Decreased glycation and structural protection properties of γ-glutamyl-S-allyl-cysteine peptide isolated from fresh garlic scales (Allium sativum L.)

Abstract

The antiglycative effect of γ-glutamyl-S-allyl-cysteine (GSAC) peptide isolated from fresh garlic scales was investigated in the bovine serum albumin (BSA)/glucose system. GSAC inhibited the increase of fluorescence intensity at about 440 nm in a concentration-dependent manner and reduced reacted free lysine side chains by 10.9%, 24.7% and 37.7%, as the GSAC concentrations increased from 0.1 to 2.5 mg mL− 1. Glycation-specific decline in BSA α-helix content (from 61.3% to 55.6%) and increase in β-sheet (from 2.1% to 5.4%) were prevented by GSAC (2.5 mg mL− 1) in vitro, implying its stabilisation effect. GSAC treatment (2.5 mg mL− 1) suppressed protein crosslinking to form polymers. Additionally, GSAC (10, 40, and 160 μg mL− 1) showed radical-scavenging and metal-chelating capacities. In conclusion, GSAC has an antiglycative effect, which may involve its radical-scavenging and metal-chelating capacities.