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Title: | Etude in silico de l’interaction ligand-protéine: cas de molécules terpénoïdes à l'alpha amylase pancréatique et à l'albumine sérique humaine |
Authors: | FACHA, Hana SIRADJ, Lamia |
Keywords: | Interactions, terpenoides, Human Pancreatic Alpha-Amylase (HPA), Human Serum Albumin (HSA), molecular docking, Molegro Virtual Docker (MVD) Interactions, terpénoïdes, alpha amylase pancréatique humaine (HPA), albumine plasmatique humaine (HSA), docking moléculaire ; Molegro Virtual Docker (MVD) |
Issue Date: | 2019 |
Publisher: | Faculté Science de la Nature et de la Vie et Sciences de la Terre - Université de Ghardaïa |
Abstract: | The present work revolves around the search for interactions formed between ligands belonging to the family of terpenoïdes and Human Pancreatic Alpha-Amylase (3BAJ) also the interaction with Human Serum Albumin (HSA) (2BXG for Sudlow site II and 1H9Z, 2BXN, 2BXP for the site I). In order to know their abilities to be inhibitory of alpha amylase and / or to modify the pharmacodynamics and pharmacokinetic parameters of the drugs after their attachments on the same site of Human Serum Albumin (HSA). This work was performed (in silico) by the molecular docking technique, thanks to the program Molegro Virtual Docker (MVD). The molecules 7-O-caffeoyl-sylvestroside I (A1), Septemfidoside (A3), 7α- acetoxyroyleanone-12-methyl ether (B11), Royleanone (B12), 3-O-[α-lrhamnopyranosyl- (1→2)-{β-d-glucopyranosyl-(1→6)-} β-dgalactopyranosyl-(1→2)-β-d-glucuronopyranosyl]- sophoradiol (D5), Calendustellatoside A (D6) and Calendustellatoside D (D8) are the metabolites that form interactions with HPA and HSA at site II and I in the three protein targets therefore are strongly proposed for (in vitro) study. |
URI: | https://dspace.univ-ghardaia.edu.dz/xmlui/handle/123456789/5913 |
Appears in Collections: | Mémoires de Master |
Files in This Item:
File | Description | Size | Format | |
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Etude in silico de l’interaction ligand-protéine cas de molécules terpénoïdes à l'alpha amylase pancréatique et à l'album~1.pdf | 9.8 MB | Adobe PDF | View/Open |
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