Antioxidative peptides from proteolytic hydrolysates of false abalone (volutharpa ampullacea perryi): Characterization, identification, and molecular docking

Shudong He, Yi Zhang, Hanju Sun, Ming Du, Jianlei Qiu, Mingming Tang, Xianbao Sun, Beiwei Zhu

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

Abstract

Antioxidative peptides were produced from false abalone (Volutharpa ampullacea perryi) using enzymatic hydrolysis. Trypsin produced the most bioactive hydrolysates with the highest scavenging ABTS+• free radicals compared to pepsin, alcalase, neutrase, and flavourzyme. The response surface methodology studies on trypsin hydrolysis indicated that the hydrolysis temperature, time, and pH were interacted with each other (p < 0.05), and the optimal conditions were hydrolysis at 51.8C for 4.1 h, pH 7.7 and the maximum predicted hydrolysis degree was 13.18% and ABTS+• scavenging activity of 79.42%. The optimized hydrolysate was subjected to ultrafiltration fractionation, and the fraction with MW < 3 kDa showed the highest ABTS+• scavenging activity. There were 193 peptide sequences identified from this peptide fraction and 133 of them were successfully docked onto human myeloperoxidase (MPO), an enzyme involved in forming reactive oxidants in vivo. The highest scored peptide, no. 39, consists of DTETGVPT. Its structure and molecular interactions with MPO active site were compared with previously characterized peptide hLF1-11. The interactions between peptide no. 39 and MPO include electrostatic charge, hydrogen bonds, and covalent bonds. The antioxidative peptide produced in this research may exert antioxidant activity in vivo due to its potential inhibition effect on MPO.

Original languageEnglish (US)
Article number116
JournalMarine Drugs
Volume17
Issue number2
DOIs
StatePublished - Feb 13 2019

All Science Journal Classification (ASJC) codes

  • Drug Discovery

Fingerprint

Dive into the research topics of 'Antioxidative peptides from proteolytic hydrolysates of false abalone (volutharpa ampullacea perryi): Characterization, identification, and molecular docking'. Together they form a unique fingerprint.

Cite this