Antioxidant Activity, Stability  in Aqueous Medium and Molecular Docking/Dynamics Study of 6-Amino- and N-Methyl-6-amino-L-ascorbic Acid

Saftić Martinović Lara; Birkić Nada; Miletić Vedran; Antolović Roberto; Štanfel Danijela; Wittine Karlo

doi:Doi.org/10.3390/ijms24021410

Pregled bibliografske jedinice broj: 1244557

Antioxidant Activity, Stability in Aqueous Medium and Molecular Docking/Dynamics Study of 6-Amino- and N-Methyl-6-amino-L-ascorbic Acid

Saftić Martinović Lara; Birkić Nada; Miletić Vedran; Antolović Roberto; Štanfel Danijela; Wittine Karlo

Antioxidant Activity, Stability in Aqueous Medium and Molecular Docking/Dynamics Study of 6-Amino- and N-Methyl-6-amino-L-ascorbic Acid // International journal of molecular sciences, 24 (2023), 1410; 24021410, 18 doi:.org/10.3390/ijms24021410 (međunarodna recenzija, članak, znanstveni)

CROSBI ID: 1244557 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Antioxidant Activity, Stability in Aqueous Medium and Molecular Docking/Dynamics Study of 6-Amino- and N-Methyl-6-amino-L-ascorbic Acid

Autori
Saftić Martinović Lara ; Birkić Nada ; Miletić Vedran ; Antolović Roberto ; Štanfel Danijela ; Wittine Karlo

Izvornik
International journal of molecular sciences (1422-0067) 24 (2023), 1410; 24021410, 18

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
ascorbic acid ; antioxidant ; stability ; peroxiredoxin ; molecular docking/dynamics ; ABTS ; DPPH ; MS/MS

Sažetak
The antioxidant activity and chemical stability of 6-amino-6-deoxy-L-ascorbic acid (D1) and N-methyl- 6-amino-6-deoxy-L-ascorbic acid (D2) were examined with ABTS and DPPH assays and compared with the reference L-ascorbic acid (AA). In addition, the optimal storing conditions, as well as the pH at which the amino derivatives maintain stability, were determined using mass spectrometry. Comparable antioxidant activities were observed for NH-bioisosteres and AA. Moreover, D1 showed higher stability in an acidic medium than the parent AA. In addition, AA, D1, and D2 share the same docking profile, with wild-type human peroxiredoxin as a model system. Their docking scores are similar to those of dithiothreitol (DTT). This suggests a similar binding af-finity to the human peroxiredoxin binding site.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Farmacija, Biotehnologija u biomedicini (prirodno područje, biomedicina i zdravstvo, biotehničko područje)

POVEZANOST RADA

Ustanove:
Sveučilište u Rijeci,
Hrvatsko katoličko sveučilište, Zagreb,
Sveučilište u Rijeci - Odjel za biotehnologiju

Profili:

Karlo Wittine (autor)