상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

The inhibitory role of Co2+ on α-glucosidase: Inhibition kinetics and molecular dynamics simulation integration study

Authors 

X LiZ R LuD ShenY ZhanH M ZhouQ ShengJinhyuk Lee

Publisher 

Elsevier

Issue Date 

2014

Citation 

Process Biochemistry, vol. 49, no. 11, pp. 1913-1919

Keywords 

Co2+Inhibition kineticsMolecular dynamicsaUnfoldingα-Glucosidase

Abstract 

It is important to study enzyme inhibition of α-glucosidase (EC 3.2.1.20) due to its clinical relevance as a target enzyme for the treatment of type 2 diabetes mellitus. In this study, we investigated Co2+-induced inhibition as well as structural changes of α-glucosidase integrated with computational simulations. α-Glucosidase activity was inhibited by Co2+ in a dose-dependent manner. Co2+ inhibited α-glucosidase in a parabolic non-competitive inhibition reaction (Ki = 0.78 ± 0.08 mM) and directly induced regional unfolding of the enzyme resulting in a slight decrease in hydrophobic surface. The computational simulations using molecular dynamics showed that simulation with Co2+ resulted in a loss of secondary structure by positioning Co2+ near the active site for glucose production, implying that the Co2+ stimulate enzyme unfolding. Our study revealed the mechanism of Co2+ ligand binding mediated structural changes as well as inhibition of α-glucosidase activity, and suggested that Co2+ could act as a potent inhibitor of α-glucosidase for the treatment of type 2 diabetes mellitus.

ISSN 

0032-9592

Link 

http://dx.doi.org/10.1016/j.procbio.2014.08.002

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)