Phenolic compounds profile in extracts of Smilax spp., antioxidant activity, and inhibition of advanced glycation end products.

Smilax genus possesses bioactive properties attributed to phenolic compounds, which may exhibit antioxidant effects and inhibit the advanced glycation end products (AGEs). However, identifying these phenolic compounds and AGEs has become increasingly relevant to understanding such activities. This study aimed to identify phenolic compounds in extracts of Smilax spp. and evaluate their antioxidant and AGEs inhibitory activities. To achieve this, the Smilax genus was identified via PCR, and phenolic compounds including chlorogenic acid, naringenin-6-C-glucoside, quercetin, quercetin-3-O-glucoside, and myricetin were identified using HPLC-MS/MS. Antioxidant activity was assessed by ferric reducing antioxidant power (FRAP), and radicals such as 2,2-diphenyl-1-picrylhydrazyl (DPPH), and 2,2'-azino-bis-[3-ethyl-benzothiazoline]-6-sulfonic acid (ABTS), while AGEs inhibition was evaluated using a model system formed by bovine serum albumin-glucose. The highest antioxidant activity was 3612.18 mM TE/g, and the inhibition of AGEs was 52.44 %. These results demonstrate that Smilax spp. can inhibit AGEs, neutralize free radicals, and reduce compounds associated with antioxidant capacity.

Phenolic profile, cheminformatics, and antiplatelet aggregation activity of orange and purple sweet potato (Ipomoea batatas L.) storage roots.

Sweet potatoes are rich in cardioprotective phytochemicals with potential anti-platelet aggregation activity, although this benefit may vary among cultivars/genotypes. The phenolic profile [HPLC-ESI(-)-qTOF-MS2], cheminformatics (ADMET properties, affinity toward platelet proteins) and anti-PA activity of phenolic-rich hydroalcoholic extracts obtained from orange (OSP) and purple (PSP) sweet potato storage roots, was evaluated. The phenolic richness [Hydroxycinnamic acids> flavonoids> benzoic acids] was PSP > OSP. Their main chlorogenic acids could interact with platelet proteins (integrins/adhesins, kinases/metalloenzymes) but their bioavailability could be poor. Just OSP exhibited a dose-dependent anti-platelet aggregation activity [inductor (IC50, mg.ml-1): thrombin receptor activator peptide-6 (0.55) > Adenosine-5'-diphosphate (1.02) > collagen (1.56)] and reduced P-selectin expression (0.75-1.0 mg.ml-1) but not glycoprotein IIb/IIIa secretion. The explored anti-PA activity of OSP/PSP seems to be inversely related to their phenolic richness. The poor first-pass bioavailability of its chlorogenic acids (documented in silico) may represent a further obstacle for their anti-PA in vivo.