Design and Synthesis of Novel Peptides to Protect Ferulic Acid against Ultraviolet Radiation Based on Domain Site IIA of Bovine Serum Albumin

Abstract

Ferulic acid (FA) is known for its excellent antioxidant properties, which can provide many health benefits. One of its drawbacks is its instability under UVA light, which limits its potency. In this study, the new peptides LW2 (QNKRFYFRKNQ) and CW2 (a cyclic form of LW2) were designed based on bovine serum albumin site IIA conformation. A UVA irradiation experiment was performed to investigate the protective ability of these peptides towards FA against UVA damage. The percentages of FA remaining under UV irradiation due to the protection of CW2 and LW2 were 83% and 76%, respectively. The results showed the importance of the cationic residues and hydrophobic residues included in the peptide sequences. Moreover, the cyclic rigid structure showed greater protective ability as compared to its linear counterpart.

Review of the Specific Features, and New Demands for Antibacterial Peptides

“…CW2 could protect FA, showing a reservation ratio of 83% after 12 h of exposure to UVA. As shown in Figure 3, the cationic and hydrophobic moieties of CW2 were essential to enhance the electrostatic and hydrophobic interactions with FA, respectively [43]. The authors suggested that the presence of the rigid cyclic structure is important to protect FA against destructive effects of UVA.…”

“…The authors also estimated the importance of the positively charged Arginine amino acid computationally using Molecular Operating Environment MOE 2018.0 software (Chemical Computing Group, Canada). The computational simulation of the minimized structure of CW2 demonstrated the great role of arginine in initiating electrostatic interaction with FA [43].…”