Cargando…

Importance of Tryptophan in Transforming an Amphipathic Peptide into a Pseudomonas aeruginosa-Targeted Antimicrobial Peptide

Here, we found that simple substitution of amino acids in the middle position of the hydrophobic face of an amphipathic peptide RI16 with tryptophan (T9W) considerably transformed into an antimicrobial peptide specifically targeting Pseudomonas aeruginosa. Minimal inhibitory concentration (MIC) resu...

Descripción completa

Detalles Bibliográficos
Autores principales:	Zhu, Xin, Ma, Zhi, Wang, Jiajun, Chou, Shuli, Shan, Anshan
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2014
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4262413/ https://www.ncbi.nlm.nih.gov/pubmed/25494332 http://dx.doi.org/10.1371/journal.pone.0114605

Ejemplares similares

Conversion of Broad-Spectrum Antimicrobial Peptides into Species-Specific Antimicrobials Capable of Precisely Targeting Pathogenic Bacteria
por: Xu, Lin, et al.
Publicado: (2020)

Peptides With Triplet-Tryptophan-Pivot Promoted Pathogenic Bacteria Membrane Defects
por: Chou, Shuli, et al.
Publicado: (2020)

Selective Antifungal Activity and Fungal Biofilm Inhibition of Tryptophan Center Symmetrical Short Peptide
por: Chou, Shuli, et al.
Publicado: (2021)

Hybrid Antimicrobial Peptide Targeting Staphylococcus aureus and Displaying Anti-infective Activity in a Murine Model
por: Shang, Lu, et al.
Publicado: (2020)

High specific selectivity and Membrane-Active Mechanism of the synthetic centrosymmetric α-helical peptides with Gly-Gly pairs
por: Wang, Jiajun, et al.
Publicado: (2015)

Systematic Design and Validation of Ion Channel Stabilization of Amphipathic α-Helical Peptides Incorporating Tryptophan Residues
por: Shigedomi, Keita, et al.
Publicado: (2020)

Contribution of Amphipathicity and Hydrophobicity to the Antimicrobial Activity and Cytotoxicity of β-Hairpin Peptides
por: Edwards, Ingrid A., et al.
Publicado: (2016)

Morphing of Amphipathic Helices to Explore the Activity and Selectivity of Membranolytic Antimicrobial Peptides
por: Müller, Alex T., et al.
Publicado: (2020)

Activity of Antimicrobial Peptides and Ciprofloxacin against Pseudomonas aeruginosa Biofilms
por: Yasir, Muhammad, et al.
Publicado: (2020)

Adaptive and Mutational Responses to Peptide Dendrimer Antimicrobials in Pseudomonas aeruginosa
por: Ben Jeddou, Fatma, et al.
Publicado: (2020)

Pseudomonas aeruginosa biofilm dispersion by the mouse antimicrobial peptide CRAMP
por: Zhang, Yang, et al.
Publicado: (2022)

Short Symmetric-End Antimicrobial Peptides Centered on β-Turn Amino Acids Unit Improve Selectivity and Stability
por: Dong, Na, et al.
Publicado: (2018)

Extracellular DNA-induced antimicrobial peptide resistance mechanisms in Pseudomonas aeruginosa
por: Lewenza, Shawn
Publicado: (2013)

Activity of a novel antimicrobial peptide against Pseudomonas aeruginosa biofilms
por: Beaudoin, Trevor, et al.
Publicado: (2018)

Mechanism of Action of Surface Immobilized Antimicrobial Peptides Against Pseudomonas aeruginosa
por: Yasir, Muhammad, et al.
Publicado: (2020)

Antimicrobial Peptide-Loaded Nanoparticles as Inhalation Therapy for Pseudomonas aeruginosa Infections
por: Falciani, Chiara, et al.
Publicado: (2020)

Key Physicochemical Determinants in the Antimicrobial Peptide RiLK1 Promote Amphipathic Structures
por: Falcigno, Lucia, et al.
Publicado: (2021)

