journal article·2017-04

Light‐Triggered Inactivation of Enzymes with Photothermal Nanoheaters

Sebastian A. Thompson, Sureyya Paterson, Marwa M. M. Azab, Alastair W. Wark, Roberto de la Rica

Small· Volume 13· Issue 15
Publisher page

Abstract

A universal method for inactivating enzymes on demand is introduced, which involves irradiating nanorod-bound enzymes with near-infrared light. The subsequent generation of plasmonic heat denatures the enzymes selectively without damaging other proteins or cell membranes present in the same solution. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Advanced Photocatalysis Techniques · Advanced biosensing and bioanalysis techniques · Advanced Nanomaterials in Catalysis

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

WestCHEM Department of Pure and Applied Chemistry University of Strathclyde Technology and Innovation Centre 99 George Street Glasgow G1 1RD Scotland UK

Department of Chemistry and Biochemistry Hunter College–City University of New York New York NY 10065 USA

Funding

WestCHEM

References (26)

Show source-provided references
1. 10.1007/s00216-016-9453-810.1007/s00216-016-9453-8 ↗
2. 10.1021/acs.langmuir.6b0107510.1021/acs.langmuir.6b01075 ↗
3. 10.1002/adma.20150394810.1002/adma.201503948 ↗
4. 10.1016/j.foodchem.2016.05.04710.1016/j.foodchem.2016.05.047 ↗
5. 10.1038/ncomms925010.1038/ncomms9250 ↗
6. 10.1002/chem.20100271610.1002/chem.201002716 ↗
7. 10.1021/nn403659n10.1021/nn403659n ↗
8. 10.1039/C4NR03865G10.1039/C4NR03865G ↗
9. 10.1039/C6SC02465C10.1039/C6SC02465C ↗
10. 10.1103/PhysRevLett.104.13680510.1103/PhysRevLett.104.136805 ↗
11. 10.1039/C4NR05179C10.1039/C4NR05179C ↗
12. 10.1021/nn503311d10.1021/nn503311d ↗
13. 10.1021/nn401187c10.1021/nn401187c ↗
14. 10.1021/la404935q10.1021/la404935q ↗
15. 10.1016/S1050-3862(99)00041-810.1016/S1050-3862(99)00041-8 ↗
16. 10.1039/C5CC05331E10.1039/C5CC05331E ↗
17. 10.1038/nnano.2009.5010.1038/nnano.2009.50 ↗
18. 10.1021/cm303708p10.1021/cm303708p ↗
19. 10.1021/nl803690510.1021/nl8036905 ↗
20. 10.1039/C5TB00556F10.1039/C5TB00556F ↗
21. 10.1111/j.1365-2621.1991.tb05328.x10.1111/j.1365-2621.1991.tb05328.x ↗
22. 10.1021/nl070345g10.1021/nl070345g ↗
23. 10.1021/nl050127s10.1021/nl050127s ↗
24. 10.1021/nl070610y10.1021/nl070610y ↗
25. 10.1039/C5SC00744E10.1039/C5SC00744E ↗
26. 10.1038/nnano.2016.5410.1038/nnano.2016.54 ↗