Cargando…
Systematic Design and Validation of Ion Channel Stabilization of Amphipathic α-Helical Peptides Incorporating Tryptophan Residues
[Image: see text] Aromatic interactions such as π–π interaction and cation−π interaction are present in membrane proteins and play important roles in both structure and function. To systematically investigate the effect of aromatic residues on the structural stability and ion permeability of peptide...
Autores principales: | Shigedomi, Keita, Osada, Satoshi, Jelokhani-Niaraki, Masoud, Kodama, Hiroaki |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2020
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7853622/ https://www.ncbi.nlm.nih.gov/pubmed/33553860 http://dx.doi.org/10.1021/acsomega.0c05254 |
Ejemplares similares
-
The Many Faces of Amphipathic Helices
por: Giménez-Andrés, Manuel, et al.
Publicado: (2018) -
Membrane Proteins: Structure, Function and Motion
por: Jelokhani-Niaraki, Masoud
Publicado: (2022) -
Morphing of Amphipathic Helices to Explore the Activity
and Selectivity of Membranolytic Antimicrobial Peptides
por: Müller, Alex T., et al.
Publicado: (2020) -
Importance of Tryptophan in Transforming an Amphipathic Peptide into a Pseudomonas aeruginosa-Targeted Antimicrobial Peptide
por: Zhu, Xin, et al.
Publicado: (2014) -
Anti-plasmodial action of de novo-designed, cationic, lysine-branched, amphipathic, helical peptides
por: Kaushik, Naveen K, et al.
Publicado: (2012)