Purification, Identification and Functional Analysis of a Novel Immunomodulatory Peptide from Silkworm Pupa Protein
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....
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Published in | International journal of peptide research and therapeutics Vol. 26; no. 1; pp. 243 - 249 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Dordrecht
Springer Netherlands
01.03.2020
Springer Nature B.V |
Subjects | |
Online Access | Get full text |
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Summary: | 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 µg/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-κB, 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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ISSN: | 1573-3149 1573-3904 |
DOI: | 10.1007/s10989-019-09832-4 |