An intrinsically disordered antimicrobial peptide dendrimer from stereorandomized virtual screening

Membrane-disruptive amphiphilic antimicrobial peptides behave as intrinsically disordered proteins by being unordered in water and becoming α-helical in contact with biological membranes. We recently discovered that synthesizing the α-helical antimicrobial peptide dendrimer L-T25 ((KL)(8)(KKL)(4)(KL...

Descripción completa

Detalles Bibliográficos
Autores principales: Cai, Xingguang, Orsi, Markus, Capecchi, Alice, Köhler, Thilo, van Delden, Christian, Javor, Sacha, Reymond, Jean-Louis
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9780108/
https://www.ncbi.nlm.nih.gov/pubmed/36632208
http://dx.doi.org/10.1016/j.xcrp.2022.101161

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9780108/
https://www.ncbi.nlm.nih.gov/pubmed/36632208
http://dx.doi.org/10.1016/j.xcrp.2022.101161

Ejemplares similares