In a previous study, the peptide LGKDQVRT, which was identified by enzymatic hydrolysis, released during the proteolysis of , had potential osteogenic activity. In this study, the octapeptide LGKDQVRT was able to spontaneously bind calcium in a 1:1 stoichiometric ratio, and the calcium-binding site likely involves calcium and amino acid VAL6 in the LGKDQVRT peptide to form a metal-donor to metal acceptor complex. The peptide LGKDQVRT has the activity of promoting the proliferation and differentiation of osteoblasts. The results of this study suggest that hydrolyzed peptides from protein can be used as a dietary supplement to improve calcium absorption and prevent osteoporosis.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9016177 | PMC |
| http://dx.doi.org/10.3389/fnut.2022.840638 | DOI Listing |
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Characterization of Chelation and Absorption of Calcium by a Derived Osteogenic Peptide.
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Key Laboratory of Biotechnology and Bioresources Utilization, College of Life Sciences, Dalian Minzu University, Ministry of Education, Dalian, China.
In a previous study, the peptide LGKDQVRT, which was identified by enzymatic hydrolysis, released during the proteolysis of , had potential osteogenic activity. In this study, the octapeptide LGKDQVRT was able to spontaneously bind calcium in a 1:1 stoichiometric ratio, and the calcium-binding site likely involves calcium and amino acid VAL6 in the LGKDQVRT peptide to form a metal-donor to metal acceptor complex. The peptide LGKDQVRT has the activity of promoting the proliferation and differentiation of osteoblasts.
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