Int J Med Sci 2021; 18(1):199-206. doi:10.7150/ijms.51382 This issue

Research Paper

Inhibition of human amylin aggregation by Flavonoid Chrysin: An in-silico and in-vitro approach

Abdullah A. Alkahtane1, Hamzah A. Alghamdi1, Bader Almutairi1, Mohd Muazzam Khan2, Md Saquib Hasnain3, Mohamed M. Abdel-Daim1,4, Wadha M. Alghamdi5, Saad Alkahtani1✉

1. Department of Zoology, College of Science, King Saud University, Riyadh, Saudi Arabia.
2. Department of Pharmacology, Faculty of Pharmacy, Integral University, Lucknow, India.
3. Department of Pharmacy, Shri Venkateshwara University, NH-24, Rajabpur, Gajraula, Amroha - 244236, U.P., India.
4. Pharmacology Department, Faculty of Veterinary Medicine, Suez Canal University, Ismailia 41522, Egypt.
5. Medical Services at the Ministry of Interior, Riyadh, Saudi Arabia.

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Citation:
Alkahtane AA, Alghamdi HA, Almutairi B, Khan MM, Hasnain MS, Abdel-Daim MM, Alghamdi WM, Alkahtani S. Inhibition of human amylin aggregation by Flavonoid Chrysin: An in-silico and in-vitro approach. Int J Med Sci 2021; 18(1):199-206. doi:10.7150/ijms.51382. Available from https://www.medsci.org/v18p0199.htm

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Abstract

Islet amyloid polypeptide (amylin), consecrated by the pancreatic β-cells with insulin, has a significant role to play in maintaining homeostasis of islet cell hormones. Alzheimer's disease is the predominant source of dementia. However, its etiology remains uncertain; it appears that type 2 diabetes mellitus and other prediabetic states of insulin resistance contribute to the intermittent Alzheimer's disease presence. Amylin is abnormally elevated in Type II diabetes patients, accumulated into amylin aggregates, and ultimately causes apoptosis of the β-cells, and till date, its mechanism remains unclear. Several flavonoids have inhibitory effects on amylin amyloidosis, but its inhibition mechanisms are unknown. Screening a collection of traditional compounds revealed the flavone Chrysin, a potential lead compound. Chrysin inhibits amyloid aggregate formation according to Thioflavin T binding, turbidimetry assay. We report results of molecular interaction analysis of Chrysin with amylin which shows potent binding affinity against amylin. Pharmacokinetics and Drug likeness studies of Chrysin also suggest that it is a potential lead compound. Therefore, Chrysin prevented amylin aggregation.

Keywords: Islet amyloid polypeptide, Chrysin, flavonoids, amylin aggregation