Cell Penetrating Peptides and Cationic Antibacterial Peptides

Plaza, Jonathan G. Rodríguez; Morales‐Nava, Rosmarbel; Diener, Christian; Schreiber, G; Gonzalez, Z; Ortiz, María Teresa Lara; Blake, Iván Ortega; Pantoja, Omar; Volkmer, Rudolf; Klipp, Edda; Herrmann, Andreas; Río, Gabriel del

doi:10.1074/jbc.m113.515023

Cited by 45 publications

(40 citation statements)

References 51 publications

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“…The existence of at least partially different mechanisms in the combination PAF26/PAF protein is also supported by the different profile of activity among different fungal strains ( Table 3 ). Furthermore, the demonstration of synergy also opens up new alternatives to improve (i) the antifungal activity of AFPs by combined action with other unrelated peptides such as PAF26, or (ii) the rational design of novel AMPs by combination of distinct peptide sequences (Badosa et al, 2009; Rodriguez Plaza et al, 2014). …”

Section: Discussionmentioning

confidence: 99%

Mapping and Identification of Antifungal Peptides in the Putative Antifungal Protein AfpB from the Filamentous Fungus Penicillium digitatum

et al. 2017

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Antifungal proteins (AFPs) from Ascomycetes are small cysteine-rich proteins that are abundantly secreted and show antifungal activity against non-producer fungi. A gene coding for a class B AFP (AfpB) was previously identified in the genome of the plant pathogen Penicillium digitatum. However, previous attempts to detect the AfpB protein were not successful despite the high expression of the corresponding afpB gene. In this work, the structure of the putative AfpB was modeled. Based on this model, four synthetic cysteine-containing peptides, PAF109, PAF112, PAF118, and PAF119, were designed and their antimicrobial activity was tested and characterized. PAF109 that corresponds to the γ-core motif present in defensin-like antimicrobial proteins did not show antimicrobial activity. On the contrary, PAF112 and PAF118, which are cationic peptides derived from two surface-exposed loops in AfpB, showed moderate antifungal activity against P. digitatum and other filamentous fungi. It was also confirmed that cyclization through a disulfide bridge prevented peptide degradation. PAF116, which is a peptide analogous to PAF112 but derived from the Penicillium chrysogenum antifungal protein PAF, showed activity against P. digitatum similar to PAF112, but was less active than the native PAF protein. The two AfpB-derived antifungal peptides PAF112 and PAF118 showed positive synergistic interaction when combined against P. digitatum. Furthermore, the synthetic hexapeptide PAF26 previously described in our laboratory also exhibited synergistic interaction with the peptides PAF112, PAF118, and PAF116, as well as with the PAF protein. This study is an important contribution to the mapping of antifungal motifs within the AfpB and other AFPs, and opens up new strategies for the rational design and application of antifungal peptides and proteins.

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Section: Discussionmentioning

confidence: 99%

Mapping and Identification of Antifungal Peptides in the Putative Antifungal Protein AfpB from the Filamentous Fungus Penicillium digitatum

et al. 2017

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“…Also, marine AMPs are highly stable also due to the presence of large number of disulfide bridges (2)(3) and unnatural amino acids [11]. Finally, a number of AMPs from various terrestrial bioresources, such as buforin, histatin, iztli peptide and indolicidin, have been previously shown to possess CPP activity and vice versa [13][14][15]. Keeping these points in view, we investigated the ability of a marine AMP, tachyplesin (Tpl), to act as a CPP.…”

Section: Introductionmentioning

confidence: 99%

Marine antimicrobial peptide tachyplesin as an efficient nanocarrier for macromolecule delivery in plant and mammalian cells

2015

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Membrane‐active peptides can be classified as cell‐penetrating peptides and antimicrobial peptides (AMPs) that are known to play interchangeable roles. In this study, this dual behaviour was studied for the marine AMP, tachyplesin. It is a well‐established cyclic peptide known to possess antimicrobial properties and was investigated for its cell‐penetrating property and cargo delivery ability. Because of its derivation from a marine organism as well as cyclic nature, it has been shown to possess higher stability in vitro. In this study, its internalization as a cell‐penetrating peptide was established and characterized in both plant and mammalian systems. It was shown to deliver cargo molecules in both living systems, emerging as an efficient nonviral macromolecule nanocarrier.

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“…Cationic antibacterial peptides (CAPs) have very similar physicochemical features with CPPs, yet they perform two different functions. CPPs are known to penetrate eukaryotic cells without any apparent toxicity or damage while the main function of CAPs is to kill bacteria [110]. Interestingly, several CPPs have been shown to have antibacterial activity.…”

Section: Amps and Cppsmentioning

confidence: 99%

Membrane Active Peptides and Their Biophysical Characterization

Avcı

Akbulut

Özkırımlı

2018

Preprint

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In the last 20 years, an increasing number of studies have been reported on membrane active peptides, which exert their biological activity by interacting with the cell membrane either to disrupt it and lead to cell lysis or to translocate through it to deliver cargos into the cell and reach their target. These peptides are attractive alternatives to currently used pharmaceuticals. Antimicrobial peptides (AMPs) and peptides designed for drug and gene delivery currently in the drug pipeline suggest that these membrane active peptides will soon constitute a significant percentage of the drug market. Here, we focus on two most prominent classes of membrane active peptides; AMPs and cell-penetrating peptides (CPPs). AMPs are a group of membrane active peptides that disrupt the membrane integrity or inhibit the cellular functions of bacteria, virus and fungi. CPPs are another group of membrane active peptides that mainly function as cargo-carriers even though they may also show antimicrobial activity to some extent. Biophysical techniques to understand how they interact with the membrane have shed light on the peptide-membrane interaction at various levels of detail. Structural investigation of membrane active peptides in the presence of the membrane provides important clues on the effect of the membrane environment on peptide conformations. Advances in live imaging techniques have allowed examination of peptide action at a single cell or single molecule level. In addition to these experimental biophysical techniques, molecular dynamics simulations provided clues on the peptide-lipid interactions and dynamics of the cell entry process at atomic detail. In this review, we summarize the recent advances in experimental and computational investigation of membrane active peptides with particular emphasis on two amphipathic membrane active peptides, the AMP melittin and the CPP pVEC.

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Cell Penetrating Peptides and Cationic Antibacterial Peptides

Cited by 45 publications

References 51 publications

Mapping and Identification of Antifungal Peptides in the Putative Antifungal Protein AfpB from the Filamentous Fungus Penicillium digitatum

Mapping and Identification of Antifungal Peptides in the Putative Antifungal Protein AfpB from the Filamentous Fungus Penicillium digitatum

Marine antimicrobial peptide tachyplesin as an efficient nanocarrier for macromolecule delivery in plant and mammalian cells

Membrane Active Peptides and Their Biophysical Characterization

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