Stach, Michaela; Maillard, Noélie; Kadam, Rameshwar; Kalbermatter, David; Meury, M.; Page, Malcolm; Fotiadis, Dimitrios José; Darbre, Tamis; Reymond, Jean-Louis (2012). Membrane disrupting antimicrobial peptide dendrimers with multiple amino termini. Medicinal chemistry communications - MedChemComm, 3(1), pp. 86-89. Cambridge: Royal Society of Chemistry 10.1039/c1md00272d
Full text not available from this repository.Antimicrobial peptide dendrimer H1 Leu8(Lys-Leu)4(Lys-Phe)2Lys-LysNH2 (Lys = branching lysine) was identified by screening a 6750-membered combinatorial library by the bead-diffusion assay. Sequence variations also revealed dendrimer bH1 Leu8(Dap-Leu)4(Dap-Phe)2Dap-LysNH2 (Dap = branching 2,3-diaminopropanoic acid) as a more potent analog. H1 and bH1 showed good antimicrobial activities mediated by membrane disruption (MIC = 2–4 μg mL−1 on Bacillus subtilis and Escherichia coli) but low hemolytic activity (MHC = 310 μg mL−1 respectively >2000 μg mL−1).
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP) 04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine |
UniBE Contributor: |
Stach, Michaela, Maillard, Noélie, Kadam, Rameshwar, Kalbermatter, David, Meury, Marcel, Page, Malcolm, Fotiadis, Dimitrios José, Darbre, Tamis, Reymond, Jean-Louis |
Subjects: |
500 Science > 570 Life sciences; biology 500 Science > 540 Chemistry 600 Technology > 610 Medicine & health |
ISSN: |
2040-2503 |
Publisher: |
Royal Society of Chemistry |
Language: |
English |
Submitter: |
Factscience Import |
Date Deposited: |
04 Oct 2013 14:37 |
Last Modified: |
05 Dec 2022 14:11 |
Publisher DOI: |
10.1039/c1md00272d |
Web of Science ID: |
000299975300015 |
URI: |
https://boris.unibe.ch/id/eprint/14798 (FactScience: 221922) |
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