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1.
Polymers (Basel) ; 14(9)2022 Apr 30.
Artigo em Inglês | MEDLINE | ID: mdl-35567027

RESUMO

Functionalised holograms are important for applications utilising smart diffractive optical elements for light redirection, shaping and in the development of sensors/indicators. This paper reports on holographic recording in novel magnetic nanocomposites and the observed temperature change in dry layers and liquid samples exposed to alternating magnetic field (AMF). The nanocomposite consists of N-isopropylacrylamide (NIPA)-based polymer doped with magnetic nanoparticles (MNPs), and local heating is achieved through magnetic induction. Here, volume transmission holographic gratings (VTHGs) are recorded with up to 24% diffraction efficiency (DE) in the dry layers of magnetic nanocomposites. The dry layers and liquid samples are then exposed to AMF. Efficient heating was observed in the liquid samples doped with Fe3O4 MNPs of 20 nm average size where the temperature increased from 27 °C to 64 °C after 300 s exposure to 111 mT AMF. The temperature increase in the dry layers doped with the same nanoparticles after exposure to 4.4 mT AMF was observed to be 6 °C. No temperature change was observed in the undoped layers. Additionally, we have successfully recorded Denisyuk holograms in the magnetic nanocomposite materials. The results reveal that the magnetic nanocomposite layers are suitable for recording holograms and need further optimisation in developing holographic indicators for mapping AMFs.

2.
J Diabetes Sci Technol ; 7(1): 13-23, 2013 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-23439156

RESUMO

BACKGROUND: This article describes a new fiber-coupled, percutaneous fluorescent continuous glucose monitoring (CGM) system that has shown 14 days of functionality in a human clinical trial. METHOD: The new optical CGM system (FiberSense) consists of a transdermal polymer optical fiber containing a biochemical glucose sensor and a small fluorescence photometer optically coupled to the fiber. The glucose-sensitive optical fiber was implanted in abdominal and upper-arm subcutaneous tissue of six diabetes patients and remained there for up to 14 days. The performance of the system was monitored during six visits to the study center during the trial. Blood glucose changes were induced by oral carbohydrate intake and insulin injections, and capillary blood glucose samples were obtained from the finger tip. The data were analyzed using linear regression and the consensus error grid analysis. RESULTS: The FiberSense worn at the upper arm exhibited excellent results during 14 wearing days, with an overall mean absolute relative difference (MARD) of 8.3% and 94.6% of the data in zone A of the consensus error grid. At the abdominal application site, FiberSense resulted in a MARD of 11.4 %, with 93.8% of the data in zone A. CONCLUSIONS: The FiberSense CGM system provided consistent, reliable measurements of subcutaneous glucose levels in human clinical trial patients with diabetes for up to 14 days.


Assuntos
Técnicas Biossensoriais/instrumentação , Automonitorização da Glicemia/instrumentação , Diabetes Mellitus/sangue , Monitorização Ambulatorial/instrumentação , Técnicas Biossensoriais/métodos , Glicemia/análise , Feminino , Transferência Ressonante de Energia de Fluorescência , Humanos , Masculino , Pessoa de Meia-Idade , Monitorização Ambulatorial/métodos
3.
J Diabetes Sci Technol ; 7(1): 24-34, 2013 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-23439157

RESUMO

BACKGROUND: To evaluate the feasibility of an implantable subconjunctival glucose monitoring system (SGMS) for long-term glucose monitoring, we investigated the in vivo performance of the system. METHOD: The SGMS consists of an implantable ocular mini implant (OMI) and a handheld fluorescence photometer. A clinical study was performed on 47 diabetes patients split into two cohorts. Two different types of OMI were used, with and without a biocompatible surface coating. Duration of the study was 1 year. Correlation between capillary blood glucose and SGMS-derived interstitial fluid glucose was investigated during the first 6 months of the study. RESULTS: Both OMI types were tolerated well in the eyes of the patients. At the beginning of the study, the SGMS of both cohorts revealed a high accuracy with mean absolute relative difference (MARD) values of 7-12%. The performance of the uncoated OMIs deteriorated within 3 months of wearing time, exhibiting a MARD value of 20%. The performance of the surface-coated OMIs was preserved longer. Glucose correlation measurement with reasonable results (MARD of 14%) could be performed for up to 6 months of wear. CONCLUSIONS: The biocompatible surface coating on the OMIs enabled a longer duration of action of up to 6 months compared with 3 months for uncoated implants in a clinical trial.


