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Cationic peptides structure-activity relationships

Structure-activity relationship studies investigating the antimicrobial activities of host defense peptides have primarily sought the characterization of the specific sequence/structural motifs that dictate antimicrobial and cytotoxic activities. Perhaps unsurprisingly these activities appear to be dictated by a delicate balance of cationicity, hydrophobicity, amphipathicity, and ultimately the structural characteristics of the peptides. [Pg.187]

Powers, J-P.S., Rozek, A. and Hancock, I.R.E.W. (2004). Structure-activity relationships for the P-hairpin cationic antimicrobial peptide polyphemusin I. Biochim. Biophys. Acta Proteins Proteomics 1698(2) 239-250. [Pg.111]


See other pages where Cationic peptides structure-activity relationships is mentioned: [Pg.189]    [Pg.127]    [Pg.255]    [Pg.205]    [Pg.324]    [Pg.206]    [Pg.176]    [Pg.188]    [Pg.427]    [Pg.177]    [Pg.231]    [Pg.128]    [Pg.424]    [Pg.333]    [Pg.11]    [Pg.198]   
See also in sourсe #XX -- [ Pg.482 ]




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