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Hydrophobic Interactions as Substitutes for a Conserved Disulfide Linkage in the Type IIa Bacteriocins, Leucocin A and Pediocin PA‐1
Author(s) -
Derksen Darren J.,
Boudreau Marc A.,
Vederas John C.
Publication year - 2008
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.200800272
Subject(s) - disulfide bond , chemistry , bacteriocin , stereochemistry , disulfide linkage , hydrophobic effect , amino acid , non covalent interactions , biochemistry , antimicrobial , organic chemistry , molecule , cysteine , hydrogen bond , enzyme
High and dry : Three analogues of leucocin A (shown in figure) and six analogues of pediocin PA‐1 were synthesized in which conserved cysteines that form a disulfide bond were replaced by pairs of hydrophobic amino acids. Noncovalent hydrophobic interactions in all of the LeuA derivatives effectively replaced the disulfide and afforded peptides with full antimicrobial activity. In contrast, all of the Ped derivatives were inactive except for 5 d .