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- Title
Arginine/Tryptophan‐Rich Cyclic α/β‐Antimicrobial Peptides: The Roles of Hydrogen Bonding and Hydrophobic/Hydrophilic Solvent‐Accessible Surface Areas upon Activity and Membrane Selectivity.
- Authors
Bagheri, Mojtaba; Amininasab, Mehriar; Dathe, Margitta
- Abstract
Abstract: The bacterial selectivity of an amphiphilic library of small cyclic α/β‐tetra‐, α/β‐penta‐, and α/β‐hexapeptides rich in arginine/tryptophan (Arg/Trp) residues, which contains asymmetric backbone configurations and differ in hydrophobicity and alternating d,l‐amino acids, was investigated against Bacillus subtilis and Escherichia coli. The structural analyses showed that the peptides tend to form assemblies of different shapes. All‐ l‐peptides, especially the most hydrophobic pentamers, were more strongly anti‐B. subtilis. With the exception to cyclo(Phe‐ d‐Trp‐β3hArg‐Arg‐ d‐Trp) (Phe=phenylalanine), the peptides had no effects on inner membrane of E. coli, but lyzed the lipopolysaccharide layer according to their activity pattern. The activities adversely changed with a decrease in the number of amide intramolecular hydrogen bonds in assemblies of diastereomeric peptides and the ratio of hydrophobic/hydrophilic solvent‐accessible surface areas. The remarkable enhanced entropic contribution for the partitioning of the least conformationally constrained cyclo(Trp‐ d‐Phe‐β3hTrp‐Arg‐ d‐Arg) sequence into the membranes supported the strong self‐assembly behavior, therefore making the peptide less penetrable through the E. coli outer layer.
- Subjects
ARGININE; TRYPTOPHAN; ANTIMICROBIAL peptides; HYDROGEN bonding; POLAR solvents; MEMBRANE selectivity (Technology)
- Publication
Chemistry - A European Journal, 2018, Vol 24, Issue 53, p14242
- ISSN
0947-6539
- Publication type
Article
- DOI
10.1002/chem.201802881