Abstract:
:In humans, alpha-glucosidase activity is present in sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM). α-glucosidase is involved in the hydrolyses of disaccharide into monosaccharides and results in hyperglycemia. Subsequently chronic hyperglycemia induces oxidative stress and ultimately leads to the secondary complications of diabetes. Hence, identifying compounds with dual beneficial activity such as efficient antioxidant and α-glucosidase inhibition property has attracted the attention in recent years. Keeping these views, in the present study astaxanthin (AST; a natural antioxidant present in marine microalgae) was biconjugated with allyl sulfur amino acid such as s-allyl cysteine (SAC). The synthesized AST-SAC (with molecular weight of 883.28) was characterized using UV-visible spectrophotometer, ESI-MS, and NMR analysis. AST-SAC showed potent antioxidant property in vitro. AST-SAC inhibited Saccharomyces cerevisiae α-glucosidase (IC50 = 3.98 μM; Ki = 1 μM) and mammalian α-glucosidase [rat intestinal maltase (IC50 = 6.4 μM; Ki = 1.3 μM) and sucrase (IC50 = 1.6 μM; Ki = 0.18 μM)] enzyme activity in a dose-dependent manner. Kinetic analysis revealed that AST-SAC inhibited all the α-glucosidases in a competitive mode. In silico analysis determined the interaction of AST-SAC with the amino acids present in the active site of S. cerevisiae and human (MGAM and SI) α-glucosidases.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Sakayanathan P,Loganathan C,Iruthayaraj A,Periyasamy P,Poomani K,Periasamy V,Thayumanavan Pdoi
10.1016/j.ijbiomac.2018.06.027subject
Has Abstractpub_date
2018-10-15 00:00:00pages
252-262issue
Pt Aeissn
0141-8130issn
1879-0003pii
S0141-8130(18)31882-8journal_volume
118pub_type
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