数字农科院2.0

Purification, Identification And Functional Analysis Of A Novel Immunomodulatory Peptide From Silkworm Pupa Protein

文献类型： 外文期刊

作者： Jin, Byung Rae;Lee, Kwang Sik;Xin, Xiangdong;Zhang, Bei;Li, Zhiyong;Zhao, Shan;Gui, Zhongzheng;Gui, Zhongzheng;Thomas, Attaribo;Charles, Asakiya

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关键词： Silkworm Pupa Protein; Immunomodulatory Peptide; Purification; Identification

期刊名称： INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS

ISSN： 1573-3149

年卷期： 2020 年 26 卷 1 期

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摘要： In this study, we isolated and characterized an immunomodulatory peptide from silkworm (Bombyx mori) pupa protein hydrolysates. Ultrasound-pretreated hydrolysates were prepared by alcalase digestion and their pro-proliferative activity was assessed with the splenic lymphocyte proliferation assay. Peptide fractions exhibiting the highest activity were purified by Sephadex-G100 and -G15 gel filtration chromatography. The structure of the purified peptides was analyzed using Liquid Chromatography Electrospray Ionisation Tandem Mass Spectrometry (LC-ESI-MS/MS); their digestive stability and their effects of the expression on immune-related cytokines were also evaluated. We purified a novel immunomodulatory peptide with a molecular weight of about 441.06 Da. The amino acid sequence was Asp-His-Ala-Val (DHAV). The splenocyte proliferation rate was 91.1% (P < 0.05) in the presence of 100 mu g/mL purified peptide. DHAV was stable in the presence of the gastrointestinal proteases pepsin and trypsin, and stimulated the expression of immune-related factors including interleukin-6 and -12, nuclear factor-kappa B, cyclin D1, and cyclin-dependent kinase 4. Thus, DHAV purified from silkworm pupa protein hydrolysate has immunomodulatory activity and potential therapeutic value.

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