Homology similarity analysis of sequences of lactoferricin and its derivatives.
A new method, homology similarity analysis (HSA), was developed to investigate homology pattern similarities of selected segments within sequences of peptides. This new approach facilitated elucidation of the structure-function relationships of lactoferricin derivatives. Helix propensity of positions 4-9 in the lactoferricin sequence was the most important in determining the antimicrobial activity of lactoferricin against Escherichia coli, followed by cationic charge pattern at positions 4-9 and 1-3. The pattern similarity of segments within sequences could be a useful tool for representing the distribution attributes of amino acid residue properties to the structure-function relationships of proteins and peptides, especially when used in conjunction with principal component similarity analysis followed by the regression version of artificial neural networks.
Nakai
Shuryo
S
Food, Nutrition, and Health Program, Faculty of Agricultural Sciences, The University of British Columbia, 6650 N.W. Marine Drive, Vancouver, Canada V6T 1Z4. nakai@interchange.ubc.ca
Chan
Judy C K
JC
Li-Chan
Eunice C Y
EC
Dou
Jinglie
J
Ogawa
Masahiro
M
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects; D007781:Lactoferrin / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000494:pharmacology; D008969:Molecular Sequence Data; D016571:Neural Networks, Computer; D010455:Peptides; D012044:Regression Analysis; D017385:Sequence Homology
D000900:Anti-Bacterial Agents; D010455:Peptides; C082171:lactoferricin B; D007781:Lactoferrin