Biophysical and in vitro absorption studies of iron chelating peptide from barley proteins
Isothermal titration calorimetry (ITC) and tandem mass spectrometry (MS/MS) were used to study the interaction between Fe2+ and the heptapeptide (SVNVPLY) from barley protein hydrolysate under physiological pH. The peptide showed an ability to form complexes with Fe2+ spontaneously, with a binding c...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2016-08-01
|
| Series: | Journal of Functional Foods |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1756464616301542 |
| _version_ | 1818406141937319936 |
|---|---|
| author | Ewelina Eckert Lei Lu Larry D. Unsworth Lingyun Chen Jianhong Xie Renyi Xu |
| author_facet | Ewelina Eckert Lei Lu Larry D. Unsworth Lingyun Chen Jianhong Xie Renyi Xu |
| author_sort | Ewelina Eckert |
| collection | DOAJ |
| description | Isothermal titration calorimetry (ITC) and tandem mass spectrometry (MS/MS) were used to study the interaction between Fe2+ and the heptapeptide (SVNVPLY) from barley protein hydrolysate under physiological pH. The peptide showed an ability to form complexes with Fe2+ spontaneously, with a binding constant reaching 107 L mol−1. Two peptide binding sites were identified and amino acid residues like Leu, Val, Pro and Tyr have been recognized as critical for iron coordination. The capacity for the heptapeptide and its shorter tripeptide analogue (VPL) to improve iron absorption was studied in vitro using Caco-2 cells. The cell uptake increased 4 times for the Fe2+–SVNVPLY complex after pepsin–pancreatin digestion compared to the iron sulfate salt. The ferritin formation in the Caco-2 cells was also significantly enhanced when iron was chelated to the peptides. This research suggests a potential application of barley peptides as dietary supplements to improve iron absorption. |
| first_indexed | 2024-12-14T09:07:14Z |
| format | Article |
| id | doaj.art-6a7172528bd149de91af85fe0ca4d099 |
| institution | Directory Open Access Journal |
| issn | 1756-4646 |
| language | English |
| last_indexed | 2024-12-14T09:07:14Z |
| publishDate | 2016-08-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Functional Foods |
| spelling | doaj.art-6a7172528bd149de91af85fe0ca4d0992022-12-21T23:08:40ZengElsevierJournal of Functional Foods1756-46462016-08-0125291301Biophysical and in vitro absorption studies of iron chelating peptide from barley proteinsEwelina Eckert0Lei Lu1Larry D. Unsworth2Lingyun Chen3Jianhong Xie4Renyi Xu5Canadian Research Chair in Plant Protein, Structure Function and Nutraceutical Delivery, Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, T6G 2P5, CanadaDepartment of Chemical and Materials Engineering, University of Alberta, 9107 - 116 Street, Edmonton, Alberta, T6G 2V4, Canada; National Research Council (Canada), National Institute for Nanotechnology, 11421 Saskatchewan Drive, Edmonton, Alberta, T6G 2M9, CanadaDepartment of Chemical and Materials Engineering, University of Alberta, 9107 - 116 Street, Edmonton, Alberta, T6G 2V4, Canada; National Research Council (Canada), National Institute for Nanotechnology, 11421 Saskatchewan Drive, Edmonton, Alberta, T6G 2M9, CanadaCanadian Research Chair in Plant Protein, Structure Function and Nutraceutical Delivery, Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, T6G 2P5, Canada; Corresponding author. Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, T6G 2P5, Canada. Tel.: +1 780 492 0038; fax: +1 780 492 4265.Wuhan Sanjiang Space Good Biotech Co., Ltd, Suizhou, Hubei 432700, ChinaWuhan Sanjiang Space Good Biotech Co., Ltd, Suizhou, Hubei 432700, ChinaIsothermal titration calorimetry (ITC) and tandem mass spectrometry (MS/MS) were used to study the interaction between Fe2+ and the heptapeptide (SVNVPLY) from barley protein hydrolysate under physiological pH. The peptide showed an ability to form complexes with Fe2+ spontaneously, with a binding constant reaching 107 L mol−1. Two peptide binding sites were identified and amino acid residues like Leu, Val, Pro and Tyr have been recognized as critical for iron coordination. The capacity for the heptapeptide and its shorter tripeptide analogue (VPL) to improve iron absorption was studied in vitro using Caco-2 cells. The cell uptake increased 4 times for the Fe2+–SVNVPLY complex after pepsin–pancreatin digestion compared to the iron sulfate salt. The ferritin formation in the Caco-2 cells was also significantly enhanced when iron was chelated to the peptides. This research suggests a potential application of barley peptides as dietary supplements to improve iron absorption.http://www.sciencedirect.com/science/article/pii/S1756464616301542Barley protein peptideIron-chelating peptideBinding affinityComplexation modelIron uptakeFerritin |
| spellingShingle | Ewelina Eckert Lei Lu Larry D. Unsworth Lingyun Chen Jianhong Xie Renyi Xu Biophysical and in vitro absorption studies of iron chelating peptide from barley proteins Journal of Functional Foods Barley protein peptide Iron-chelating peptide Binding affinity Complexation model Iron uptake Ferritin |
| title | Biophysical and in vitro absorption studies of iron chelating peptide from barley proteins |
| title_full | Biophysical and in vitro absorption studies of iron chelating peptide from barley proteins |
| title_fullStr | Biophysical and in vitro absorption studies of iron chelating peptide from barley proteins |
| title_full_unstemmed | Biophysical and in vitro absorption studies of iron chelating peptide from barley proteins |
| title_short | Biophysical and in vitro absorption studies of iron chelating peptide from barley proteins |
| title_sort | biophysical and in vitro absorption studies of iron chelating peptide from barley proteins |
| topic | Barley protein peptide Iron-chelating peptide Binding affinity Complexation model Iron uptake Ferritin |
| url | http://www.sciencedirect.com/science/article/pii/S1756464616301542 |
| work_keys_str_mv | AT ewelinaeckert biophysicalandinvitroabsorptionstudiesofironchelatingpeptidefrombarleyproteins AT leilu biophysicalandinvitroabsorptionstudiesofironchelatingpeptidefrombarleyproteins AT larrydunsworth biophysicalandinvitroabsorptionstudiesofironchelatingpeptidefrombarleyproteins AT lingyunchen biophysicalandinvitroabsorptionstudiesofironchelatingpeptidefrombarleyproteins AT jianhongxie biophysicalandinvitroabsorptionstudiesofironchelatingpeptidefrombarleyproteins AT renyixu biophysicalandinvitroabsorptionstudiesofironchelatingpeptidefrombarleyproteins |