Skip to main content

News about Scitation

In December 2016 Scitation will launch with a new design, enhanced navigation and a much improved user experience.

To ensure a smooth transition, from today, we are temporarily stopping new account registration and single article purchases. If you already have an account you can continue to use the site as normal.

For help or more information please visit our FAQs.

banner image
No data available.
Please log in to see this content.
You have no subscription access to this content.
No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.
The full text of this article is not currently available.
/content/aip/journal/jcp/143/6/10.1063/1.4928455
1.
1.O. Sadik, W. Land, and J. Wang, Electroanalysis 15, 1149 (2003).
http://dx.doi.org/10.1002/elan.200390140
2.
2.A. A. Ellington, I. J. Kullo, K. R. Bailey, and G. G. Klee, Clin. Chem. 56, 186 (2010).
http://dx.doi.org/10.1373/clinchem.2009.127514
3.
3.B. H. Garcia II, A. Hargrave, A. Morgan, G. Kilmer, E. Hommema, J. Nahrahari, B. Webb, and R. Wiese, J. Biomol. Tech. 18, 245 (2007).
4.
4.P. Pavlickova, E. Schneider, and H. Hug, Clin. Chim. Acta 343, 17 (2004).
http://dx.doi.org/10.1016/j.cccn.2004.01.009
5.
5.I. Balboni, S. M. Chan, M. Kattah, J. D. Tenenbaum, A. J. Butte, and P. J. Utz, Annu. Rev. Immunol. 24, 391 (2006).
http://dx.doi.org/10.1146/annurev.immunol.24.021605.090709
6.
6.P. Angenendt, J. Glokler, J. Sobek, H. Lehrach, and D. Cahill, J. Chromatogr. A 1009, 97 (2003).
http://dx.doi.org/10.1016/S0021-9673(03)00769-6
7.
7.P. Angenendt, Drug Discovery Today 10, 503 (2005).
http://dx.doi.org/10.1016/S1359-6446(05)03392-1
8.
8.A. Hucknall, D.-H. Kim, S. Rangarajan, R. T. Hill, W. M. Reichert, and A. Chilkoti, Adv. Mater. 21, 1968 (2009).
http://dx.doi.org/10.1002/adma.200803125
9.
9.P. Angenendt, J. Glokler, D. Murphy, H. Lehrach, and D. J. Cahill, Anal. Biochem. 309, 253 (2002).
http://dx.doi.org/10.1016/S0003-2697(02)00257-9
10.
10.T. S. Tsapikouni and Y. F. Missirlis, Mater. Sci. Eng. B 152, 2 (2008).
http://dx.doi.org/10.1016/j.mseb.2008.06.007
11.
11.A. P. Le Brun, S. A. Holt, D. S. Shah, C. F. Majkrzak, and J. H. Lakey, Eur. Biophys. J. 37, 639 (2008).
http://dx.doi.org/10.1007/s00249-008-0291-2
12.
12.S. Wei and T. A. Knotts IV, J. Chem. Phys. 134, 185101 (2011).
http://dx.doi.org/10.1063/1.3589863
13.
13.S. Wei and T. A. Knotts IV, J. Chem. Phys. 133, 115102 (2010).
http://dx.doi.org/10.1063/1.3479039
14.
14.B. K. Loong and T. A. Knotts IV, J. Chem. Phys. 141, 051104 (2014).
http://dx.doi.org/10.1063/1.4891971
15.
15.S.-W. Hung, P.-Y. Hsiao, M.-C. Lu, and C.-C. Chieng, J. Phys. Chem. B 116, 12661 (2012).
http://dx.doi.org/10.1021/jp304695w
16.
16.R. B. Pandey, Z. Kuang, B. L. Farmer, S. S. Kim, and R. R. Naik, Soft Matter 8, 9101 (2012).
http://dx.doi.org/10.1039/c2sm25870f
17.
17.L. J. Harris, S. B. Larson, K. W. Hasel, and A. McPherson, Biochemistry 36, 1581 (1997).
http://dx.doi.org/10.1021/bi962514+
18.
18.S. Wei and T. A. Knotts IV, J. Chem. Phys. 139, 095102 (2013).
http://dx.doi.org/10.1063/1.4819131
19.
19.J. Karanicolas and C. Brooks, J. Mol. Biol. 334, 309 (2003).
http://dx.doi.org/10.1016/j.jmb.2003.09.047
20.
20.J. Karanicolas and C. Brooks, Protein Sci. 11, 2351 (2002).
http://dx.doi.org/10.1110/ps.0205402
21.
21.Y. Sugita and Y. Okamoto, Chem. Phys. Lett. 314, 141 (1999).
http://dx.doi.org/10.1016/S0009-2614(99)01123-9
22.
22.M. R. Shirts and J. D. Chodera, J. Chem. Phys. 129, 124105 (2008).
http://dx.doi.org/10.1063/1.2978177
23.
23.See supplementary material at http://dx.doi.org/10.1063/1.4928455 for further details on the simulations, model, and analysis methods.[Supplementary Material]
24.
24.D. Lowe, K. Dudgeon, R. Rouet, P. Schofield, L. Jermutus, and D. Christ, Adv. Protein Chem. Struct. Biol. 84, 4161 (2011).
http://dx.doi.org/10.1016/B978-0-12-386483-3.00004-5
25.
25.K. Zheng, C. Bantog, and R. Bayer, mAbs 3, 568 (2011).
http://dx.doi.org/10.4161/mabs.3.6.17922
26.
26.N. Chennamsetty, V. Voynov, V. Kayser, B. Helk, and B. L. Trout, Proc. Natl. Acad. Sci. U. S. A. 106, 11937 (2009).
http://dx.doi.org/10.1073/pnas.0904191106
27.
27.M. Friedel, A. Baumketner, and J.-E. Shea, Proc. Natl. Acad. Sci. U. S. A. 103, 8396 (2006).
http://dx.doi.org/10.1073/pnas.0601210103
28.
28.M. Friedel, A. Baumketner, and J.-E. Shea, J. Chem. Phys. 126, 095101 (2007).
http://dx.doi.org/10.1063/1.2464114
29.
29.Y. Jung, J. Y. Jeong, and B. H. Chung, Analyst 133, 697 (2008).
http://dx.doi.org/10.1039/b800014j
30.
30.M. T. Smith, J. C. Wu, C. T. Varner, and B. C. Bundy, Biotechnol. Prog. 29, 247 (2013).
http://dx.doi.org/10.1002/btpr.1671
31.
31.J. C. Y. Wu, C. H. Hutchings, M. J. Lindsay, C. J. Werner, and B. C. Bundy, J. Biotechnol. 193, 83 (2015).
http://dx.doi.org/10.1016/j.jbiotec.2014.10.039
http://aip.metastore.ingenta.com/content/aip/journal/jcp/143/6/10.1063/1.4928455
Loading
/content/aip/journal/jcp/143/6/10.1063/1.4928455
Loading