Large-Scale Analysis of Antimicrobial Activities in Relation to Amphipathicity and Charge Reveals Novel Characterization of Antimicrobial Peptides
por: Wang, Chien-Kuo, et al.
Publicado: (2017)

Tryptophan-Rich and Proline-Rich Antimicrobial Peptides
por: Mishra, Awdhesh Kumar, et al.
Publicado: (2018)

Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles
por: Hong, Hui, et al.
Publicado: (2017)

Anti-Pseudomonas aeruginosa activity of natural antimicrobial peptides when used alone or in combination with antibiotics
por: Chen, Xueqi, et al.
Publicado: (2023)

Cationic Amphipathic Antimicrobial Peptides Perturb the Inner Membrane of Germinated Spores Thus Inhibiting Their Outgrowth
por: Omardien, Soraya, et al.
Publicado: (2018)

The evolution of antimicrobial peptide resistance in Pseudomonas aeruginosa is shaped by strong epistatic interactions
por: Jochumsen, Nicholas, et al.
Publicado: (2016)

Antimicrobial Activity of Poly-epsilon-lysine Peptide Hydrogels Against Pseudomonas aeruginosa
por: Kennedy, Stephnie M., et al.
Publicado: (2020)

Identification of an amphipathic peptide sensor of the Bacillus subtilis fluid membrane microdomains
por: Jiang, Yiping, et al.
Publicado: (2019)

Advances of Antimicrobial Peptide‐Based Biomaterials for the Treatment of Bacterial Infections
por: Li, Guoyu, et al.
Publicado: (2023)

Membrane Thinning and Thickening Induced by Membrane-Active Amphipathic Peptides
por: Grage, Stephan L., et al.
Publicado: (2016)

Chirality-Dependent Adsorption between Amphipathic Peptide and POPC Membrane
por: Chen, Ke, et al.
Publicado: (2019)

A Second Life for MAP, a Model Amphipathic Peptide
por: Silva, Sara, et al.
Publicado: (2022)

High Specific Selectivity and Membrane-Active Mechanism of Synthetic Cationic Hybrid Antimicrobial Peptides Based on the Peptide FV7
por: Tan, Tingting, et al.
Publicado: (2017)

Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4
por: Chang, Ting-Wei, et al.
Publicado: (2017)

Synergy Pattern of Short Cationic Antimicrobial Peptides Against Multidrug-Resistant Pseudomonas aeruginosa
por: Ruden, Serge, et al.
Publicado: (2019)

Microbiome-derived antimicrobial peptides offer therapeutic solutions for the treatment of Pseudomonas aeruginosa infections
por: Mulkern, Adam J., et al.
Publicado: (2022)

Design of Embedded-Hybrid Antimicrobial Peptides with Enhanced Cell Selectivity and Anti-Biofilm Activity
por: Xu, Wei, et al.
Publicado: (2014)

Cell-Penetrating Peptides: Design Strategies beyond Primary Structure and Amphipathicity
por: Kalafatovic, Daniela, et al.
Publicado: (2017)

An efficient expression tag library based on self-assembling amphipathic peptides
por: Zhao, Weixin, et al.
Publicado: (2019)

Amphipathic Peptide Antibiotics with Potent Activity against Multidrug-Resistant Pathogens
por: Shi, Jingru, et al.
Publicado: (2021)

Amphipathic Peptides Impede Lipid Domain Fusion in Phase-Separated Membranes
por: Pinigin, Konstantin V., et al.
Publicado: (2021)

Model Amphipathic Peptide Coupled with Tacrine to Improve Its Antiproliferative Activity
por: Silva, Sara, et al.
Publicado: (2020)

LL-37, a Multi-Faceted Amphipathic Peptide Involved in NETosis
por: Radic, Marko, et al.
Publicado: (2022)

Cannot write session to /tmp/vufind_sessions/sess_qrf8fenjjglrq93tejb3qpp9nm