Quantitative analysis of the relationship between structure and antioxidant activity of tripeptides.

Peptides from enzymatic hydrolysates of food proteins exhibit significant antioxidant activity. Several studies have attempted to determine the factors contributing to the antioxidant activity of peptides; however, the physicochemical properties and factors essential for the antioxidant activity of peptides are still unclear. In this study, in order to clarify the factors important for peptide antioxidant activity based on the properties of component amino acids, 55 tripeptides were synthesized from 20 natural amino acids and their antioxidant activity was measured using the Trolox equivalent antioxidant capacity (TEAC) assay system. The tripeptides were divided into two data sets: a training set comprising 50 compounds and a validated set comprising five compounds. The structure-activity relationship of the training set was then analyzed using classical quantitative structure-activity relationship (QSAR) analysis. The study findings demonstrate that the presence of a cysteine residue at any position, an aromatic amino acid at the C-terminus, higher hydrophobicity of the N-terminal residue, and smaller HOMO-LUMO energy gap of the middle residue can significantly enhance the antioxidant activity. The activities of the five validated compounds were predicted using the constructed QSAR model, and a good correlation between measured and predicted activities was observed. The information obtained from the QSAR model could be useful for effective production of antioxidant peptides from food proteins such as egg white proteins.

Intramolecular Interaction, Photoisomerization, and Mechanical C-C Bond Dissociation of 1,2-Di(9-anthryl)benzene and Its Photoisomer: A Fundamental Moiety of Anthracene-Based π-Cluster Molecules.

We report variable and unique properties of 1,2-di(9-anthryl)benzene 1 as a fundamental moiety of anthracene-based π-cluster molecules. Due to a through-space π-conjugation between anthracene units, excimer emission at room temperature and charge delocalized state in radical cation state of 1 could be observed. Photoirradiation to 1 afforded an intramolecular [4 + 4] cyclized anthracene dimer 1' having a high strain energy with long C-C bond that exceeded 1.68 Å, resulting in C-C bond dissociation by simple mechanical grinding.

The glycerol-3-phosphate acyltransferase PLAT2 functions in the generation of DHA-rich glycerolipids in Aurantiochytrium limacinum F26-b.

Thraustochytrids possess docosahexaenoic acid (DHA, 22:6n-3) as acyl chain(s) of triacylglycerol (TG) and phosphatidylcholine (PC), some of which contain multiple DHAs. However, little is known about how these DHA-rich glycerolipids are produced in thraustochytrids. In this study, we identified PLAT2 in Aurantiochytrium limacinum F26-b as a glycerol-3-phosphate (G3P) acyltransferase (GPAT) by heterologous expression of the gene in budding yeast. Subsequently, we found that GPAT activity was reduced by disruption of the PLAT2 gene in A. limacinum, resulting in a decrease in DHA-containing lysophosphatidic acid (LPA 22:6). Conversely, overexpression of PLAT2 increased both GPAT activity and LPA 22:6. These results indicate that PLAT2 is a GPAT that transfers DHA to G3P in vivo as well as in vitro. Overexpression of the PLAT2 gene increased the production of a two DHA-containing diacylglycerol (DG 44:12), followed by an increase in the three DHA-containing TG (TG 66:18), two-DHA-containing TG (TG 60:12), and two DHA-containing PC (PC 44:12). However, overexpression of PLAT2 did not increase DHA-free DG (DG32:0), which was preferentially converted to three 16:0-containing TG (TG 48:0) but not two 16:0-containing PC (PC 32:0). Collectively, we revealed that DHA-rich glycerolipids are produced from a precursor, LPA 22:6, which is generated by incorporating DHA to G3P by PLAT2 in the A. limacinum.

Egg white hydrolysate improves fatigue due to short-term swimming load test in mice.

We studied the effect of egg white hydrolysate (EWH) on swimming endurance in mice. 7-week-old male ddY mice (28-30 g) were divided into three groups and fed an AIN-93G diet supplemented with casein (n = 8), EWH (n = 7), or egg white protein (EWP, n = 8) for 14 days. From day 11, the mice underwent a swimming test daily with a weight load equivalent to 10% of their body weight, and the lengths of time they swam were recorded. Blood was sampled for testing on the last day of the study. We observed that increases in the swimming duration through day 14 were significantly greater in the EWH group than in the casein group (p = 0.049). As a factor underlying this, the hexanoyl-lysine level in blood was confirmed to be decreased in the former group (p = 0.013). These findings indicate that consumption of EWH extended the swimming duration and suggest the mechanistic involvement of an antifatigue effect mediated by its antioxidant activity.