Chemoenzymatic modification of daptomycin's lipopeptide structure created hybrid antibiotics with novel activity profiles, revealing structure-activity relationships for this clinically important cyclic peptide antibiotic class.
Key findingChemoenzymatic design of daptomycin-related acidic lipopeptides created hybrid antibiotics with modified activity profiles, revealing SAR rules for th
What the researchers found
Chemoenzymatic design of daptomycin-related acidic lipopeptides created hybrid antibiotics with modified activity profiles, revealing SAR rules for the daptomycin macrocyclic core and advancing next-generation cyclic lipopeptide antibiotic design.
Why it matters
Relevant for cyclic-peptides, antimicrobial-peptides, peptide-design.
How the study worked
in-vitro study on cyclic-peptides, antimicrobial-peptides.
What this study cannot tell us
See abstract.
How to read the evidence
preliminary evidence.
When this study was published
Published in 2006.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
- Clinical translation to evaluate.
Common questions
What was studied?
What was found?
Read the original research
Chemoenzymatic design of acidic lipopeptide hybrids: new insights into the structure-activity relationship of daptomycin and A54145.
Biochemistry, 45(35), 10474-81
Citation
Kopp, Florian; Grünewald, Jan; Mahlert, Christoph; Marahiel, Mohamed A. (2006). Chemoenzymatic design of acidic lipopeptide hybrids: new insights into the structure-activity relationship of daptomycin and A54145.. Biochemistry, 45(35), 10474-81.