Plasmonic Nanosensors for the Determination of Drug Effectiveness on Membrane Receptors
Source abstract
Abstract
We demonstrate the potential of the NanoSPR (nanoscale surface plasmon resonance sensors) method as a simple and cheap tool for the quantitative study of membrane protein-protein interactions. We use NanoSPR to determine the effectiveness of two potential drug candidates that inhibit the protein complex formation between FtsA and ZipA at initial stages of bacterial division. As the NanoSPR method relies on individual gold nanorods as sensing elements, there is no need for fluorescent labels or organic cosolvents, and it provides intrinsically high statistics. NanoSPR could become a powerful tool in drug development, drug delivery, and membrane studies.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Advanced biosensing and bioanalysis techniques · Bacteriophages and microbial interactions · Monoclonal and Polyclonal Antibodies Research
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Institute of Physical Chemistry, University of Mainz, Duesbergweg 10-14, D-55128 Mainz, Germany
Graduate School Materials Science in Mainz, Staudingerweg 9, D-55128 Mainz, Germany
Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Cientı́ficas, c/Ramiro de Maeztu 9, 28040 Madrid, Spain
Funding
European Research Council · Ministerio de Economía y Competitividad · Graduate School of Excellence Materials Science In Mainz
References (29)
Show source-provided references
1. 10.1038/nrmicro294910.1038/nrmicro2949 ↗
2. 10.1016/j.cmi.2016.01.01210.1016/j.cmi.2016.01.012 ↗
3. 10.1126/science.aad329210.1126/science.aad3292 ↗
4. 10.4155/fmc-2016-002710.4155/fmc-2016-0027 ↗
5. 10.1016/j.pharmthera.2016.01.01010.1016/j.pharmthera.2016.01.010 ↗
6. 10.1074/jbc.M112.38895910.1074/jbc.M112.388959 ↗
7. 10.1016/j.bbamem.2013.04.02810.1016/j.bbamem.2013.04.028 ↗
8. 10.1016/j.cbpa.2015.10.03210.1016/j.cbpa.2015.10.032 ↗
9. 10.3390/ijms16102491810.3390/ijms161024918 ↗
10. 10.1021/nl501865p10.1021/nl501865p ↗
11. 10.1038/nmat216210.1038/nmat2162 ↗
12. 10.1021/nl034372s10.1021/nl034372s ↗
13. 10.1103/PhysRevLett.88.07740210.1103/PhysRevLett.88.077402 ↗
14. 10.1016/j.nantod.2009.04.00110.1016/j.nantod.2009.04.001 ↗
15. 10.1038/nrd251010.1038/nrd2510 ↗
16. 10.1074/jbc.R113.47951910.1074/jbc.R113.479519 ↗
17. 10.1046/j.1365-2958.1999.01322.x10.1046/j.1365-2958.1999.01322.x ↗
18. 10.1093/emboj/19.13.317910.1093/emboj/19.13.3179 ↗
19. 10.1016/j.ab.2003.08.03310.1016/j.ab.2003.08.033 ↗
20. 10.1021/nl401354f10.1021/nl401354f ↗
21. 10.1113/jphysiol.1910.sp00136610.1113/jphysiol.1910.sp001366 ↗
22. 10.1529/biophysj.105.06019410.1529/biophysj.105.060194 ↗
23. 10.1016/0006-2952(73)90196-210.1016/0006-2952(73)90196-2 ↗
24. 10.1111/j.1476-5381.2009.00604.x10.1111/j.1476-5381.2009.00604.x ↗
25. 10.1074/jbc.M113.49168810.1074/jbc.M113.491688 ↗
26. 10.1038/ncb288510.1038/ncb2885 ↗
27. 10.1021/nl204496g10.1021/nl204496g ↗
28. 10.1074/jbc.275.16.1174010.1074/jbc.275.16.11740 ↗
29. 10.1021/bi101495x10.1021/bi101495x ↗