ArticleJournal of food and drug analysis2016
High performance liquid chromatography (HPLC) fingerprints and primary structure identification of corn peptides by HPLC-diode array detection and HPLC-electrospray ionization tandem mass spectrometry.
Article in Journal of food and drug analysis, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 17 citations in OpenAlex.
- Bioactive Peptides from Corn (Biology · 2024Review
- Quality Evaluation of Peony Petals Based on the Chromatographic Fingerprints and Simultaneous Determination of Sixteen Bioactive Constituents Using UPLC-DAD-MS/MS.Molecules (Basel, Switzerland) · 2023Article
- Procyanidins: a comprehensive review encompassing structure elucidation via mass spectrometry.Phytochemistry reviews : proceedings of the Phytochemical Society of Europe · 2018Article
- The Structure-Activity Relationship of the Antioxidant Peptides from Natural Proteins.Molecules (Basel, Switzerland) · 2016Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Corn peptides (CPs) are reported to have many biological functions, such as facilitating alcohol metabolism, antioxidation, antitumor, antihypertension, and hepatoprotection. To develop a method for quality control, the high-performance liquid chromatography (HPLC) system was applied. Twenty-eight common peaks were found in all the CPs of corn samples from Enshi, China, based on which, a fingerprinting chromatogram was established for use in quality control in future research. Subsequently, the major chemical constituents of these common peaks were identified respectively using the HPLC-diode-array detection electrospray ionization tandem mass spectrometry (DAD-ESI-MS/MS) system, and 48 peptide fractions were determined ultimately. This was the first time for the majority of these peptides to be reported, and many of them contained amino acids of glutamine (Q), L and A, which might play an important role in the exhibition of the bioactivities of CPs. Many peptides had a similar primary structure to the peptides which had been proven to be bioactive such as facilitating alcohol metabolism, scavenging free radicals, and inhibiting lipid peroxidation. This systematical analysis of the primary structure of CPs facilitated subsequent studies on the relationship between the structures and functions, and could accelerate holistic research on CPs.
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Registered trials
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