Rational Design of Oncocin Derivatives with Superior Protease Stabilities and Antibacterial Activities Based on the High-Resolution Structure of the Oncocin-DnaK Complex

Countering MDR pathogens: The proline‐rich designer peptide oncocin is highly active against a number of antibiotic‐resistant, Gram‐negative pathogens. Here we deduce residues critical to its activity and the crystal structure of an oncocin–DnaK complex from a positional Ala scan. New lead compounds...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2011-04, Vol.12 (6), p.874-876
Main Authors: Knappe, Daniel, Zahn, Michael, Sauer, Ute, Schiffer, Guido, Sträter, Norbert, Hoffmann, Ralf
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacokinetics
antibiotics
Antimicrobial Cationic Peptides - chemistry
Antimicrobial Cationic Peptides - pharmacokinetics
Bacteria - metabolism
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Binding Sites
Drug Design
Drug Stability
Half-Life
Mice
Molecular Chaperones - chemistry
Molecular Chaperones - genetics
Molecular Chaperones - metabolism
Molecular Sequence Data
oncocin
peptides
Protein Structure, Tertiary
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Structure-Activity Relationship
structure-activity relationships
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Summary:Countering MDR pathogens: The proline‐rich designer peptide oncocin is highly active against a number of antibiotic‐resistant, Gram‐negative pathogens. Here we deduce residues critical to its activity and the crystal structure of an oncocin–DnaK complex from a positional Ala scan. New lead compounds were highly resistant against serum and E. coli proteases.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201000792