Photoluminescent silicon nanoparticles 1-2 nm in size were synthesized by a wet chemical procedure and derivatized with propylamine （NH2SiNP）. Surface NH2 groups were used as linkers for additional poly（ethylene gl...Photoluminescent silicon nanoparticles 1-2 nm in size were synthesized by a wet chemical procedure and derivatized with propylamine （NH2SiNP）. Surface NH2 groups were used as linkers for additional poly（ethylene glycol） （PEG） and folic acid （Fo） attachment （PEG-NHSiNP and Fo-NHSiNP, respectively） to enable efficient targeting of the particles to tumors and inflammatory sites. The particles were characterized by transmission electron microscopy, Fourier transform infrared spectroscopy, X-ray photoelectron spectroscopy, ζ potential, dynamic light scattering, and time-resolved anisotropy. The photophysical properties and photosensitizing capacity of the particles and their interaction with proteins was dependent on the nature of the attached molecules. While PEG attachment did not alter the photophysical behavior of NH2SiNP, the attachment of Fo diminished particle photoluminescence. Particles retained the capacity for 1O2 generation; however, efficient 1O2 quenching by the attached surface groups may be a drawback when using these particles as 1O2photosensitizers. In addition, Fo attachment provided particles with the capacity to generate the superoxide anion radical （O2-）. The particles were able to bind tryptophan residues of bovine serum albumin （BSA） within quenching distances. NH2SiNP and PEG-NHSLNP ground state complexes with BSA showed binding constants of （3.1 ± 0.3） × 10^4 and （1.3 ±0.4） × 10^3 M-1, respectively. The lower value observed for PEG-NHSiNP complexes indicates that surface PEGylation leads to a reduction in protein adsorption, which is required to prevent opsonization. An increase in particle luminescence upon BSA binding was attributed to the hydrophobic environment generated by the protein. NH2SiNP-BSA complexes were also capable of resonance energy transfer.展开更多
Canonical transient receptor potential 4(TRPC4) forms non-selective cation channels that contribute to phospholipase C-dependent Ca2+ entry into cells following stimulation of G protein coupled receptors and receptor ...Canonical transient receptor potential 4(TRPC4) forms non-selective cation channels that contribute to phospholipase C-dependent Ca2+ entry into cells following stimulation of G protein coupled receptors and receptor tyrosine kinases.Moreover,the channels are regulated by pertussis toxin-sensitive Gi/o proteins,lipids,and various other signaling mechanisms.TRPC4-containing channels participate in the regulation of a variety of physiological functions,including excitability of both gastrointestinal smooth muscles and brain neurons.This review is to present recent advances in the understanding of physiology and development of small molecular modulators of TRPC4 channels.展开更多
文摘Photoluminescent silicon nanoparticles 1-2 nm in size were synthesized by a wet chemical procedure and derivatized with propylamine （NH2SiNP）. Surface NH2 groups were used as linkers for additional poly（ethylene glycol） （PEG） and folic acid （Fo） attachment （PEG-NHSiNP and Fo-NHSiNP, respectively） to enable efficient targeting of the particles to tumors and inflammatory sites. The particles were characterized by transmission electron microscopy, Fourier transform infrared spectroscopy, X-ray photoelectron spectroscopy, ζ potential, dynamic light scattering, and time-resolved anisotropy. The photophysical properties and photosensitizing capacity of the particles and their interaction with proteins was dependent on the nature of the attached molecules. While PEG attachment did not alter the photophysical behavior of NH2SiNP, the attachment of Fo diminished particle photoluminescence. Particles retained the capacity for 1O2 generation; however, efficient 1O2 quenching by the attached surface groups may be a drawback when using these particles as 1O2photosensitizers. In addition, Fo attachment provided particles with the capacity to generate the superoxide anion radical （O2-）. The particles were able to bind tryptophan residues of bovine serum albumin （BSA） within quenching distances. NH2SiNP and PEG-NHSLNP ground state complexes with BSA showed binding constants of （3.1 ± 0.3） × 10^4 and （1.3 ±0.4） × 10^3 M-1, respectively. The lower value observed for PEG-NHSiNP complexes indicates that surface PEGylation leads to a reduction in protein adsorption, which is required to prevent opsonization. An increase in particle luminescence upon BSA binding was attributed to the hydrophobic environment generated by the protein. NH2SiNP-BSA complexes were also capable of resonance energy transfer.
基金supported in part by the National Natural Science Foundation of China(81228021)US National Institutes of Health(DK081654)
文摘Canonical transient receptor potential 4(TRPC4) forms non-selective cation channels that contribute to phospholipase C-dependent Ca2+ entry into cells following stimulation of G protein coupled receptors and receptor tyrosine kinases.Moreover,the channels are regulated by pertussis toxin-sensitive Gi/o proteins,lipids,and various other signaling mechanisms.TRPC4-containing channels participate in the regulation of a variety of physiological functions,including excitability of both gastrointestinal smooth muscles and brain neurons.This review is to present recent advances in the understanding of physiology and development of small molecular modulators of TRPC4 channels.
