Back to Search
Start Over
Development of helix-stabilized antimicrobial peptides composed of lysine and hydrophobic α,α-disubstituted α-amino acid residues
- Source :
- Bioorganic & Medicinal Chemistry Letters. 27:3950-3953
- Publication Year :
- 2017
- Publisher :
- Elsevier BV, 2017.
-
Abstract
- Lysine-based amphipathic nonapeptides, including homochiral peptides [Ac-(l-Lys-l-Lys-Xaa)3-NH2 (Xaa=Gly, Ala, Aib, Ac5c, or Ac6c) and Ac-(d-Lys-d-Lys-Aib)3-NH2], a heterochiral peptide [Ac-(l-Lys-d-Lys-Aib)3-NH2], and a racemic mixture of diastereomeric peptides [Ac-(rac-Lys-rac-Lys-Aib)3-NH2] were designed and synthesized to investigate the relationship between their preferred secondary structures and their antimicrobial activity. Peptide 5, [Ac-(l-Lys-l-Lys-Ac6c)3-NH2] formed a stable α-helical structure and exhibited strong activity against Gram-negative bacteria (Escherichia coli and Pseudomonas aeruginosa).
- Subjects :
- Circular dichroism
Stereochemistry
Clinical Biochemistry
Lysine
Antimicrobial peptides
Pharmaceutical Science
Peptide
Microbial Sensitivity Tests
010402 general chemistry
medicine.disease_cause
01 natural sciences
Biochemistry
Structure-Activity Relationship
Drug Discovery
Escherichia coli
medicine
Amino Acids
Molecular Biology
chemistry.chemical_classification
Dose-Response Relationship, Drug
Molecular Structure
010405 organic chemistry
Organic Chemistry
Diastereomer
0104 chemical sciences
chemistry
Pseudomonas aeruginosa
Helix
Molecular Medicine
Racemic mixture
Antimicrobial Cationic Peptides
Subjects
Details
- ISSN :
- 0960894X
- Volume :
- 27
- Database :
- OpenAIRE
- Journal :
- Bioorganic & Medicinal Chemistry Letters
- Accession number :
- edsair.doi.dedup.....002d9343c71e19697ac2ea6799ebaf2d