Naslov
Amadori and Heyns Rearrangement Products as Possible Galectin-3 Ligands

Autori
Jakas, Andreja ; Ayyalasomayajula, Ramya ; Čudić, Mare

Vrsta, podvrsta i kategorija rada
Radovi u zbornicima skupova, cjeloviti rad (in extenso), znanstveni

Izvornik
Proceedings of the 36th European and the 12th International Peptide Symposium / Lebl, Michal - Sitges : European Peptide Society, 2022, 197-199

ISBN
979-8987214008

Skup
36th European Peptide Symposium and 12th International Peptide Symposium

Mjesto i datum
Sitges, Španjolska, 28.08.2022. - 02.09.2022

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
Amadori rearrangement ; Heyns rearrangement ; Maillard reaction ; Galectin-3 ; advance glycation end products (AGEs)

Sažetak
The Amadori and Heyns rearrangements, two well- known reactions in carbohydrate chemistry, are the initial step in the Maillard reaction cascade. The end products of the classical Mallard reaction, the advanced glycation end products (AGEs), are first defined as product of nonenzymatic browning reaction during food processing, and later linked to human aging and development of many age-related morbidities. The Amadori rearrangement is a reaction between a-hydroxy aldehydes and suitable amines leading to a-amino ketones (1-5).1, 2 The Heyns rearrangement follows, in principle, the same pattern but employs a-hydroxy ketones as starting materials and proceeds via a glycosylamine to the corresponding 2-amino-2- deoxyaldoses (6-8).2 Receptor for advanced glycation end products (RAGE) and its ligands have been considered an important pathogenic triggers for the progression of the vascular injuries in diabetes. Strong evidence indicates that galectin-3 participates in the pathogenesis of diabetic complications via its receptor function for advanced glycation end- products (AGEs).3, 4 Here we are investigating the possibility of galectin-3 to interact with initial products of Maillard reaction, Amadori compounds 1-5 and Heyns compounds 6-8. Amadori and Heyns compounds are derivatives of endogenous opioid peptide Leu-enkephalin, its truncated parts, and tetrapeptide Leu-Ser-Lys-Leu biologically important for activation of TGF-β. 1 A. Jakas and Š. Horvat, Biopolymers, 2003, 69, 421–431. 2 A. Jakas, A. Katić, N. Bionda and Š. Horvat, Carbohydr. Res., 2008, 343, 2475–2480. 3 H. Vlassara, Y. M. Li, F. Imani, D. Wojciechowicz, Z. Yang, F.-T. Liu and A. Cerami, Mol. Med., 1995, 1, 634–646. 4 G. Pugliese, C. Iacobini, C. M. Pesce and S. Menini, Glycobiology, 2015, 25, 136–150.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

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