4.7 Article

In silico modelling of apo-lactoferrin under simulated gastric conditions: Structural dynamics, binding with β-lactoglobulin and α-lactalbumin, and functional implications

期刊

LWT-FOOD SCIENCE AND TECHNOLOGY
卷 148, 期 -, 页码 -

出版社

ELSEVIER
DOI: 10.1016/j.lwt.2021.111726

关键词

Lactoferrin; Gastric digestion; Molecular dynamics simulations; Steered molecular dynamics simulations; Umbrella sampling

资金

  1. Government for providing Research Training Program (RTP) scholarship
  2. Australian Government.

向作者/读者索取更多资源

The study shows that acidic pH weakens interactions between lactoferrin and other proteins, but some contacts are maintained. This property could be used for developing novel food materials and indicates the potential antibacterial capability of apo-lactoferrin.
This study employs computational techniques to investigate whether the inclusion of beta-lactoglobulin and alpha-lactalbumin can enhance the molecular stability of apo-lactoferrin in conditions of gastric pH. Atomistic molecular dynamics simulations reveal that acidic pH results in weakened interactions between lactoferrin and the other proteins compared to those under neutral pH. Nevertheless, protein-protein dissociation free energy calculations using the umbrella sampling calculations confirm that some contacts are maintained between apolactoferrin and the other whey proteins, specifically the beta-lactoglobulin units. This is manifested as a broad energy minimum at the intermediate inter-molecular distance of the inter-protein free energy profiles; thereby, demonstrating the formation of a nano-scale flocculant, followed by a potential gel, composed of protein particles. Practically, this property could be exploited to entrap further bioactive components within the protein matrix for novel engineered food materials. Furthermore, it was found that the anti-bacterial peptide regions of apo-lactoferrin are unaffected by the acidic pH, indicating the potential capability of apo-lactoferrin to act against harmful bacteria. Overall, this work unveils an understanding at a molecular level regarding the structural changes of the aforementioned proteins that maybe beneficial for future advancement of nutraceuticals.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据