Abstract
Five new acylated aminooligosaccharides (1–5), together with one known related analogue (6), were isolated from Streptomyces sp. HO1518. Their structure was identified by extensive spectroscopic analysis, including 1D and 2D NMR data and high resolution electrospray ionization mass spectrometry (HRESIMS), and by comparison with those reported in the literature. All of the new compounds showed more promising porcine pancreatic α-amylase (PPA) inhibitory activities than the clinical drug acarbose, indicating them as potential pharmaceutical drug leads toward type II diabetes.
Highlights
Introduction αAmylase, belonging to glycoside hydrolase family 13 (GH 13), is widely found in organisms, including plants, animals, bacteria, and fungi [1]
This paper describes the This isolation, structural elucidation, and structural inhibitory activity of these metabolites
In our screening program to search for α-amylase inhibitors from the Yellow Sea marine actinomycetes, we evaluated compounds 1–5 for their inhibitory activity against porcine pancreatic α-amylase (PPA) and the results revealed that all new isolates showed promising PPA inhibitory activities with IC50 values ranging from 0.03 to 0.70 μM (Table 3), of which 1 (0.029 μM) and 2 (0.049 μM), being similar to 6, were ca. 540- and 320-fold, while 3–5 were ca. 23- to 80-fold, stronger than the positive control acarbose (15.7 μM)
Summary
Amylase, belonging to glycoside hydrolase family 13 (GH 13), is widely found in organisms, including plants, animals, bacteria, and fungi [1]. It is an endoamylas, which catalyzes the hydrolysis of α-(1 → 4)-D-glucosidic bind of starch, amylase, amylopectin, glycogen, and various maltodextrins into smaller oligomers [2]. The well-known acarbose, originated from Actinoplanes species, is recognized as one of the most clinically important α-amylase inhibitor [4]. It is a member of the aminooligosaccharides family exclusively produced by microorganisms, soil bacteria of the order of Actinomycetes.
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