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Rational Design of Oncocin Derivatives with Superior Protease Stabilities and Antibacterial Activities Based on the High‐Resolution Structure of the Oncocin‐DnaK Complex
Author(s) -
Knappe Daniel,
Zahn Michael,
Sauer Ute,
Schiffer Guido,
Sträter Norbert,
Hoffmann Ralf
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000792
Subject(s) - proteases , protease , rational design , peptide , computational biology , chemistry , escherichia coli , drug design , stereochemistry , biochemistry , combinatorial chemistry , enzyme , biology , genetics , gene
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.