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1.
Chemistry ; 25(14): 3606-3616, 2019 Mar 07.
Article in English | MEDLINE | ID: mdl-30633421

ABSTRACT

Fifteen new photochromic hybrid materials were synthesized by gas phase loading of fluorinated azobenzenes, namely ortho-tetrafluoroazobenzene (tF-AZB), 4H,4H'-octafluoroazobenzene (oF-AZB), and perfluoroazobenzene (pF-AZB), into the pores of the well-known metal-organic frameworks MOF-5, MIL-53(Al), MIL-53(Ga), MIL-68(Ga), and MIL-68(In). Their composition was analysed by elemental (CHNS) and DSC/TGA. For pF-AZB0.34 @MIL-53(Al), a structural model based on high-resolution synchrotron powder diffraction data was developed and the host-guest and guest-guest interactions were elucidated from this model. These interactions of O-H⋅⋅⋅F and π⋅⋅⋅π type were confirmed by significant shifts of the O-H frequencies in loaded and unloaded MOFs of the MIL-53 and MIL-68 series. Most remarkably, all of the synthesized F-AZB@MOF systems can be switched with visible light, and some of them show almost quantitative (>95 %) photo-isomerization between its E and Z forms with no significant fatigue after repeated switching cycles.

2.
Chem Commun (Camb) ; 53(57): 8070-8073, 2017 Jul 13.
Article in English | MEDLINE | ID: mdl-28676871

ABSTRACT

Photoswitchable metal-organic frameworks (MOFs) enable the dynamic remote control of their key properties. Here, a readily producible approach is presented where photochromic molecules, i.e. azobenzene (AB) and o-tetrafluoroazobenzene (tfAB), are loaded in MOF films of type HKUST-1. These nanoporous films, which can be reversibly switched with UV/visible or only visible light, have remote-controllable guest uptake properties.

3.
J Biol Chem ; 281(2): 1296-304, 2006 Jan 13.
Article in English | MEDLINE | ID: mdl-16286466

ABSTRACT

Caspases were recently implicated in the functional impairment of the nuclear pore complex during apoptosis, affecting its dual activity as nucleocytoplasmic transport channel and permeability barrier. Concurrently, electron microscopic data indicated that nuclear pore morphology is not overtly altered in apoptotic cells, raising the question of how caspases may deactivate nuclear pore function while leaving its overall structure largely intact. To clarify this issue we have analyzed the fate of all known nuclear pore proteins during apoptotic cell death. Our results show that only two of more than 20 nuclear pore core structure components, namely Nup93 and Nup96, are caspase targets. Both proteins are cleaved near their N terminus, disrupting the domains required for interaction with other nucleoporins actively involved in transport and providing the permeability barrier but dispensable for maintaining the nuclear pore scaffold. Caspase-mediated proteolysis of only few nuclear pore complex components may exemplify a general strategy of apoptotic cells to efficiently disable huge macromolecular machines.


Subject(s)
Caspases/metabolism , Cell Nucleus/metabolism , Apoptosis , Cell Proliferation , Cell Separation , DNA/chemistry , DNA Fragmentation , Electrophoresis, Polyacrylamide Gel , Etoposide/pharmacology , Flow Cytometry , HeLa Cells , Humans , Immunoblotting , Microscopy, Electron , Nuclear Pore Complex Proteins/chemistry , Nuclear Proteins/chemistry , Nucleosomes/metabolism , Porins/chemistry , Protein Binding , Protein Conformation , Protein Structure, Tertiary , S Phase , Time Factors
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