:: Volume 16, Issue 7 (Supplement 2013) ::
Feyz 2013, 16(7): 643-644 Back to browse issues page
Evaluating the folding variations in human amylin peptid in the presence of Lead and Selenium
Sayyed Mahdi Mirhashemi *, Mohammad Hossein Aarabi, Fahimeh Talebi, Fatemeh Nejati, Zahra Jafari, Farzaneh Khalaji, Fatemeh Motaharian
Kashan University of Medical Sciences , mirhashemi@kaums.ac.ir
Abstract:   (28436 Views)

Background: Amylin is a 37-aa pancreatic hormone. It has been determined that an aggregation of amylin is associated with the pathogenesis of type 2 diabetes mellitus. This study aimed to evaluate the variations in aggregation potential in the presence and absence of Lead (Pb) and Selenium (Se).

Materials and Methods: The peptide stock solution was prepared by adding 1 ml Dimethyl Sulfoxide (DMSO). Stock solution (1mg/ml) was diluted with Krebs buffer (pH: 7.4) to a final concentration of 0.4 μM. The samples without the elements were selected as control. Selenium and Lead with concentration of 50 and 10 μM were prepared in the two separate groups, respectively. The last group included Se 50 μM +Pb10 μM in amylin solution. All samples were incubated at 37oC. To monitor the peptide folding, Thioflavin T (ThT) assay was performed and recorded by a fluorescence spectrometer.

Results: The obtained results showed that after 144 hour incubation, Selenium, decreased amylin aggregation by 30.2 % (P<0.05) and Pb increased the aggregation potential by 23.1 % (P<0.05). Combined effect of Se and Pb decreased the amylin aggregation by 9.52% compared to the Pb group.

Conclusion: According to the results of the study, Selenium not only reduced amylin aggregation significantly but also detoxified Pb toxicity. Therefore, it can be concluded that the toxic effects of amylin amyloid on pancreas may be reduced by Selenium.

Keywords: Amylin, Diabetes mellitus, Lead, Selenium
Full-Text [PDF 136 kb]   (934 Downloads)    
Type of Study: Research | Subject: General
Received: 2013/03/2 | Published: 2013/03/15

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Volume 16, Issue 7 (Supplement 2013) Back to browse issues page