FOOD SCIENCE ›› 2018, Vol. 39 ›› Issue (10): 185-192.doi: 10.7506/spkx1002-6630-201810029

• Bioengineering • Previous Articles     Next Articles

Inhibitory Effects of Peptides Derived from Tryptic Hydrolysate of Skin Collagen from Melanogrammus aeglefinus on UVB-Induced Photodamage in HaCaT Cells

DONG Lisha1, LI Yanyan2, ZHANG Hongyan1, CUI Chenxi1, HAN Jiaojiao1, WANG Zhaoyang1, SI Kaixue1, ZHOU Jun1, LU Chenyang1, SU Xiurong1,*   

  1. (1. School of Marine Sciences, Ningbo University, Ningbo 315211, China; 2. College of Agriculture and Life Sciences, Cornell University, Ithaca 14853, USA)
  • Online:2018-05-25 Published:2018-05-15

Abstract: Objective: This study aimed to examine the antioxidant activity of peptides produced by tryptic hydrolysis of skin collagen from Melanogrammus aeglefinus and its inhibitory effect against photodamage in an effort to improve the reuse potential of M. aeglefinus skin. Methods: One-factor-at-a-time method and response surface methodology were used in conjunction to determine the optimum hydrolysis process for skin collagen from M. aeglefinus. The obtained peptides were sequenced by matrix-assisted laser desorption/ionization time of flight tandem mass spectrometry (MALDI-TOF MS/MS). The dominant peptides were docked with Kelch-like ECH-associated protein 1 (Keap1) by using the CDOCKER module in Discovery Studio. At the same time, HaCaT cells were pretreated with different concentrations of the collagen hydrolysate and then induced by ultraviolet B (UVB) to establish a cellular model of photodamage. The activities of superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), malondialdehyde (MDA) and the cell apoptosis and cycle were examined to test the ability of the peptides to inhibit photodamage. Results: Optimal hydrolysis conditions were determined as follows: hydrolysis time 1.75 h, enzyme concentration 1.23%, and temperature 52.95 ℃. The corresponding degree of hydrolysis was 78.33%. The dominant peptide sequences in the hydrolysate were identified as V-IFFVTMGTP-R, L-SIVPV-R and L-MHT-T. Molecular docking showed that the binding of V-IFFVTMGTPR to Keap1 was the most stable, thereby predicting that the peptide has antioxidant effect. The SOD and GSH-Px activities of HaCaT cells treated with the hydrolysate at 250 mg/mL were significantly higher than those of the model group (P < 0.01), accompanied by a significant decrease in MDA content (P < 0.01). Conclusion: The tryptic hydrolysis of collagen from M. aeglefinus skin has antioxidant activity, and an inhibitory effect on photodamage.

Key words: collagen from Melanogrammus aeglefinus skin, trypsin, polypeptide, molecular docking, photodamage in HaCaT cells

CLC Number: