Source:http://linkedlifedata.com/resource/pubmed/id/14966842
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2004-2-17
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pubmed:abstractText |
Secondary ion mass spectrometry (SIMS) for biomolecular analysis is greatly enhanced by the instrumental combination of orthogonal extraction time-of-flight mass spectrometry with massive gold cluster primary ion bombardment. Precursor peptide molecular ion yield enhancements of 1000, and signal-to-noise improvements of up to 20, were measured by comparing SIMS spectra obtained using Au(+) and massive Au(400) (4+) cluster primary ion bombardment of neat films of the neuropeptide fragment dynorphin 1-7. Remarkably low damage cross-sections were also measured from dynorphin 1-7 and gramicidin S during prolonged bombardment with 40 keV Au(400) (4+). For gramicidin S, the molecular ion yield increases slightly as a function of Au(400) (4+) beam fluence up to at least 2 x 10(13) Au(400) (4+)/cm(2). This is in marked contrast to the rapid decrease observed when bombarding with ions such as Au(5) (+) and Au(9) (+). When gramicidin S is impinged with Au(5) (+), the molecular ion yield decreases by a factor of 10 after a fluence of only 8 x 10(12) ions/cm(2). Comparison of these damage cross-sections implies that minimal surface damage occurs during prolonged Au(400) (4+) bombardment. Several practical analytical implications are drawn from these observations.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Dynorphins,
http://linkedlifedata.com/resource/pubmed/chemical/Gastrins,
http://linkedlifedata.com/resource/pubmed/chemical/Gold,
http://linkedlifedata.com/resource/pubmed/chemical/Gramicidin,
http://linkedlifedata.com/resource/pubmed/chemical/Ions,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides
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pubmed:status |
MEDLINE
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pubmed:issn |
0951-4198
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pubmed:author |
pubmed-author:BensaoulaHH,
pubmed-author:CaroffMM,
pubmed-author:Della-NegraSS,
pubmed-author:DepauwJJ,
pubmed-author:FuhrerKK,
pubmed-author:GoninMM,
pubmed-author:JacquesEE,
pubmed-author:LebeyecYY,
pubmed-author:NovikovAA,
pubmed-author:PautratMM,
pubmed-author:SchultzJ AJA,
pubmed-author:TempezAgnèsA,
pubmed-author:UgarovMM,
pubmed-author:WoodsAminaA
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pubmed:copyrightInfo |
Copyright 2004 John Wiley & Sons, Ltd.
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pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
371-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14966842-Dynorphins,
pubmed-meshheading:14966842-Gastrins,
pubmed-meshheading:14966842-Gold,
pubmed-meshheading:14966842-Gramicidin,
pubmed-meshheading:14966842-Ions,
pubmed-meshheading:14966842-Mass Spectrometry,
pubmed-meshheading:14966842-Peptides,
pubmed-meshheading:14966842-Spectrometry, Mass, Secondary Ion
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pubmed:year |
2004
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pubmed:articleTitle |
Orthogonal time-of-flight secondary ion mass spectrometric analysis of peptides using large gold clusters as primary ions.
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pubmed:affiliation |
Ionwerks Inc., 2472 Bolsover St, Suite 255, Houston, TX 77030, USA. agnes@ionwerks.com
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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