An identified antioxidant peptide obtained from ostrich (Struthio camelus) egg white protein hydrolysate shows wound healing properties. (August 2015)

• Record Type: Journal Article
• Authors: Homayouni-Tabrizi, Masoud; Asoodeh, Ahmad; Abbaszadegan, Mohammad-Reza; Shahrokhabadi, Khadijeh; Nakhaie Moghaddam, Mahboobeh
• Is Part Of: Pharmaceutical biology. Volume 53:Number 8(2015:Aug.)
• Page Start: 1155
• Page End: 1162
• Publication Date: 2015-08
• Subjects: Pharmacognosy -- Periodicals; Materia medica, Vegetable -- Periodicals; 615.321
• DOI: 10.3109/13880209.2014.962061
• Languages: English
• ISSNs: 1388-0209

Abstract

<abstract> <title>Abstract</title> <p> <italic>Context</italic>: Ostrich (<italic>Struthio camelus</italic>) egg possesses a high amount of food proteins and thus plays an important role in nutrition.</p> <p> <italic>Objective</italic>: Ostrich egg white proteins were hydrolyzed with pepsin and pancreatin to examine its antioxidant properties and further characterized the most active peptide.</p> <p> <italic>Materials and methods</italic>: Ostrich egg white protein hydrolysate (OEWPH) was fractionized using reversed phase high-pressure liquid chromatography (HPLC). The antioxidant activity of OEWPH and its HPLC fraction were investigated based on their scavenging capacity1, 1-diphenyl-2-picrylhydrazyl (DPPH) radical, 2, 2′-azinobis (3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS), superoxide (<inline-formula><tex-math notation="TeX"><![CDATA[\def\newpage{\vfill \break } \nopagenumbers $ {\rm O}_2^{ \bullet - } $ \newpage \end]]></tex-math></inline-formula>), hydroxyl (OH<sup>−</sup>) radicals, and Cu<sup>+2</sup> chelating. In a wound healing assay, paravertebral excision (1 cm diameter) was made on the skin and the percentage of wound closure was measured at defined intervals (0, 3, 7, and 14 d).</p> <p> <italic>Results</italic>: A potent antioxidant peptide named DG-10 with the sequence DAESLSRLLG (<italic>M</italic><sub>W</sub>: 1060.18 ± 0.5 Da) was identified from OEWPH. The peptide DG-10 showed DPPH (IC<sub>50</sub> = 0.0085 mg/ml), ABTS<sup>+</sup> (IC<sub>50</sub> = 0.56 mg/ml), superoxide (IC<sub>50</sub> = 0.36 mg/ml), and hydroxyl (IC<sub>50</sub> = 0.4 mg/ml) radical scavenger and copper chelating activity (IC<sub>50</sub> = 0.28 mg/ml). <italic>In vitro</italic> cultured HFLF-pI 5, the cell model, also revealed that DG-10 could protect HFLF-pI 5 cells against H<sub>2</sub>O<sub>2</sub>-treated necrosis. Ointment composed of DG-10 peptide exhibited wound-healing properties on adult rats (Wistar strain). The percentage of wound closure in peptide-treated group was 98% by day 14.</p> <p> <italic>Discussion and conclusion</italic>: Our results suggested that DG-10 is a natural agent obtained from ostrich egg possessing considerable antioxidant and wound-healing properties.</p> </abstract>