Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
2010-9-27
pubmed:abstractText
A cytotoxic peptide, polytheonamide B (pTB), from marine sponge was examined for cytotoxic spectrum and specific activity to mammalian cells was demonstrated. pTB is composed of alternative D- and L-amino acid residues throughout the 48-mer peptide. This suggests the formation of a ?-helix similar to gramicidin channels. Planar bilayer experiments revealed that pTB forms monovalent cation-selective channels, being compatible with the inner pore diameter of ?4Å for a ?-helical structure. pTB penetrated vectorially into the membrane, formed a channel by means of a single molecule, and remained in the membrane. These functional properties may account for specific cytotoxic activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1873-3468
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
24
pubmed:volume
584
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3995-9
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
A cytotoxic peptide from a marine sponge exhibits ion channel activity through vectorial-insertion into the membrane.
pubmed:affiliation
Department of Molecular Physiology and Biophysics, University of Fukui Faculty of Medical Sciences, Fukui, Japan.
pubmed:publicationType
Journal Article