rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
6
|
pubmed:dateCreated |
2004-3-15
|
pubmed:abstractText |
We report the synthesis and the functional studies of multiple crown alpha-helical peptides designed to form artificial ion channels. The approach combines the versatility of solid phase peptide synthesis, the conformational predictability of peptidic molecules, and the solution synthesis of crown ethers with engineerable ion-binding abilities. Several biophysical methods were employed to characterize the activity and the mode of action of these crown peptide nanostructures. The 21 residue peptides bearing six 21-EC-7 turned out to facilitate the translocation of ions in a similar fashion to natural ion channels.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0968-0896
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
12
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1279-90
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:15018900-Breast Neoplasms,
pubmed-meshheading:15018900-Cell Division,
pubmed-meshheading:15018900-Crown Ethers,
pubmed-meshheading:15018900-Female,
pubmed-meshheading:15018900-Humans,
pubmed-meshheading:15018900-Ion Channels,
pubmed-meshheading:15018900-Leukemia,
pubmed-meshheading:15018900-Lipid Bilayers,
pubmed-meshheading:15018900-Membranes, Artificial,
pubmed-meshheading:15018900-Microbial Sensitivity Tests,
pubmed-meshheading:15018900-Models, Molecular,
pubmed-meshheading:15018900-Peptide Fragments,
pubmed-meshheading:15018900-Phosphatidylcholines,
pubmed-meshheading:15018900-Protein Conformation,
pubmed-meshheading:15018900-Structure-Activity Relationship,
pubmed-meshheading:15018900-Tumor Cells, Cultured
|
pubmed:year |
2004
|
pubmed:articleTitle |
Design, synthesis, and characterization of peptide nanostructures having ion channel activity.
|
pubmed:affiliation |
Département de chimie and Centre de recherche sur la fonction, la structure et l'ingénierie des protéines, Faculté des sciences et de génie, Université Laval, Québec, Canada G1K 7P4.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|