TY - JOUR
T1 - Protegrin structure-activity relationships
T2 - Using homology models of synthetic sequences to determine structural characteristics important for activity
AU - Ostberg, Nathan
AU - Kaznessis, Yiannis
PY - 2005/2/1
Y1 - 2005/2/1
N2 - The protegrin family of antimicrobial peptides is among the shortest in sequence length while remaining very active against a variety of microorganisms. The major goal of this study is to characterize easily calculated molecular properties, which quantitatively show high correlation with antibacterial activity. The peptides studied have high sequence similarity but vary in activity over more than an order of magnitude. Hence, sequence analysis alone cannot be used to predict activity for these peptides. We calculate structural properties of 62 protegrin and protegrin-analogue peptides and correlate them to experimental activities against six microbe species, as well as hemolytic and cytotoxic activities. Natural protegrins structures were compared with synthetic derivatives using homology modeling, and property descriptors were calculated to determine the characteristics that confer their antimicrobial activity. A structure-activity relationship study of all these peptides provides information about the structural properties that affect activity against different microbial species.
AB - The protegrin family of antimicrobial peptides is among the shortest in sequence length while remaining very active against a variety of microorganisms. The major goal of this study is to characterize easily calculated molecular properties, which quantitatively show high correlation with antibacterial activity. The peptides studied have high sequence similarity but vary in activity over more than an order of magnitude. Hence, sequence analysis alone cannot be used to predict activity for these peptides. We calculate structural properties of 62 protegrin and protegrin-analogue peptides and correlate them to experimental activities against six microbe species, as well as hemolytic and cytotoxic activities. Natural protegrins structures were compared with synthetic derivatives using homology modeling, and property descriptors were calculated to determine the characteristics that confer their antimicrobial activity. A structure-activity relationship study of all these peptides provides information about the structural properties that affect activity against different microbial species.
KW - Antimicrobial peptide
KW - Homology modeling
KW - Structure-activity relationships
UR - http://www.scopus.com/inward/record.url?scp=11144242839&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=11144242839&partnerID=8YFLogxK
U2 - 10.1016/j.peptides.2004.09.020
DO - 10.1016/j.peptides.2004.09.020
M3 - Article
C2 - 15629531
AN - SCOPUS:11144242839
SN - 0196-9781
VL - 26
SP - 197
EP - 206
JO - Peptides
JF - Peptides
IS - 2
ER -