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Using Fluorous Amino Acids to Modulate the Biological Activity of an Antimicrobial Peptide
Author(s) -
Gottler Lindsey M.,
Lee HyangYeol,
Shelburne Charles E.,
Ramamoorthy Ayyalusamy,
Marsh E. Neil G.
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.200700643
Subject(s) - magainin , proteolysis , peptide , antimicrobial , antimicrobial peptides , amino acid , chemistry , biological activity , computational biology , in vivo , biochemistry , combinatorial chemistry , biology , in vitro , microbiology and biotechnology , organic chemistry , enzyme
Leap frog : Antimicrobial peptides based on the structure of the magainin peptides from the African clawed frog have shown great promise as therapeutic agents. However their efficacy in vivo is limited by their susceptibility to proteolysis. We show that incorporating the fluorous amino acid hexafluoroleucine into a magainin analogue (see scheme) dramatically improves stability to proteolysis while retaining biological activity.