Calcium-binding properties, stability, and osteogenic ability of phosphorylated soy peptide-calcium chelate

Abstract

IntroductionBioactive peptides based on foodstuffs are of particular interest as carriers for calcium delivery due to their safety and high activity. The phosphorylated peptide has been shown to enhance calcium absorption and bone formation.MethodA novel complex of peptide phosphorylation modification derived from soybean protein was introduced, and the mechanism, stability, and osteogenic differentiation bioactivity of the peptide with or without calcium were studied.ResultThe calcium-binding capacity of phosphorylated soy peptide (SPP) reached 50.24 ± 0.20 mg/g. The result of computer stimulation and vibration spectrum showed that SPP could chelate with calcium by the phosphoric acid group, carboxyl oxygen of C-terminal Glu, Asp, and Arg, and phosphoric acid group of Ser on the SPP at a stoichiometric ratio of 1:1, resulting in the formation of the complex of ligand and peptide. Thermal stability showed that chelation enhanced peptide stability compared with SPP alone. Additionally, in vitro results showed that SPP-Ca could facilitate osteogenic proliferation and differentiation ability.DiscussionSPP may function as a promising alternative to current therapeutic agents for bone loss.

Characterization and Mechanism of a Novel Rice Protein Peptide (AHVGMSGEEPE) Calcium Chelate in Enhancing Calcium Absorption in Caco-2 Cells

“…Additionally, the absorption intensity increased from 2.146 to 2.253. The increased absorption intensity could potentially stem from changes in the electronic cloud of the amide bond and the light absorption characteristics of the ligand caused by binding to Ca 2+ as reflected in the results of quantum chemistry. Wang et al found that the absorption band intensity of purified peptide–calcium complex FVDVT-Ca significantly increased .…”

“…The content of acidic amino acids in bioactive peptides is closely related to their calcium ion binding ability. 30 Therefore, in this experiment, the top 10 peptide segments containing a minimum of three acidic amino acids and with the highest abundance in RPP (LEKPEGADLE, LIEKHEGGLEE, IE-KHEGGLEE, VAGSAPGIEGDEIAPL, LTESQSQSHKFK-DEHQ, RVDEDREEL, LEEQKGSDVM, EVEERSQNIFSG, AHVGMSGEEPE and ISGFEGDNMIER) were chosen as the receptor and ligand for molecular docking with Ca 2+ (Figure 1A and Supporting Figure 1). The length of these peptides ranged from 9 to 16 amino acids, and their mass ranged from 1100 to 2057 Da (Table 1).…”