Linked Life Data

20942387

Source:http://linkedlifedata.com/resource/pubmed/id/20942387

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2011-4-18
pubmed:abstractText
The development of a general approach for the nondestructive chemical and biological functionalization of graphene could expand opportunities for graphene in both fundamental studies and a variety of device platforms. Graphene is a delicate single-layer, two-dimensional network of carbon atoms whose properties can be affected by covalent modification. One method for functionalizing materials without fundamentally changing their inherent structure is using biorecognition moieties. In particular, oligopeptides are molecules containing a broad chemical diversity that can be achieved within a relatively compact size. Phage display is a dominant method for identifying peptides that possess enhanced selectivity toward a particular target. Here, we demonstrate a powerful yet benign approach for chemical functionalization of graphene via comprehensively screened phage displayed peptides. Our results show that graphene can be selectively recognized even in nanometer-defined strips. Further, modification of graphene with bifunctional peptides reveals both the ability to impart selective recognition of gold nanoparticles and the development of an ultrasensitive graphene-based TNT sensor. We anticipate that these results could open exciting opportunities in the use of graphene in fundamental biochemical recognition studies, as well as applications ranging from sensors to energy storage devices.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1530-6992
pubmed:author
pubmed:issnType
Electronic
pubmed:day
10
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4559-65
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Chemical functionalization of graphene enabled by phage displayed peptides.
pubmed:affiliation
Department of Mechanical and Aerospace Engineering, Princeton University, Princeton, New Jersey 08544, United States.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't