Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions

Abstract Galectins are involved in the regulation of divergent physiological and pathological processes and are increasingly recognized to play important roles in a number of diseases. However, a simple and effective way in assessing galectin-ligand interactions is lacking. Our examination of the se...

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Autores principales:	Paulina Sindrewicz, Xiaoxin Li, Edwin A. Yates, Jeremy E. Turnbull, Lu-Yun Lian, Lu-Gang Yu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/030c40846b0749f9815431bef71e56dd
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spelling	oai:doaj.org-article:030c40846b0749f9815431bef71e56dd2021-12-02T16:08:04ZIntrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions10.1038/s41598-019-47658-82045-2322https://doaj.org/article/030c40846b0749f9815431bef71e56dd2019-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-019-47658-8https://doaj.org/toc/2045-2322Abstract Galectins are involved in the regulation of divergent physiological and pathological processes and are increasingly recognized to play important roles in a number of diseases. However, a simple and effective way in assessing galectin-ligand interactions is lacking. Our examination of the sequence of all 12 human galectin members reveals the presence of one or more tryptophan residues in the carbohydrate-recognition domains of each galectin. This led us to investigate the possibility that alteration of the galectin intrinsic tryptophan fluorescence could be used in determining the strength of galectin-ligand interactions. One representative member from each of the three subtype galectins, galectin-2 (proto-), galectin-3 (chimera-) and galectin-4 (tandem repeat-type), was selected and analysed for galectin interaction with three ligands of different affinities: galactose, lactose and N-acetyl-lactosamine using tryptophan fluorescence spectroscopy (TFS) and, as a comparison, isothermal titration calorimetry (ITC). Good agreement between TFS and ITC measurements were revealed in ligand bindings of all galectin members. Moreover, TFS detected very weak galectin binding where ITC could not reliably do so. The reliability of TFS in determining galectin-ligand interactions was further validated by analysis of galectin-3 interaction with a semisynthetic ligand, F3. Thus, TFS can be used as a simple, sensitive and reliable way to determine galectin-ligand interactions and also as a drug-discovery platform in developing galectin-targeted therapeutic drugs.Paulina SindrewiczXiaoxin LiEdwin A. YatesJeremy E. TurnbullLu-Yun LianLu-Gang YuNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 9, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Paulina Sindrewicz Xiaoxin Li Edwin A. Yates Jeremy E. Turnbull Lu-Yun Lian Lu-Gang Yu Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions
description	Abstract Galectins are involved in the regulation of divergent physiological and pathological processes and are increasingly recognized to play important roles in a number of diseases. However, a simple and effective way in assessing galectin-ligand interactions is lacking. Our examination of the sequence of all 12 human galectin members reveals the presence of one or more tryptophan residues in the carbohydrate-recognition domains of each galectin. This led us to investigate the possibility that alteration of the galectin intrinsic tryptophan fluorescence could be used in determining the strength of galectin-ligand interactions. One representative member from each of the three subtype galectins, galectin-2 (proto-), galectin-3 (chimera-) and galectin-4 (tandem repeat-type), was selected and analysed for galectin interaction with three ligands of different affinities: galactose, lactose and N-acetyl-lactosamine using tryptophan fluorescence spectroscopy (TFS) and, as a comparison, isothermal titration calorimetry (ITC). Good agreement between TFS and ITC measurements were revealed in ligand bindings of all galectin members. Moreover, TFS detected very weak galectin binding where ITC could not reliably do so. The reliability of TFS in determining galectin-ligand interactions was further validated by analysis of galectin-3 interaction with a semisynthetic ligand, F3. Thus, TFS can be used as a simple, sensitive and reliable way to determine galectin-ligand interactions and also as a drug-discovery platform in developing galectin-targeted therapeutic drugs.
format	article
author	Paulina Sindrewicz Xiaoxin Li Edwin A. Yates Jeremy E. Turnbull Lu-Yun Lian Lu-Gang Yu
author_facet	Paulina Sindrewicz Xiaoxin Li Edwin A. Yates Jeremy E. Turnbull Lu-Yun Lian Lu-Gang Yu
author_sort	Paulina Sindrewicz
title	Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions
title_short	Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions
title_full	Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions
title_fullStr	Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions
title_full_unstemmed	Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions
title_sort	intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/030c40846b0749f9815431bef71e56dd
work_keys_str_mv	AT paulinasindrewicz intrinsictryptophanfluorescencespectroscopyreliablydeterminesgalectinligandinteractions AT xiaoxinli intrinsictryptophanfluorescencespectroscopyreliablydeterminesgalectinligandinteractions AT edwinayates intrinsictryptophanfluorescencespectroscopyreliablydeterminesgalectinligandinteractions AT jeremyeturnbull intrinsictryptophanfluorescencespectroscopyreliablydeterminesgalectinligandinteractions AT luyunlian intrinsictryptophanfluorescencespectroscopyreliablydeterminesgalectinligandinteractions AT lugangyu intrinsictryptophanfluorescencespectroscopyreliablydeterminesgalectinligandinteractions
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Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions

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