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1.
Molecules ; 28(1)2023 Jan 02.
Artigo em Inglês | MEDLINE | ID: mdl-36615562

RESUMO

Photodetectors based on organic materials are attractive due to their tunable spectral response and biocompatibility, meaning that they are a promising platform for an artificial human eye. To mimic the photoelectric response of the human eye, narrowband spectrally-selective organic photodetectors are in great demand, and single-component organic photodetectors based on donor-acceptor conjugated molecules are a noteworthy candidate. In this work, we present single-component selective full-color organic photodetectors based on donor-acceptor conjugated molecules synthetized to mimic the spectral response of the cones and rods of a human eye. The photodetectors demonstrated a high responsivity (up to 70 mA/W) with a response time of less than 1 µs, which is three orders of magnitude faster than that of human eye photoreceptors. Our results demonstrate the possibility of the creation of an artificial eye or photoactive eye "prostheses".


Assuntos
Órgãos Artificiais , Olho , Humanos , Tempo de Reação
2.
Proc Natl Acad Sci U S A ; 108(51): 20568-72, 2011 Dec 20.
Artigo em Inglês | MEDLINE | ID: mdl-22158895

RESUMO

Cofilin/ADF proteins play key roles in the dynamics of actin, one of the most abundant and highly conserved eukaryotic proteins. We used cryoelectron microscopy to generate a 9-Å resolution three-dimensional reconstruction of cofilin-decorated actin filaments, the highest resolution achieved for a complex of F-actin with an actin-binding protein. We show that the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state. The changes between the actin protomer in naked F-actin and in the actin-cofilin filament are greater than the conformational changes between G- and F-actin. Our results show the structural plasticity of actin, suggest that other actin-binding proteins may also induce large but different conformational changes, and show that F-actin cannot be described by a single molecular model.


Assuntos
Fatores de Despolimerização de Actina/química , Actinas/química , Cofilina 2/química , Citoesqueleto/química , Polímeros/química , Microscopia Crioeletrônica/métodos , Biblioteca Gênica , Humanos , Microscopia Eletrônica/métodos , Modelos Moleculares , Conformação Molecular , Músculo Esquelético/metabolismo , Conformação Proteica , Estrutura Secundária de Proteína
3.
ACS Biomater Sci Eng ; 10(2): 1139-1152, 2024 02 12.
Artigo em Inglês | MEDLINE | ID: mdl-38241460

RESUMO

Organic semiconductor materials with a unique set of properties are very attractive for interfacing biological objects and can be used for noninvasive therapy or detection of biological signals. Here, we describe the synthesis and investigation of a novel series of organic push-pull conjugated molecules with the star-shaped architecture, consisting of triphenylamine as a branching electron donor core linked through the thiophene π-spacer to electron-withdrawing alkyl-dicyanovinyl groups. The molecules could form stable aqueous dispersions of nanoparticles (NPs) without the addition of any surfactants or amphiphilic polymer matrixes with the average size distribution varying from 40 to 120 nm and absorption spectra very similar to those of human eye retina pigments such as rods and green cones. Variation of the terminal alkyl chain length of the molecules forming NPs from 1 to 12 carbon atoms was found to be an efficient tool to modulate their lipophilic and biological properties. Possibilities of using the NPs as light nanoactuators in biological systems or as artificial pigments for therapy of degenerative retinal diseases were studied both on the model planar bilayer lipid membranes and on the rat cortical neurons. In the planar bilayer system, the photodynamic activity of these NPs led to photoinactivation of ion channels formed by pentadecapeptide gramicidin A. Treatment of rat cortical neurons with the NPs caused depolarization of cell membranes upon light irradiation, which could also be due to the photodynamic activity of the NPs. The results of the work gave more insight into the mechanisms of light-controlled stimulation of neuronal activity and for the first time showed that fine-tuning of the lipophilic affinity of NPs based on organic conjugated molecules is of high importance for creating a bioelectronic interface for biomedical applications.


