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1.
Neuroscience ; 511: 110-130, 2023 02 10.
Article in English | MEDLINE | ID: mdl-36442745

ABSTRACT

Nuclear TAR DNA-binding protein 43 (TDP-43) mitigates cellular function, but the dynamic nucleus-cytoplasm shuttling of TDP-43 is disrupted in diseases, such as Amyotrophic Lateral Sclerosis (ALS). The polymorphic nature of the TDP-43 structures in vitro and in vivo is a result of environmental factors leading to the protein pathogenesis. Once the triggers which mitigate TDP-43 biochemistry are identified, new therapies can be developed. This review aims to illustrate recent discoveries in the diversity of TDP-43 structures (amyloidogenic and non-amyloidogenic) and highlight the triggers which result in their formation.


Subject(s)
Amyotrophic Lateral Sclerosis , Cell Nucleus , Humans , Amyotrophic Lateral Sclerosis/metabolism , Cell Nucleus/metabolism , Cytoplasm/metabolism , DNA-Binding Proteins/metabolism
2.
Spectrochim Acta A Mol Biomol Spectrosc ; 279: 121444, 2022 Oct 15.
Article in English | MEDLINE | ID: mdl-35660143

ABSTRACT

The post-translational modification of amino acid plays a critical role in normal and diseased biological states. Specifically, nitrotyrosine (nTyr) has been linked to diseases, including neurodegeneration, among others. Hence, alternative methods are required for detection and differentiation of nTyr from other structurally similar analogues, such as Tyrosine (Tyr) or phosphotyrosine (pTyr). Herein, the selective detection of nTyr, over other congeners, was achieved by using dual-fluorescent carbon dots (CDs) in buffered solution, artificial saliva, bovine serum albumin and diluted equine serum. The nTyr induced fluorescence quenching of the blue and red emissions of CDs, in the 20-105 µM linear range, and with the limit of detection (LOD) at 34 µM, which was well below the physiological concentration required for detection. The sensor was functional at biological pH values, with optimal quenching efficiency at basic pH. The sensor was highly selective for nTyr even in the presence of common biological interferences (metal cations, organic anions, amino acids, nucleosides and other biologicals). The mechanism of quenching (a combination of static and dynamic) was ascribed to the nonradiative energy transfer, due to electronic overlap between nTyr absorbance and CDs fluorescence emission, and electron transfer from excited CDs state to nTyr as an electron acceptor. The dual-fluorescent CDs represent viable sensors for key biological modifications, and their selectivity and sensitivity may be further improved through tailored chemical synthesis of CDs, such as tunable surface chemistry to promote selective recognition of analyte of interest.


Subject(s)
Carbon , Quantum Dots , Animals , Carbon/chemistry , Fluorescent Dyes/chemistry , Horses , Limit of Detection , Quantum Dots/chemistry , Spectrometry, Fluorescence , Tyrosine/analogs & derivatives
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