhifsorrmevaiteiown.focuses on antimicrobial peptides and their mechanism of action against biofilm formation
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