Linked Life Data

10559740

Source:http://linkedlifedata.com/resource/pubmed/id/10559740

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-1-21
pubmed:abstractText
Synthetic materials capable of specifically recognizing proteins are important in separations, biosensors, and biomaterials. In this study, polysaccharide-like surfaces with tailored protein-binding nanocavities were prepared by a novel templating approach based on radiofrequency plasma deposition of thin films. The template-imprinted proteins included albumin, immunoglobulin, fibrinogen, lysozyme, ribonuclease A, alpha-lactalbumin, and glutamine synthetase. Transmission electron microscopy showed that nanometer-sized "pits" in the shape of imprinted protein were formed on the surfaces of template-imprinted polymer films. Electron spectroscopy for chemical analysis and time-of-flight secondary ion mass spectrometry indicated the saccharide covering of imprint surfaces and the removal of template proteins. (125)I-labeled protein adsorption from single solutions showed a similar amount of protein was adsorbed to its own imprint as to the imprint of another protein. However, more protein remained on the former surface than on the latter following elution with the detergents Tween 20 or sodium dodecyl sulfate. Competitive adsorption of a binary protein mixture showed a highly preferential adsorption of template protein to the corresponding imprint. This template recognition diminished as the number of protein-imprinted pits decreased. Structurally unstable proteins such as alpha-lactalbumin exhibited weaker template recognition that "robust" proteins such as lysozyme. The hypothesis that protein recognition is due to complementarity between the protein and its imprinted nanopit was supported by protein turnover experiments that showed template protein adsorbed to its own imprint was less readily displaced by a nontemplate protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9304
pubmed:author
pubmed:copyrightInfo
Copyright 2000 John Wiley & Sons, Inc.
pubmed:issnType
Print
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-11
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Template recognition of protein-imprinted polymer surfaces.
pubmed:affiliation
Department of Bioengineering, University of Washington, Box 351720, Seattle, Washington 98195, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't