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Isolation, identification, and virtual screening of peptides with ferrous ion chelating activity from poultry blood hemoglobin

文献类型: 外文期刊

作者: Hanyu, Guo 1 ; Ying, Zhou 2 ; Daoying, Wang 2 ; Weimin, Xu 2 ; Yingying, Li 1 ; Ji, Luo 1 ; Jing, Yang 2 ;

作者机构: 1.Anhui Normal Univ, Sch Life Sci, Wuhu 241001, Anhui, Peoples R China

2.Jiangsu Acad Agr Sci, Inst Agroprod Proc, Nanjing 210014, Jiangsu, Peoples R China

关键词: Poultry blood hemoglobin; Ferrous ion chelating peptide; Virtual screening; Molecular docking

期刊名称:LWT-FOOD SCIENCE AND TECHNOLOGY ( 影响因子:6.6; 五年影响因子:6.9 )

ISSN: 0023-6438

年卷期: 2025 年 231 卷

页码:

收录情况: SCI

摘要: To improve the utilization and value of poultry blood, identification, virtual screening, and binding mode of Fe2+ chelating peptide from poultry blood hemoglobin were investigated in this study. Virtual enzymatic hydrolysis results indicated that the peptide obtained from the hydrolysis of duck blood hemoglobin by thermolysin exhibited the highest Fe2+ chelating activity. The crude peptides were separated, and the fraction with the best Fe2+ chelating ability was identified. Subsequently, virtual screening and molecular docking were performed on the identified peptides. Finally, 6 peptides with potential biological activity as well as good intestinal absorption, without toxicity, allergenicity, and bitterness were screened through virtual screening. Among them, 4 peptides can stably bind to Fe2+. They showed two binding modes: peptides that presented a loop structure upon binding to Fe2+ have a binding site at the C-terminus; peptides that showed a beta-folded structure upon binding to Fe2+, with the binding site in the middle of the peptide chain. The carboxyl O atom was the main binding site. The poultry blood hemoglobin peptides with Fe2+ chelating ability were isolated and identified, and the chelating modes were analyzed to offer a theoretical foundation and technical strategy for the development of new iron nutrition fortifiers.

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