To evaluate likely antiamyloidogenic property of ferulic acid and baicalein against human islet amyloid polypeptide aggregation, in vitro Study

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Type 2 diabetes mellitus is a common endocrine disorder in which carbohydrates, fats and proteins metabolism have been interrupted and results in diabetic compli-cations include cardiac abnormality, diabetic retinopathy, nephropathy and atherosclerosis (Naqshbandi et al., 2008). The etiology of diabetes and its complications is still not clear; but it has been implicated that human islet amyloid polypeptide (hIAPP) aggregates in type II diabetics to form oligomers that interfere with beta-cell function, eventually leading to the loss of insulin production (Reddy et al., 2011). Human Islet Amyloid Polypeptide (hIAPP, also known as amylin) is a 37 residue peptide hormone secreted from pan-creatic β-cells (Brender et al., 2008). In its normal physiological role, hIAPP is associated with appetite suppression and, in conjunction with insulin, in maintaining proper glycemic