Assuntos
Nanopartículas , Ratos , Humanos , Animais , Nanopartículas/química , Polímeros/química , Aminas , Água , Neurônios
4.
Cell Signal ; 19(10): 2035-45, 2007 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-17604605

RESUMO

Two-dimensional crystals of protein kinase C delta (PKCdelta) and of its regulatory domain (RDdelta) were grown on lipid monolayers and analyzed by electron microscopy at tilt angles varying from -50 degrees to +55 degrees. Although the crystals exhibit pseudo-3-fold symmetry, analysis of difference phase residuals indicates that there is only one way to align the crystals for merging so the data were processed in plane group P1. Three-dimensional reconstructions generated for several two-dimensional crystals each of PKCdelta and RDdelta show good agreement and are consistent with membrane attachment via a single C1 subdomain, a small surface contact by one or two loops from the C2 domain, and, in intact PKCdelta, a small appendage from the catalytic domain, probably V5. Two-dimensional crystallography with three-dimensional reconstruction should be suitable for examination of additional PKC isozymes and for analysis of the enzymes bound to substrates and other proteins.


Assuntos
Modelos Moleculares , Proteína Quinase C-delta/ultraestrutura , Cristalização , Imageamento Tridimensional , Lipídeos de Membrana/química , Proteína Quinase C-delta/química , Estrutura Terciária de Proteína
5.
J Phys Chem C Nanomater Interfaces ; 121(12): 6424-6435, 2017 Mar 30.
Artigo em Inglês | MEDLINE | ID: mdl-28413568

RESUMO

Small push-pull molecules attract much attention as prospective donor materials for organic solar cells (OSCs). By chemical engineering, it is possible to combine a number of attractive properties such as broad absorption, efficient charge separation, and vacuum and solution processabilities in a single molecule. Here we report the synthesis and early time photophysics of such a molecule, TPA-2T-DCV-Me, based on the triphenylamine (TPA) donor core and dicyanovinyl (DCV) acceptor end group connected by a thiophene bridge. Using time-resolved photoinduced absorption and photoluminescence, we demonstrate that in blends with [70]PCBM the molecule works both as an electron donor and hole acceptor, thereby allowing for two independent channels of charge generation. The charge-generation process is followed by the recombination of interfacial charge transfer states that takes place on the subnanosecond time scale as revealed by time-resolved photoluminescence and nongeminate recombination as follows from the OSC performance. Our findings demonstrate the potential of TPA-DCV-based molecules as donor materials for both solution-processed and vacuum-deposited OSCs.

6.
Biophys J ; 82(5): 2700-8, 2002 May.
Artigo em Inglês | MEDLINE | ID: mdl-11964256

RESUMO

Two-dimensional crystals of protein kinase C (PKC) delta, its regulatory domain (RDdelta), and the enzyme complexed with the substrate myelin basic protein have been grown on lipid monolayers composed of phosphatidylcholine: phosphatidylserine: diolein (45:50:5, molar ratio). Images have been reconstructed to 10-A resolution. The unit cells of all three proteins have cell edges a = b and interedge angle gamma = 60 degrees. RDdelta has an edge length of 33 +/- 1 A, and its reconstruction is donut shaped. The three-dimensional reconstructions from the PKCdelta C1b crystal structure () can be accommodated in this two-dimensional projection. Intact PKCdelta has an edge length of 46 +/- 1 A in the presence or absence of a nonhydrolyzable ATP analog, AMP-PnP. Its reconstruction has a similar donut shape, which can accommodate the C1b domain, but the spacing between donuts is greater than that in RDdelta; some additional structure is visible between the donuts. The complex of PKCdelta and myelin basic protein, with or without AMP-PnP, has an edge length of 43 +/- 1 A and a distinct structure. These results indicate that the C1 domains of RDdelta are tightly packed in the plane of the membrane in the two-dimensional crystals, that there is a single molecule of PKCdelta in the unit cell, and that its interaction with myelin basic protein induces a shift in conformation and/or packing of the enzyme.


Assuntos
Isoenzimas/química , Proteína Básica da Mielina/química , Proteína Quinase C/química , Animais , Sítios de Ligação , Linhagem Celular , Cristalografia por Raios X , Isoenzimas/ultraestrutura , Microscopia Eletrônica , Proteína Básica da Mielina/ultraestrutura , Proteína Quinase C/ultraestrutura , Proteína Quinase C-delta , Proteínas Recombinantes/química , Proteínas Recombinantes/ultraestrutura , Spodoptera , Propriedades de Superfície , Transfecção
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