Virus-cell fusion inhibitory activity of novel analogue peptides based on the HP (2-20) derived from N-terminus of Helicobacter pylori Ribosomal Protein L1.
HP (2-20) (AKKVFKRLEKLFSKIQNDK) is the antibacterial sequence derived from N-terminus of Helicobacter pylori Ribosomal Protein L1 (RPL1). It has a broad-spectrum microbicidal activity in vitro that is thought to be related to the membrane-disruptive properties of the peptide. Based on the putative membrane-targeted mode of action, we postulated that HP (2-20) might be possessed virus-cell fusion inhibitory activity. To develop the novel virus-cell fusion inhibitory peptides, several analogues with amino acid substitution were designed to increase or decrease only net hydrophobic region. In particular, substitution of Gln and Asp for hydrophobic amino acid, Trp at position 17 and 19 of HP (2-20) (Anal 3) caused a dramatic increase in virus-cell fusion inhibitory activity without hemolytic effect.
Woo
Eun-Rhan
ER
Research Center for Proteineous Materials, Chosun University, 375 Seosuk-Dong, Dong-Ku, Kwangju 501-759, South Korea.
Lee
Dong Gun
DG
Chang
Young-Su
YS
Park
Yoonkyung
Y
Hahm
Kyung-Soo
KS
D000998:Antiviral Agents / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D001681:Biological Assay; D005818:Genetic Engineering; D006367:HeLa Cells; D016480:Helicobacter pylori / Q000378:metabolism; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D014616:Vaccinia virus / Q000378:metabolism* / Q000472:pathogenicity
D000998:Antiviral Agents; D001426:Bacterial Proteins; C433783:Hp (2-20) protein, Helicobacter pylori; D010446:Peptide Fragments; D010455:Peptides; D012269:Ribosomal Proteins; C028546:ribosomal protein L1