Linked Life Data

20196123

Source:http://linkedlifedata.com/resource/pubmed/id/20196123

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-3-11
pubmed:abstractText
A series of Trp and Arg analogs of antibacterial indolicidin (Ind) was synthesized and the antimicrobial and hemolytic activities were investigated. [L(9)]Ind, [L(11)]Ind, [K(8),L(9)]Ind and [K(6, 8),L(9)]Ind showed desirable characteristics, exhibiting negligible hemolytic activity while keeping strong antibacterial activity. The results indicated that the Trp residue at position 11 essentially contributes to both activities and one can not be exchanged for the other, whereas the Trp residues at positions 4 and 9 play important roles in antimicrobial and hemolytic activities, respectively. The Trp residues at positions 6 and 8 play no important roles in biological activities. We then found that the retro analog of Ind showed higher antibacterial activity than Ind against both Gram-positive and Gram-negative bacteria but remarkably lower hemolytic activity than that of Ind.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1099-1387
pubmed:author
pubmed:copyrightInfo
Copyright (c) 2010 European Peptide Society and John Wiley & Sons, Ltd.
pubmed:issnType
Electronic
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-7
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Structure-activity relationship of indolicidin, a Trp-rich antibacterial peptide.
pubmed:affiliation
Department of Chemistry, Faculty of Science, Fukuoka University, Jonan-ku, Fukuoka, Japan. andos@fukuoka-u.ac.jp
pubmed:publicationType
Journal Article