Assuntos
Técnicas Biossensoriais/instrumentação , Automonitorização da Glicemia/instrumentação , Glicemia/análise , Túnica Conjuntiva/cirurgia , Diabetes Mellitus/sangue , Técnicas Biossensoriais/métodos , Automonitorização da Glicemia/métodos , Estudos de Viabilidade , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Monitorização Fisiológica/instrumentação , Monitorização Fisiológica/métodos , Fatores de Tempo
4.
Proc Natl Acad Sci U S A ; 106(49): 20740-5, 2009 Dec 08.
Artigo em Inglês | MEDLINE | ID: mdl-19933333

RESUMO

We used single-molecule FRET in combination with other biophysical methods and molecular simulations to investigate the effect of temperature on the dimensions of unfolded proteins. With single-molecule FRET, this question can be addressed even under near-native conditions, where most molecules are folded, allowing us to probe a wide range of denaturant concentrations and temperatures. We find a compaction of the unfolded state of a small cold shock protein with increasing temperature in both the presence and the absence of denaturant, with good agreement between the results from single-molecule FRET and dynamic light scattering. Although dissociation of denaturant from the polypeptide chain with increasing temperature accounts for part of the compaction, the results indicate an important role for additional temperature-dependent interactions within the unfolded chain. The observation of a collapse of a similar extent in the extremely hydrophilic, intrinsically disordered protein prothymosin alpha suggests that the hydrophobic effect is not the sole source of the underlying interactions. Circular dichroism spectroscopy and replica exchange molecular dynamics simulations in explicit water show changes in secondary structure content with increasing temperature and suggest a contribution of intramolecular hydrogen bonding to unfolded state collapse.


Assuntos
Transferência Ressonante de Energia de Fluorescência/métodos , Proteínas de Choque Térmico/química , Proteínas de Choque Térmico/metabolismo , Dobramento de Proteína , Precursores de Proteínas/química , Precursores de Proteínas/metabolismo , Temperatura , Timosina/análogos & derivados , Guanidina/farmacologia , Interações Hidrofóbicas e Hidrofílicas , Simulação de Dinâmica Molecular , Desnaturação Proteica/efeitos dos fármacos , Dobramento de Proteína/efeitos dos fármacos , Estrutura Secundária de Proteína , Análise Espectral , Timosina/química , Timosina/metabolismo
5.
Biochemistry ; 47(8): 2458-65, 2008 Feb 26.
Artigo em Inglês | MEDLINE | ID: mdl-18215068

RESUMO

Large oligomeric proteins are usually thought to fold and assemble hierarchically: Domains fold and coalesce to form the subunits, and folded subunits can then associate to form the multimeric structure. We have investigated the refolding pathway of the beta-sheet protein pea seed lectin using spectroscopic and hydrodynamic techniques. In vivo, it is proteolytically processed post-translationally, so that the single-domain subunits of the initial homodimer themselves become heterodimers of intertwined fragment polypeptide chains. Despite this complex topology, mature pea seed lectin reassembles with considerable efficiency at low total protein concentration (10 mug/mL) and low temperature (10 degrees C), albeit very slowly (t1/2 approximately 2 days). Contrary to expectations, the primary assembly product is not the intact beta-sheet domain, but the larger fragment chains first dimerize to form the native-like subunit interface. The smaller fragment chains then associate with this preformed dimer.


Assuntos
Lectinas de Plantas/química , Lectinas de Plantas/metabolismo , Cromatografia em Gel , Reagentes de Ligações Cruzadas/farmacologia , Dimerização , Cinética , Modelos Moleculares , Lectinas de Plantas/isolamento & purificação , Desnaturação Proteica , Dobramento de Proteína , Estrutura Quaternária de Proteína , Estrutura Secundária de Proteína
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