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001 ocn713205230;

003 OCoLC;

005 20141212050504.0;

006 m o d f ;

007 cr mn|||||||||;

008 100915s2009 mdua eob f000 0 eng d;

027 a| ARL-TR-5015;

029 0 a| DTICEb| ADA512469;

035 a| (Sirsi) o713205230;

040 a| DTICEc| DTICEd| GPOd| UtOrBLW;

049 a| ERE#;

074 a| 0324-A-01 (online);

086 0 a| D 101.133:5015;

100 1 a| Stratis-Cullum, Dimitra N.=| ^A1412527;

245 10 a| Affinity probe capillary electrophoresis evaluation of aptamer binding to Campylobacter jejuni bacteria /c| by Dimitra N. Stratis-Cullum, Sun McMasters, and Paul M. Pellegrino.;

260 a| Adelphi, MD :b| Army Research Laboratory,c| [2009];

300 a| 1 online resource (vi, 14 pages) :b| illustrations (some color).;

336 a| text2| rdacontent;

337 a| computer2| rdamedia;

338 a| online resource2| rdacarrier;

490 1 a| ARL-TR ;v| 5015;

513 a| Progress report;b| 2007-2008.;

500 a| Title from title screen (viewed on Nov. 11, 2012).;

500 a| "November 2009.";

504 a| Includes bibliographical references (p. 9-12).;

506 a| APPROVED FOR PUBLIC RELEASE.;

520 a| In this work, we developed a capillary electrophoresis immunoassay to evaluate aptamer binding to bacterial cells. This work is the first known demonstration of aptamer affinity probe capillary electrophoresis to a whole cell target. The aptamer probes investigated were developed against a Campylobacter jejuni bacterial cell target, and we evaluated binding relative to other common food-borne pathogens. Specific binding affinity was evidenced by a pronounced mobility shift and peak broadening with increasing bacteria concentration. Little to no mobility shift was observed for food-borne pathogens, Salmonella typhirium and Escherichia coli, even when increasing concentrations 10-fold over target. These results suggest that affinity probe capillary electrophoresis could be useful for qualitative screening of aptamer candidates to bacterial cell targets.;

650 17 a| Medicine and medical research.2| scgdst;

650 27 a| Microbiology.2| scgdst;

650 17 a| Pathogenic microorganisms.2| dtict;

650 17 a| Jejunum.2| dtict;

650 17 a| Escherichia coli.2| dtict;

650 27 a| Immunoassay.2| scgdst;

650 27 a| Food.2| scgdst;

650 27 a| Bioassay.2| scgdst;

650 27 a| Electrophoresis.2| scgdst;

650 27 a| Salmonella.2| scgdst;

650 27 a| Shifting.2| scgdst;

650 27 a| Capillarity.2| scgdst;

650 27 a| Bacteria.2| scgdst;

650 0 a| Campylobacter jejuni.=| ^A1133125;

650 0 a| Electrophoresis.=| ^A12683;

650 0 a| Immunoassay.=| ^A7166;

653 2 a| APTAMER;

653 2 a| CAMPYLOBACTER JEJUNI;

653 2 a| AFFINITY PROBES;

653 2 a| CAPILLARY ELECTROPHORESIS;

653 2 a| FOOD PATHOGEN;

700 1 a| McMasters, Sun.?| UNAUTHORIZED;

700 1 a| Pellegrino, Paul M.?| UNAUTHORIZED;

710 2 a| U.S. Army Research Laboratory.=| ^A367731;

830 0 a| ARL-TR (Aberdeen Proving Ground, Md.) ;v| 5015.=| ^A566074;

856 40 u| https://purl.fdlp.gov/GPO/gpo31787;

856 40 u| http://handle.dtic.mil/100.2/ADA512469;

949 a| Click on web addressw| ASISh| JOYNER94;

998 a| 3242692;

998 a| u3242692;

596 a| 1;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 3242692-1001l| JNETm| JOYNERr| Ys| Yt| JNE1DOu| 1/10/2013x| EDOCUMENTz| JERESOURCE;

Affinity probe capillary electrophoresis evaluation of aptamer binding to Campylobacter jejuni bacteria / by Dimitra N. Stratis-Cullum, Sun McMasters, and Paul M. Pellegrino.

Author/creator	Stratis-Cullum, Dimitra N.
Other author	McMasters, Sun.
Other author	Pellegrino, Paul M.
Other author	U.S. Army Research Laboratory.
Format	Electronic
Publication Info	Adelphi, MD : Army Research Laboratory, [2009]
Description	1 online resource (vi, 14 pages) : illustrations (some color).
Supplemental Content	https://purl.fdlp.gov/GPO/gpo31787
Supplemental Content	http://handle.dtic.mil/100.2/ADA512469
Subjects	Campylobacter jejuni. Electrophoresis. Immunoassay.

Series	ARL-TR ; 5015 ARL-TR (Aberdeen Proving Ground, Md.) ; 5015. ^A566074
Abstract	In this work, we developed a capillary electrophoresis immunoassay to evaluate aptamer binding to bacterial cells. This work is the first known demonstration of aptamer affinity probe capillary electrophoresis to a whole cell target. The aptamer probes investigated were developed against a Campylobacter jejuni bacterial cell target, and we evaluated binding relative to other common food-borne pathogens. Specific binding affinity was evidenced by a pronounced mobility shift and peak broadening with increasing bacteria concentration. Little to no mobility shift was observed for food-borne pathogens, Salmonella typhirium and Escherichia coli, even when increasing concentrations 10-fold over target. These results suggest that affinity probe capillary electrophoresis could be useful for qualitative screening of aptamer candidates to bacterial cell targets.
General note	Title from title screen (viewed on Nov. 11, 2012).
General note	"November 2009."
Bibliography note	Includes bibliographical references (p. 9-12).
Access restriction	APPROVED FOR PUBLIC RELEASE.
Report note	Progress report; 2007-2008.
Technical rpt#	ARL-TR-5015
GPO item number	0324-A-01 (online)
Govt. docs number	D 101.133:5015

Availability

Library	Location	Call Number	Status	Item Actions
	Electronic Resources	Online Content https://purl.fdlp.gov/GPO/gpo31787 http://handle.dtic.mil/100.2/ADA512469	✔ Available

Affinity probe capillary electrophoresis evaluation of aptamer binding to Campylobacter jejuni bacteria / by Dimitra N. Stratis-Cullum, Sun McMasters, and Paul M. Pellegrino.

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