{'fraction_non_alphanumeric': 0.021775544388609715, 'fraction_numerical': 0.0, 'mean_word_length': 5.390374331550802, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Dihydrolipoic acid as an effective cofactor for peptide methionine sulfoxide reductase in enzymatic repair of oxidative damage to both lipid-free and lipid-bound apolipoprotein a-I.

The aim of this study was to examine the possible use of dihydrolipoic acid (DHLA), the reduced form of lipoic acid, in the reduction of oxidized apolipoprotein A-I mediated by peptide methionine sulfoxide reductase (PMSR), and to test the accessibility of methionine sulfoxides in the lipid-bound oxidized apolipoprotein A-I to this reaction. We show that DHLA acts as an effective cofactor for PMSR, mediating restoration of the native secondary structure, tertiary structure, stability, and lipid-binding properties of the native unoxidized protein. Reconstituted high-density lipoproteins were used to demonstrate effective enzymatic reduction of the lipid-bound oxidized protein in the presence of DHLA. These findings suggest that the enzymatic repair of oxidative damage to intact lipoproteins could provide a model of a possible repair mechanism active in vivo during oxidative stress and that the restoration of high-density lipoprotein function could be one of the therapeutic benefits of lipoic acid.