期刊
ACS NANO
卷 5, 期 5, 页码 3788-3794出版社
AMER CHEMICAL SOC
DOI: 10.1021/nn200120e
关键词
protein-nanoparticle hybrids; photo-cleavage; thermal denaturation; pulsed X-ray scattering; nanobubbles
类别
资金
- Ministry of Science, Education and the Arts Baden-Wurttemberg
- Creative Research Initiatives (Center for Time-Resolved Diffraction) of MEST/NRF
- WCU [R31-2008-000-10071-0]
- DFG
Protein-coated gold nanoparticles in suspension are excited by intense laser pulses to mimic the light-induced effect on biomolecules that occur In photothermal laser therapy with nanoparticles as photosensitizer. Ultrafast X-ray scattering employed to access the nanoscale structural modifications of the protein-nanoparticle hybrid reveals that the protein shell Is expelled as a whole without denaturation at a laser fluence that coincides with the bubble formation threshold. In this ultrafast heating mediated by the nanoparticles, time-resolved scattering data show that proteins are not denatured in terms of secondary structure even at much higher temperatures than the static thermal denaturation temperature, probably because time Is too short for the proteins to unfold and the temperature stimulus has vanished before this motion sets in. Consequently the laser pulse length has a strong influence on whether the end result is the ligand detachment (for example drug delivery) or biomaterial degradation.
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