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

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

  • Nat Prod Res. 2015;29(23):2219-22. doi: 10.1080/14786419.2014.1003065.
Dehong Tan 1 Yao Zhang 2 Lulu Chen 1 Ling Liu 1 Xuan Zhang 1 Zhaoxia Wu 1 Bing Bai 1 Shujuan Ji 1
Affiliations

Affiliations

  • 1 a College of Food Science, Shenyang Agricultural University , Shenyang , Liaoning Province 110866 , P.R. China.
  • 2 b College of Fine Art and Design, Shenyang Normal University , Shenyang Liaoning Province 110034 , P.R. China.
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.

Keywords

Maillard reaction; advanced glycation end products; chelating; organosulphur peptide; radical-scavenging.

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