Biological role of an arginine residue present in a histidine-rich peptide which inhibits hemagglutination of Porphyromonas gingivalis.
Inhibitory effects of synthetic fragments in histatin 8, having the sequence Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr, on hemagglutination by Porphyromonas gingivalis 381 were examined. The hemagglutinating activity was reduced much more by the peptide Lys-His-His-Ser-His-Arg-Gly-Tyr than by the peptides Lys-His-His-Ser-His and/or Lys-Phe-His-Glu-Lys. These results suggest that the arginine residue may have an important role in the inhibition of hemagglutination by P. gingivalis.
Murakami
Y
Y
Department of Preventive Dentistry, Faculty of Dentistry, Osaka University, Japan.
Tamagawa
H
H
Shizukuishi
S
S
Tsunemitsu
A
A
Aimoto
S
S
D000595:Amino Acid Sequence; D006384:Hemagglutination / Q000187:drug effects*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology*; D016966:Porphyromonas gingivalis / Q000187:drug effects* / Q000276:immunology; D011506:Proteins / Q000737:chemistry / Q000494:pharmacology*; D012471:Salivary Proteins and Peptides / Q000737:chemistry / Q000494:pharmacology; D013329:Structure-Activity Relationship; D000099053:Histidine-Rich Glycoprotein
D010446:Peptide Fragments; D011506:Proteins; D012471:Salivary Proteins and Peptides; D000099053:Histidine-Rich Glycoprotein