ArticleProtein science : a publication of the Protein Society2018
Secondary structure of cell-penetrating peptides during interaction with fungal cells.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Cell-Penetrating Peptide-Mediated Biomolecule Transportation in Artificial Lipid Vesicles and Living Cells.Molecules (Basel, Switzerland) · 2024Review
- Sneaking in SpyCatcher using cell penetrating peptides forNanotechnology · 2023Article
- Stability of ACE2 Peptide Mimetics and Their Implications on the Application for SARS-CoV2 Detection.Biosensors · 2023Article
- Cell-Penetrating Peptides for Use in Development of Transgenic Plants.Molecules (Basel, Switzerland) · 2023Review
- In vitro and in silico studies for the identification of anti-cancer and antibacterial peptides from camel milk protein hydrolysates.PloS one · 2023Article
- Understanding the Biophysical Interaction of LTX-315 with Tumoral Model Membranes.International journal of molecular sciences · 2022Article
- Cell-Penetrating Antimicrobial Peptides with Anti-Infective Activity against Intracellular Pathogens.Antibiotics (Basel, Switzerland) · 2022Review
- Unveiling the Metal-Dependent Aggregation Properties of the C-terminal Region of Amyloidogenic Intrinsically Disordered Protein Isoforms DPF3b and DPF3a.International journal of molecular sciences · 2022Article
- Article
- Systematic Screening of Penetratin's Protein Targets by Yeast Proteome Microarrays.International journal of molecular sciences · 2022Article
- Article
- Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca.Scientific reports · 2021Article
- Impact of a Single Point Mutation on the Antimicrobial and Fibrillogenic Properties of Cryptides from Human Apolipoprotein B.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Physicochemical Features and Peculiarities of Interaction of AMP with the Membrane.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Identification of Candida glabrata Transcriptional Regulators That Govern Stress Resistance and Virulence.Infection and immunity · 2021Article
- Novel Assay Platform to Evaluate Intracellular Killing ofFrontiers in immunology · 2021Article
- Conformational Changes of Anoplin, W-MreBInternational journal of molecular sciences · 2020Article
- Cupid, a cell permeable peptide derived from amoeba, capable of delivering GFP into a diverse range of species.Scientific reports · 2020Article
- Drug Conjugation Induced Modulation of Structural and Membrane Interaction Features of Cationic Cell-Permeable Peptides.International journal of molecular sciences · 2020Article
- Application of Biophysical Techniques to Investigate the Interaction of Antimicrobial Peptides With Bacterial Cells.Frontiers in medical technology · 2020Review
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3 authors.
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Abstract
Cell-penetrating peptides (CPPs) are peptides that cross cell membranes, either alone or while carrying molecular cargo. Although their interactions with mammalian cells have been widely studied, much less is known about their interactions with fungal cells, particularly at the biophysical level. We analyzed the interactions of seven CPPs (penetratin, Pep-1, MPG, pVEC, TP-10, MAP, and cecropin B) with the fungal pathogen Candida albicans using experiments and molecular simulations. Circular dichroism (CD) of the peptides revealed a structural transition from a random coil or weak helix to an α-helix occurs for all peptides when the solvent is changed from aqueous to hydrophobic. However, CD performed in the presence of C. albicans cells showed that proximity to the cell membrane is not necessarily sufficient to induce this structural transition, as penetratin, Pep-1, and MPG did not display a structural shift in the presence of cells. Monte Carlo simulations were performed to further probe the molecular-level interaction with the cell membrane, and these simulations suggested that pVEC, TP-10, MAP, and cecropin B strongly penetrate into the hydrophobic domain of the membrane lipid bilayer, inducing a transition to an α-helical conformation. In contrast, penetratin, Pep-1 and MPG remained in the hydrophilic region without a shift in conformation. The experimental data and MC simulations combine to explain how peptide structure affects their interaction with cells and their mechanism of translocation into cells (direct translocation vs. endocytosis). Our work also highlights the utility of combining biophysical experiments, biological experiments, and molecular modeling to understand biological phenomena.
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