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Sensing Properties of NH(2)-MIL-101 Series for Specific Amino Acids via Turn-On Fluorescence

Metal–organic frameworks (MOFs) have been demonstrated to be desired candidates for sensing definite species owing to their tunable composition, framework structure and functionality. In this work, the NH(2)-MIL-101 series was utilized for sensing specific amino acids. The results show that cysteine...

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Autores principales: Dong, Jing, Dao, Xiao-Yao, Zhang, Xiao-Yu, Zhang, Xiu-Du, Sun, Wei-Yin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8434598/
https://www.ncbi.nlm.nih.gov/pubmed/34500766
http://dx.doi.org/10.3390/molecules26175336
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author Dong, Jing
Dao, Xiao-Yao
Zhang, Xiao-Yu
Zhang, Xiu-Du
Sun, Wei-Yin
author_facet Dong, Jing
Dao, Xiao-Yao
Zhang, Xiao-Yu
Zhang, Xiu-Du
Sun, Wei-Yin
author_sort Dong, Jing
collection PubMed
description Metal–organic frameworks (MOFs) have been demonstrated to be desired candidates for sensing definite species owing to their tunable composition, framework structure and functionality. In this work, the NH(2)-MIL-101 series was utilized for sensing specific amino acids. The results show that cysteine (Cys) can significantly enhance the fluorescence emission of NH(2)-MIL-101-Fe suspended in water, while NH(2)-MIL-101-Al exhibits the ability to sense lysine (Lys), arginine (Arg) and histidine (His) in aqueous media via turn-on fluorescence emission. Titration experiments ensure that NH(2)-MIL-101-Fe and NH(2)-MIL-101-Al can selectively and quantitatively detect these amino acids. The sensing mechanism was examined and discussed. The results of this study show that the metal centers in MOFs are crucial for sensing specific amino acids.
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spelling pubmed-84345982021-09-12 Sensing Properties of NH(2)-MIL-101 Series for Specific Amino Acids via Turn-On Fluorescence Dong, Jing Dao, Xiao-Yao Zhang, Xiao-Yu Zhang, Xiu-Du Sun, Wei-Yin Molecules Article Metal–organic frameworks (MOFs) have been demonstrated to be desired candidates for sensing definite species owing to their tunable composition, framework structure and functionality. In this work, the NH(2)-MIL-101 series was utilized for sensing specific amino acids. The results show that cysteine (Cys) can significantly enhance the fluorescence emission of NH(2)-MIL-101-Fe suspended in water, while NH(2)-MIL-101-Al exhibits the ability to sense lysine (Lys), arginine (Arg) and histidine (His) in aqueous media via turn-on fluorescence emission. Titration experiments ensure that NH(2)-MIL-101-Fe and NH(2)-MIL-101-Al can selectively and quantitatively detect these amino acids. The sensing mechanism was examined and discussed. The results of this study show that the metal centers in MOFs are crucial for sensing specific amino acids. MDPI 2021-09-02 /pmc/articles/PMC8434598/ /pubmed/34500766 http://dx.doi.org/10.3390/molecules26175336 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Dong, Jing
Dao, Xiao-Yao
Zhang, Xiao-Yu
Zhang, Xiu-Du
Sun, Wei-Yin
Sensing Properties of NH(2)-MIL-101 Series for Specific Amino Acids via Turn-On Fluorescence
title Sensing Properties of NH(2)-MIL-101 Series for Specific Amino Acids via Turn-On Fluorescence
title_full Sensing Properties of NH(2)-MIL-101 Series for Specific Amino Acids via Turn-On Fluorescence
title_fullStr Sensing Properties of NH(2)-MIL-101 Series for Specific Amino Acids via Turn-On Fluorescence
title_full_unstemmed Sensing Properties of NH(2)-MIL-101 Series for Specific Amino Acids via Turn-On Fluorescence
title_short Sensing Properties of NH(2)-MIL-101 Series for Specific Amino Acids via Turn-On Fluorescence
title_sort sensing properties of nh(2)-mil-101 series for specific amino acids via turn-on fluorescence
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8434598/
https://www.ncbi.nlm.nih.gov/pubmed/34500766
http://dx.doi.org/10.3390/molecules26175336
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