Linked Life Data

12147359

Source:http://linkedlifedata.com/resource/pubmed/id/12147359

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2002-7-30
pubmed:abstractText
HP (2-20) (AKKVFKRLEKLFSKIQNDK) is the antimicrobial sequence derived from the N-terminus of Helicobacter pylori ribosomal protein L1 (RPL1). In order to develop novel antibiotic peptides useful as therapeutic agents, potent antibiotic activities against bacteria, fungi and cancer cells without a cytotoxic effect are essential. To this end, several analogues with amino acid substitutions were designed to increase or decrease only the net hydrophobicity. In particular, the substitution of Trp for the hydrophobic amino acids, Gln and Asp at positions 17 and 19 of HP (2-20) (Anal 3), caused a dramatic increase in antibiotic activity without a hemolytic effect. In contrast, the decrease of hydrophobicity brought about by substituting Ser for Leu and Phe at positions 12 and 19 of HP (2-20), respectively (Anal 4, Anal 5), did not have a significant effect on the antibiotic activity. The antibiotic effects of these synthetic peptides were further investigated by treating prepared protoplasts of Candida albicans and conducting an artificial liposomal vesicle (PC/PS; 3:1, w/w) disrupting activity test. The results demonstrated that the Anal 3 prevented the regeneration of fungal cell walls and induced an enhanced release of fluorescent dye (carboxyfluorescein) trapped in the artificial membrane vesicles to a greater degree than HP (2-20). The potassium-release test conducted on C. albicans indicated that Anal 3 induced greater amounts of potassium ion to be released than the parent peptide, HP (2-20) did. These results indicated that the hydrophobic region of peptides is prerequisite for its effective antibiotic activity and may facilitate easy penetration of the lipid bilayers of the cell membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
1598
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
185-94
pubmed:dateRevised
2009-11-3
pubmed:meshHeading
pubmed-meshheading:12147359-Amino Acid Sequence, pubmed-meshheading:12147359-Animals, pubmed-meshheading:12147359-Anti-Bacterial Agents, pubmed-meshheading:12147359-Antineoplastic Agents, pubmed-meshheading:12147359-Bacillus subtilis, pubmed-meshheading:12147359-Bacterial Proteins, pubmed-meshheading:12147359-Drug Design, pubmed-meshheading:12147359-Escherichia coli, pubmed-meshheading:12147359-Helicobacter pylori, pubmed-meshheading:12147359-Hemolysis, pubmed-meshheading:12147359-Humans, pubmed-meshheading:12147359-Microbial Sensitivity Tests, pubmed-meshheading:12147359-Molecular Sequence Data, pubmed-meshheading:12147359-Peptide Fragments, pubmed-meshheading:12147359-Peptides, pubmed-meshheading:12147359-Protein Structure, Secondary, pubmed-meshheading:12147359-Ribosomal Proteins, pubmed-meshheading:12147359-Structure-Activity Relationship, pubmed-meshheading:12147359-Tumor Cells, Cultured
pubmed:year
2002
pubmed:articleTitle
Design of novel analogue peptides with potent antibiotic activity based on the antimicrobial peptide, HP (2-20), derived from N-terminus of Helicobacter pylori ribosomal protein L1.
pubmed:affiliation
Research Center for Proteineous Materials, Chosun University, 375 Seosuk-Dong, Dong-Ku, Kwangju, South Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't