Novel xanthine oxidase inhibitory peptides derived from whey protein: identification, in vitro inhibition mechanism and in vivo activity validation

化学 体内 黄嘌呤氧化酶 水解物 高尿酸血症 生物化学 圆二色性 对接(动物) IC50型 体外 药理学 尿酸 护理部 生物技术 水解 生物 医学
作者
Xiaofen Qi,Hao Chen,Kaifang Guan,Yue Sun,Rongchun Wang,Qiming Li,Ying Ma
出处
期刊:Bioorganic Chemistry [Elsevier BV]
卷期号:128: 106097-106097 被引量:35
标识
DOI:10.1016/j.bioorg.2022.106097
摘要

As the development of hyperuricemia (HUA) and gout continues to accelerate worldwide, there is increasing interest in the use of xanthine oxidase (XO) inhibitors as therapeutic agents for the management of HUA and gout. In the present study, XO inhibitory peptides were identified from whey protein isolate (WPI) hydrolysates, and the underlying inhibitory mechanism and in vivo activities was investigated. WPI hydrolysates were isolated and purified, and two peptides (ALPM and LWM) with lower binding energy were screened by molecular docking. The result showed that these two peptides interacted with residues around the active site of XO through hydrogen bond and hydrophobic interaction. The IC50 values of ALPM and LWM were 7.23 ± 0.22 and 5.01 ± 0.31 mM, respectively. According to the Lineweaver-Burk curve, the inhibition types of ALPM and LWM were non-competitive inhibition. Circular dichroism (CD) spectra indicated ALPM and LWM could change the secondary structure of XO. Molecular dynamics simulations revealed that XO-peptide complexes were more stable and compact than XO. Moreover, animal studies have shown that ALPM and LWM have anti-hyperuricemia effects in vivo. This study suggested that ALPM and LWM can be considered as natural XO inhibitors for the treatment of HUA.
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