Purification and identification of a novel antidiabetic peptide from Chinese giant salamander (Andrias davidianus) protein hydrolysate against α-amylase and α-glucosidase

Abstract

This study aimed to purify and identify a novel antidiabetic peptides from Chinese giant salamander (Andrias davidianus) protein hydrolysate and to evaluate its anti-diabetic properties against α-amylase and α-glucosidase. The isolation was done by gel filtration, reverse phase chromatography (RF-HLPC), and finally peptide and amino acid sequences were identified by LC/MS/MS system. Our results revealed five novel peptides that strongly inhibited α-amylase and αglucosidase. The peptides' amino acid sequences were Cys-Ser-Ser-Val (MW = 393.99 Da), Tyr-Ser-Phe-Arg (MW = 570.99 Da), Ser-Ala-Ala-Pro (MW = 343.89 Da), Pro-Gly-Gly-Pro (MW = 325.99 Da) and Leu-Gly-Gly-Gly-Asn (MW = 415.99 Da) possessing α-amylase inhibitory activity IC 50 of 13.76 × 10 3 , 10.82 × 10 3 , 4.46 × 10 3 , 4.23 × 10 3 , and 2.86 × 10 3 µg/mL, respectively; and for αglucosidase with IC 50 of 206. 00, 162.00, 66.90, 63.50, and 42.93 µg/mL, respectively. Intriguingly, the peptide LGGGN showed higher inhibition on both αamylase and α-glucosidase and could be considered as a potential anti-diabetic inhibitor. ARTICLE HISTORY

Characteristics of New Peptides GQLGEHGGAGMG, GEHGGAGMGGGQFQPV, EQGFLPGPEESGR, RLARAGLAQ, YGNPVGGVGH, and GNPVGGVGHGTTGT as Inhibitors of Enzymes Involved in Metabolic Syndrome and Antimicrobial Potential

“…Glucose absorption into the bloodstream in patients with insulin disorders causes a sharp increase in the blood glucose level, which may lead to development of the disease [11]. Peptides with enzyme inhibitory activity involved in polysaccharide metabolism and exhibiting a potent anti-diabetic effect were described previously: CSSV, YSPR, SAAP, PGGP, and LGGGNT [12], or LPLLR [13] Fats are energy-delivering molecules. Before being absorbed in the small intestine, they should be hydrolyzed by lipase into monoglycerol and free fatty acids.…”

Phytopharmacological Strategies in the Management of Type 2 Diabetes Mellitus

“…Protein hydrolysate from Chinese giant salamander (Andrias davidianus) was evaluated for its potential inhibitory activity against alpha-amylase and alpha-glucosidase, with further purification and identification of antidiabetic peptides [78]. The peptides amino acid sequences were Cys-Ser-Ser-Val, Tyr-Ser-Phe-Arg, Ser-Ala-Ala-Pro, Pro-Gly-Gly-Pro, and Leu-Gly-Gly-Gly-Asn with alpha-amylase IC 50 values of 13.76 × 10 3 , 10.82 × 10 3 , 4.46 × 10 3 , 4.23 × 10 3 and 2.86 × 10 3 , respectively; and with alpha-glucosidase IC 50 values of 206.00, 162.00, 66.90, 63.50, and 42.93 µg/mL, respectively [78]. Garza and colleagues also reported the inhibition of alpha-amylase by valoneaic acid dilactone obtained from banaba (Lagerstroemia speciosa), ethanol extract of chestnut astringent skin, and a purified compound isolated from white beans (Phaseolus vulgaris) [22].…”

Marine Bioactive Peptides—An Overview of Generation, Structure and Application with a Focus on Food Sources

“…Difference in percentages of different AA residues in peptides with particular bioactivity can be explained through correlations between structure and function. For example, a high percentage of hydrophobic (aliphatic and aromatic) AA residues in antidiabetic peptides (Figure 4) [109][110][111] is necessary for inhibition of dipeptidyl peptidase IV, a key enzyme involved in degradation of incretins [110,112,113], and for recognition of receptors for glucagon-like peptides [114,115]. A high percentage of negatively charged AA residues (Figure 4) has been reported in antithrombotic peptides showing both direct thrombin inhibition [116,117] and inhibition of factors in intrinsic pathways [72,118].…”