Data & Media loading...

Loading

Article metrics loading...

/content/aip/journal/jcp/143/6/10.1063/1.4928455
2015-08-11
2016-12-05

Abstract

Antibody microarrays have the potential to revolutionize molecular detection in scientific, medical, and other biosensor applications, but their current use is limited because of poor reliability. It is hypothesized that one reason for their poor performance results from strong antibody-surface interactions that destabilize the antibody structure and create steric interference for antigen recognition. Using a recently developed coarse-grain protein-surface model that has been parameterized against experimental data, antibody-surface interactions for two antibody orientations on two types of surfaces have been investigated. The results show that regardless of attachment geometry, antibodies tend to collapse onto hydrophobic surfaces and exhibit lower overall stability compared to antibodies on hydrophilic surfaces or in bulk solution. The results provide an unprecedented view into the dynamics of antibodies on surfaces and offer new insights into the poor performance exhibited by current antibody microarrays.

Loading

Full text loading...

/deliver/fulltext/aip/journal/jcp/143/6/1.4928455.html;jsessionid=RxJ6i9WPc48eaQeCDYwUW24z.x-aip-live-06?itemId=/content/aip/journal/jcp/143/6/10.1063/1.4928455&mimeType=html&fmt=ahah&containerItemId=content/aip/journal/jcp
true
true

Access Key

  • FFree Content
  • OAOpen Access Content
  • SSubscribed Content
  • TFree Trial Content
752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
/content/realmedia?fmt=ahah&adPositionList=
&advertTargetUrl=//oascentral.aip.org/RealMedia/ads/&sitePageValue=jcp.aip.org/143/6/10.1063/1.4928455&pageURL=http://scitation.aip.org/content/aip/journal/jcp/143/6/10.1063/1.4928455'
Right1,Right2,Right3,