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

Author(s): Eun-Rhan Woo, Dong Gun Lee, Young-Su Chang, Yoonkyung Park, Kyung-Soo Hahm.

Journal Name: Protein & Peptide Letters

Volume 9 , Issue 6 , 2002

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Abstract:

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.

Keywords: hp(2-20), broad-spectrum microbicidal activity, virus-cell fusion inhibitory activity

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Article Details

VOLUME: 9
ISSUE: 6
Year: 2002
Page: [477 - 486]
Pages: 10
DOI: 10.2174/0929866023408463
Price: $58

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