Inhibition of human amylin aggregation by Flavonoid Chrysin: An in-silico and in-vitro approach.
Int J Med Sci
; 18(1): 199-206, 2021.
Article
en En
| MEDLINE
| ID: mdl-33390788
ABSTRACT
Islet amyloid polypeptide (amylin), consecrated by the pancreatic ß-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 ß-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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Contexto en salud:
6_ODS3_enfermedades_notrasmisibles
Problema de salud:
6_alzheimer_other_dementias
/
6_endocrine_disorders
/
6_mental_health_behavioral_disorders
Asunto principal:
Flavonoides
/
Diabetes Mellitus Tipo 2
/
Polipéptido Amiloide de los Islotes Pancreáticos
/
Enfermedad de Alzheimer
/
Agregación Patológica de Proteínas
Tipo de estudio:
Etiology_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Int J Med Sci
Asunto de la revista:
MEDICINA
Año:
2021
Tipo del documento:
Article
País de afiliación:
Arabia Saudita