The primary structure identification of a corn peptide facilitating alcohol metabolism by HPLC–MS/MS

► The structure of corn peptides (CPs) with facilitating alcohol metabolism activity was researched. ► The primary structure of the CPs was preliminarily identified by HPLC–MS/MS. ► Then it was further identified by comparing with zein sequence in the MS database. ► It was a pentapeptide – Q-L-L-P-F...

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Published inPeptides (New York, N.Y. : 1980) Vol. 37; no. 1; pp. 138 - 143
Main Authors Ma, Zhi-Li, Zhang, Wen-Jun, Yu, Guo-Cai, He, Hui, Zhang, Yan
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.09.2012
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Summary:► The structure of corn peptides (CPs) with facilitating alcohol metabolism activity was researched. ► The primary structure of the CPs was preliminarily identified by HPLC–MS/MS. ► Then it was further identified by comparing with zein sequence in the MS database. ► It was a pentapeptide – Q-L-L-P-F. ► Its ability to facilitate alcohol metabolism was validated in vivo. The aim of this study is to identify the primary structure of corn peptides (CPs) with a facilitating alcohol metabolism effect. Corn protein was hydrolyzed by Alcalase first. The hydrolysate, crude corn peptides (CPs), was then fractionated through ultrafiltration technology. The primary structure of a peptide from the fraction (Mm<5kDa) was identified by HPLC–MS/MS, coupled with the peptide sequence retrieval using the MS–MS online database. The amino acid sequence of the peptide was determined as Q-L-L-P-F, and the pentapeptide was synthesized by Fmoc solid-phase peptide synthesis (SPPS) method. Its ability to facilitate alcohol metabolism was evaluated in vivo. Results showed that the synthetic peptide (10mg/kg) had a higher ability to eliminate alcohol in vivo compared to the mixed peptides (Mm<5kDa, 200mg/kg). In conclusion, the pentapeptide Q-L-L-P-F has a potent ability in facilitating alcohol metabolism, and this pentapeptide is the main bioactive component in the mixed peptides obtained from corn.
Bibliography:http://dx.doi.org/10.1016/j.peptides.2012.07.004
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0196-9781
1873-5169
DOI:10.1016/j.peptides.2012.07.004