Antimicrobial Peptides in 2014

Wang, Guangshun; Mishra, Biswajit; Lau, Kyle; Lushnikova, Tamara; Golla, Radha M.; Wang, Xiuqing

doi:10.3390/ph8010123

Cited by 164 publications

(146 citation statements)

References 188 publications

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“…In conclusion, AMPs are effective antibiofilm compounds, 22,33 and human cathelicidin LL-37 has been established as an important antibiofilm peptide. 12−21 As an advance, we have recently engineered LL-37 into a potent, selective, and stable peptide.…”

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confidence: 95%

Anti-Staphylococcal Biofilm Effects of Human Cathelicidin Peptides

Mishra

Golla

Lau

et al. 2015

ACS Med. Chem. Lett.

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101

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Staphylococcus aureus can live together in the form of biofilms to avoid elimination by the host. Thus, a useful strategy to counteract bacterial biofilms is to re-engineer human antimicrobial peptide LL-37 so that it can be used as a remedy for preventing and removing biofilms. This study reports antibiofilm effects of four human cathelicidin LL-37 peptides against community-associated and hospital isolated methicillin-resistant Staphylococcus aureus (MRSA) strains. Although the intact molecule LL-37 inhibited biofilm formation at low concentrations, it did not inhibit bacterial attachment nor disrupt preformed biofilms. However, two 17-residue peptides, GF-17 and 17BIPHE2, inhibited bacterial attachment, biofilm growth, and disrupted established biofilms. An inactive peptide RI-10 was used as a negative control. Our results obtained using the S. aureus mutants in a static biofilm model are consistent with the literature obtained in a flow cell biofilm model. Because 17BIPHE2 is the most effective biofilm disruptor with desired stability to proteases, it is a promising lead for developing new anti-MRSA biofilm agents.

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confidence: 95%

Anti-Staphylococcal Biofilm Effects of Human Cathelicidin Peptides

Mishra

Golla

Lau

et al. 2015

ACS Med. Chem. Lett.

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101

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“…Antimicrobial peptides (AMPs), which are isolated from a range of organisms, including insects, fish, amphibians and mammals (3,4), are typically cationic and amphipathic molecules (5). AMPs exhibit a wide range of antibacterial activities through direct electrostatic bonding to the anionic surfaces of bacteria, leading to the disruption of their plasma membrane (6).…”

Section: Introductionmentioning

confidence: 99%

Bovine lactoferricin P13 triggers ROS-mediated caspase-dependent apoptosis in SMMC7721 cells

Meng

et al. 2016

Oncology Letters

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Abstract. Bovine lactoferricin P13 (LfcinB-P13) is a peptide derived from LfcinB. In the present study, the effect of LfcinB-P13 on the human liver cancer cell line SMMC7721 was investigated in vitro and in vivo. The results of the present study indicate that LfcinB-P13 significantly decreased SMMC7721 cell viability in vitro (P=0.032 vs. untreated cells), while exhibiting low cytotoxicity in the wild-type liver cell line L02. In addition, the rate of apoptosis in SMMC7721 cells was significantly increased following treatment with 40 and 60 µg/ml LfcinB-P13 (P=0.0053 vs. the control group), which was associated with an increase in the level of reactive oxygen species (ROS) and the activation of caspase-3 and -9. Furthermore, ROS chelation led to the suppression of LfcinB-P13-mediated caspase-3 and -9 activation in SMMC7721 cells. LfcinB-P13 was demonstrated to markedly inhibit tumor growth in an SMMC7721-xenograft nude mouse model. The results of the present study indicate that LfcinB-P13 is a novel candidate therapeutic agent for the treatment of liver cancer.

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“…A ntimicrobial peptides (AMPs) represent a promising alternative to conventional therapeutics in the face of concerns about the rise of antibiotic-resistant bacteria in clinical settings (1). Traditionally, AMPs were believed to kill bacteria through membrane disruption.…”

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confidence: 99%

Bacterial Spheroplasts as a Model for Visualizing Membrane Translocation of Antimicrobial Peptides

Lei

LaBouyer

Darling

et al. 2016

Antimicrob Agents Chemother

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Studies attempting to characterize the membrane translocation of antimicrobial and cell-penetrating peptides are frequently limited by the resolution of conventional light microscopy. This study shows that spheroplasts provide a valuable approach to overcome these limits. Spheroplasts produce less ambiguous images and allow for more systematic analyses of localization. Data collected with spheroplasts are consistent with studies using normal bacterial cells and imply that a particular peptide may not always follow the same mechanism of action.A ntimicrobial peptides (AMPs) represent a promising alternative to conventional therapeutics in the face of concerns about the rise of antibiotic-resistant bacteria in clinical settings (1). Traditionally, AMPs were believed to kill bacteria through membrane disruption. While many AMPs do induce membrane permeabilization, researchers have identified increasing numbers of peptides that function by translocating into bacterial cells and targeting intracellular components (2). Thus, it has become increasingly important for researchers to reliably determine whether AMPs are able to effectively translocate into bacterial cells (3). Many researchers have turned to confocal microscopy in order to assess cell entry (4-11). However, bacterial cells are so small that effective imaging is limited by the resolution of conventional light microscopes. For example, in order to distinguish whether any observed signal from peptides arises from inside the cell versus on the cell membrane, researchers ideally should examine individual focal plane images throughout cells. However, if signal on the membrane is sufficiently strong it can "contaminate" slices ostensibly taken "inside" the cell, as we have observed in measurements of the membrane-localized dye di-8-ANEPPS (Fig. 1).In order to overcome these resolution limits, we have employed bacterial spheroplasts (12)(13)(14). Spheroplasts are produced by culturing bacteria in the presence of an antibiotic, such as cephalexin, that prevents division while still allowing cells to grow. The resulting elongated bacterial "snakes" are then exposed to lysozyme, which digests the outer cell wall and produces spherical spheroplasts that are typically 2 to 5 m in diameter (see Fig. S1 in the supplemental material). Perhaps even more important than larger size, the spherical shape allows one to obtain consistent slices regardless of how a spheroplast is oriented during imaging.In order to test the validity of using spheroplasts to assess peptide translocation, we have measured the cellular localization of four previously characterized peptides (Table 1). To this end, we exposed Escherichia coli spheroplasts to peptides with an N-terminally conjugated fluorescein isothiocyanate (FITC) label for imaging; detailed methods for spheroplast preparation and peptide incubation are provided in the supplemental material. As one set of positive and negative controls, we chose buforin II (BF2), arguably the best-studied membrane-translocating AMP (15), and BF2 with...

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Antimicrobial Peptides in 2014

Cited by 164 publications

References 188 publications

Anti-Staphylococcal Biofilm Effects of Human Cathelicidin Peptides

Anti-Staphylococcal Biofilm Effects of Human Cathelicidin Peptides

Bovine lactoferricin P13 triggers ROS-mediated caspase-dependent apoptosis in SMMC7721 cells

Bacterial Spheroplasts as a Model for Visualizing Membrane Translocation of Antimicrobial Peptides

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