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10.12.2015 | Original Contribution

N- and S-homocysteinylation reduce the binding of human serum albumin to catechins

verfasst von: Angelo Zinellu, Salvatore Sotgia, Bastianina Scanu, Dionigia Arru, Annalisa Cossu, Anna Maria Posadino, Roberta Giordo, Arduino A. Mangoni, Gianfranco Pintus, Ciriaco Carru

Erschienen in: European Journal of Nutrition | Ausgabe 2/2017

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Abstract

Purpose

The dietary flavonoids epicatechin (EC), epigallocatechin (EGC), epicatechin gallate (ECG) and epigallocatechin gallate (EGCG) have been shown to interact with circulating albumin for transport in blood to different body tissues. This interaction may modulate their bioavailability and effectiveness.

Methods

Using affinity capillary electrophoresis to assess binding constants (K _b), we investigated whether posttranslational modification of human serum albumin (HSA) through N- and S-homocysteinylation, commonly observed in hyperhomocysteinemia, may modify its interaction with catechins.

Results

S-Hcy HSA had lower K_b values toward EC (14 %), EGC (18 %), ECG (24 %) and EGCG (30 %). Similarly, N-Hcy HSA had lower K_b values toward EC (17 %), EGC (22 %), ECG (23 %) and EGCG (32 %). No differences were observed in the affinity between catechins, albumin and mercaptalbumin.

Conclusion

Therefore, HSA posttranslational modifications typical of hyperhomocysteinemia reduce its affinity to catechins, potentially affecting their pharmacokinetics and availability at the active sites.

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Titel: N- and S-homocysteinylation reduce the binding of human serum albumin to catechins
verfasst von: Angelo Zinellu
Salvatore Sotgia
Bastianina Scanu
Dionigia Arru
Annalisa Cossu
Anna Maria Posadino
Roberta Giordo
Arduino A. Mangoni
Gianfranco Pintus
Ciriaco Carru
Publikationsdatum: 10.12.2015
Verlag: Springer Berlin Heidelberg
Erschienen in: European Journal of Nutrition / Ausgabe 2/2017
Print ISSN: 1436-6207
Elektronische ISSN: 1436-6215
DOI: https://doi.org/10.1007/s00394-015-1125-5

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N- and S-homocysteinylation reduce the binding of human serum albumin to catechins

Abstract

Purpose

Methods

Results

Conclusion

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