Strategic Preparations of DPP-IV Inhibitory Peptides from Val-Pro-Xaa and Ile-Pro-Xaa Peptide Mixtures
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Strategic Preparations of DPP‑IV Inhibitory Peptides from Val‑Pro‑Xaa and Ile‑Pro‑Xaa Peptide Mixtures Changge Guan1,2 · Shun Iwatani2 · Xin‑hui Xing1 · Naoyuki Yamamoto2 Accepted: 29 September 2020 © Springer Nature B.V. 2020
Abstract Various peptides with inhibitory activity against human dipeptidyl peptidase-IV (hDPP-IV), which degrades glucagon-like peptide 1 (GLP-1) and decreases insulin release, were isolated from synthetic tripeptide mixtures, having sequences Val-ProXaa (VPX) or Ile-Pro-Xaa (IPX). All peptides isolated by reversed-phase high performance liquid chromatography (HPLC) analysis were measured for hDPP-IV inhibitory activity. VPV and VPI prepared from the VPX mixture and IPI isolated from the IPX mixture, showed the highest hDPP-IV inhibitory activity. The dissociation constants for hDPP-IV and IC50 values of the peptides were analyzed to understand the reason for the potent inhibitory activity of these tripeptides. The I C50 and Ki values of VPV, VPI, and IPI were found to be 20.2, 22.2, and 46.7 µM and 10.8, 11.3 and 21.4 M−1, respectively. Further, degradation of the peptides by the proteolytic action of hDPP-IV was analyzed to understand the stability of these peptides. Peptides with lower Ki and I C50 values showed relatively slower degradation when incubated with hDPP-IV. These results suggested that a peptide might have higher hDPP-IV inhibitory activity because of its higher affinity and stronger resistance to hDPP-IV, which is caused by the introduction of a hydrophobic amino acid at the C-terminal end of its VP or IP sequence. Keywords Val-Pro-Xaa (VPX) · Ile-Pro-Xaa (IPX) · hDPP-IV inhibitory peptide · Synthetic tripeptides
Introduction Many kinds of food derived bioactive peptides were previously isolated and reviewed (Chakrabarti et al. 2014; Maqsoudlou et al. 2019; Pessione and Cirrincione 2016; Marcone et al. 2017). Many of these peptides were found to have certain effects on human health, in many clinical trials (Hill and Newburg 2015; Akazawa et al. 2008; Dobenecker et al. 2018). Proteins obtained from major food materials were considered safe based on a history of consumption for a long period of time without any adverse effects, and advantageous due to their low cost and stable supply. The commonest food derived proteins were obtained from milk, soy, wheat, eggs,
* Naoyuki Yamamoto n‑[email protected] 1
MOE Key Laboratory for Industrial Biocatalysis, Department of Chemical Engineering, Institute of Biochemical Engineering, Tsinghua University, Beijing 100084, China
School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Kanagawa 226‑8501, Japan
2
rice, oat, meat, and fish (Rutherfurd-Markwick 2012; Fields et al. 2009; Moller et al. 2008). Currently, various peptides with DPP-IV inhibitory activity are developed from food derived protein hydrolysates to reduce appetite and diet uptakes (Silveira et al. 2013; Nongonierma et al. 2019, 2017). The induction of incretins, GLP-1 and glucose-dependent insulinotropic peptide (GIP), which
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