Open AccessEasy Strategy To Protect Antimicrobial Peptides from Fast Degradation in Serum
Author(s) -
Daniel Knappe,
Petra Henklein,
Ralf Hoffmann,
Kai Hilpert
Publication year - 2010
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.00300-10
Subject(s) - antimicrobial , proteases , peptide , antimicrobial peptides , biochemistry , chemistry , arginine , amino acid , amino acid residue , peptide sequence , enzyme , organic chemistry , gene
Antimicrobial peptides are promising novel peptide leads, but their low serum stability often limits their further consideration in drug development programs. Here, we describe a generally applicable strategy to stabilize peptides against serum proteases by replacing arginine residues with α-amino-3-guanidino-propionic acid (Agp). Peptide NH2 -RRWRIVVIRVRR-CONH2 was nearby totally degraded after 8 h in mouse serum, whereas the variant with Agp substituted was degraded less than 20%. The antimicrobial activity was not affected.