Le Xu
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Le Xu has a total of 4 co-authors. Here are the top co-authors by number of shared publications:
- Chen Fan
Agricultural Science and Engineering School, Liaocheng University, Liaocheng 252059, China
1 shared publication - Lele Cao
School of Pharmaceutical Sciences and Food Engineering, State Key Laboratory of Macromolecular Drugs and Large-scale Preparation, Liaocheng University, 1th Hunan Road, Dongchangfu District, Liaocheng 252000, PR China
1 shared publication - Rong Liang
Shandong Key Laboratory of Applied Technology for Protein and Peptide Drugs, School of Pharmaceutical Sciences and Food Engineering, Liaocheng University, Liaocheng 252059, China
1 shared publication - Xingfeng Guo
Shandong Key Laboratory of Applied Technology for Protein and Peptide Drugs, School of Pharmaceutical Science and Food Engineering, Liaocheng University, Liaocheng 252000, China
1 shared publication
Latest Publications
- Open Access
Structural Characteristics and Antioxidant Mechanism of Donkey-Hide Gelatin Peptides by Molecular Dynamics Simulation
This study aimed to explore the structural characteristics and antioxidant mechanism of donkey-hide gelatin peptides. After hydrolysis and ultrafiltration treatment, five gelatin peptides with different molecular weights (MWs) were obtained. Amino acid analysis showed that gelatin peptides with different MWs contained a large number of amino acids, including G, P, E, N, A, and R, and differences were noted in the content of various amino acids. Fourier transform infrared spectroscopy and circular dichroism revealed that these gelatin peptides differed in terms of the peak strength of functional groups and number of secondary structures. Moreover, 26 pentapeptides/hexapeptides were identified. Among them, we investigated by molecular docking how PGPAP, which has the best antioxidant activity, may interact with the Keap1 protein. The results showed that the PGPAP-Keap1 complex had a stable conformation, and Arg415, Gly462, Phe478, and Tyr572 were the key residues involved in the binding of the peptide PGPAP to Keap1. Our results demonstrated that PGPAP could serve as a bioactive peptide with antioxidant activity.
Open AccessStructural Characteristics and Antioxidant Mechanism of Donkey-Hide Gelatin Peptides by Molecular Dynamics Simulation
This study aimed to explore the structural characteristics and antioxidant mechanism of donkey-hide gelatin peptides. After hydrolysis and ultrafiltration treatment, five gelatin peptides with different molecular weights (MWs) were obtained. Amino acid analysis showed that gelatin peptides with different MWs contained a large number of amino acids, including G, P, E, N, A, and R, and differences were noted in the content of various amino acids. Fourier transform infrared spectroscopy and circular dichroism revealed that these gelatin peptides differed in terms of the peak strength of functional groups and number of secondary structures. Moreover, 26 pentapeptides/hexapeptides were identified. Among them, we investigated by molecular docking how PGPAP, which has the best antioxidant activity, may interact with the Keap1 protein. The results showed that the PGPAP-Keap1 complex had a stable conformation, and Arg415, Gly462, Phe478, and Tyr572 were the key residues involved in the binding of the peptide PGPAP to Keap1. Our results demonstrated that PGPAP could serve as a bioactive peptide with antioxidant activity.