Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes.
Biochim Biophys Acta Biomembr
; 1860(6): 1414-1423, 2018 Jun.
Article
en En
| MEDLINE
| ID: mdl-29621496
ABSTRACT
Hydrophobic interactions govern specificity for natural antimicrobial peptides. No such relationship has been established for synthetic peptoids that mimic antimicrobial peptides. Peptoid macrocycles synthesized with five different aromatic groups are investigated by minimum inhibitory and hemolytic concentration assays, epifluorescence microscopy, atomic force microscopy, and X-ray reflectivity. Peptoid hydrophobicity is determined using high performance liquid chromatography. Disruption of bacterial but not eukaryotic lipid membranes is demonstrated on the solid supported lipid bilayers and Langmuir monolayers. X-ray reflectivity studies demonstrate that intercalation of peptoids with zwitterionic or negatively charged lipid membranes is found to be regulated by hydrophobicity. Critical levels of peptoid selectivity are demonstrated and found to be modulated by their hydrophobic groups. It is suggested that peptoids may follow different optimization schemes as compared to their natural analogues.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Péptidos Catiónicos Antimicrobianos
/
Lípidos de la Membrana
Límite:
Humans
Idioma:
En
Año:
2018
Tipo del documento:
Article