Synthesis and Characterisation of Chickpea Peptides-Zinc Chelates Having ACE2 Inhibitory Activity

IF 1.9 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY The Protein Journal Pub Date : 2023-08-23 DOI:10.1007/s10930-023-10133-5
Nurkhodja Mukhamedov, Akmal Asrorov, Ansor Yashinov, Muzaffar Kayumov, Ahmidin Wali, Sharafitdin Mirzaakhmedov, Haji Akber Aisa, Abulimiti Yili
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Abstract

Tryptic hydrolysates of protein fractions obtained by the Osborne method from chickpea (Cicer arietinum L.) seeds interacted with zinc ions and the results of chelation were monitored by the Energy Dispersive X-Ray (EDX) technique. The glutelin hydrolysate (GluHyd) reacted with zinc ions and depicted a relatively higher zinc content. For this reason, the zinc complex of the glutelin hydrolysate (GluHyd-Zn) was studied deeper, and 11 peptides were identified in its more zinc-containing second fraction obtained after gel filtration. The peptide HKERVQLHIIPTAVGK showed a relatively higher chelating capacity (57.86 ± 2.14%). According to the result of the ICP-OS analysis, 1 mg peptide could chelate 381.61 ± 133.39 µg zinc, and the molar ratio of peptide-zinc was about 1:4. Spectral methods proved that side chain and C-termini carboxyl groups of the peptide mostly were involved in chelation and N atoms of amino side chains, imidazole group of histidine, and N-termini at some extents were occupied by the metal ions. Modeling of zinc-peptide interaction was done using Molecular Operating Environment (MOE) software. The results of the docking correlate with the experimental data.

ACE2 inhibitory effect of HKERVQLHIIPTAVGK-Zn complex (IC50 = 1.5 mg/mL) was better than that of HKERVQLHIIPTAVGK (IC50 = 2.2 mg/mL).

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具有ACE2抑制活性的鹰嘴豆肽锌螯合物的合成与表征
用能量色散x射线(EDX)技术对鹰嘴豆(Cicer arietinum L.)种子奥斯本法获得的胰蛋白酶水解产物与锌离子的相互作用及螯合结果进行了监测。谷蛋白水解物(GluHyd)与锌离子反应,锌含量相对较高。因此,我们对谷蛋白水解产物的锌络合物(GluHyd-Zn)进行了更深入的研究,并在凝胶过滤后获得的含锌量更高的第二部分中鉴定了11个肽段。肽HKERVQLHIIPTAVGK具有较高的螯合能力(57.86±2.14%)。ICP-OS分析结果显示,1 mg肽能螯合381.61±133.39µg锌,肽与锌的摩尔比约为1:4。光谱方法证明,肽的侧链和c端羧基主要参与螯合,氨基侧链的N原子、组氨酸的咪唑基团和N端部分被金属离子占据。利用分子操作环境(MOE)软件对锌-肽相互作用进行建模。对接结果与实验数据相吻合。HKERVQLHIIPTAVGK- zn复合物对ACE2的抑制作用(IC50 = 1.5 mg/mL)优于HKERVQLHIIPTAVGK复合物(IC50 = 2.2 mg/mL)。
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来源期刊
The Protein Journal
The Protein Journal 生物-生化与分子生物学
CiteScore
5.20
自引率
0.00%
发文量
57
审稿时长
12 months
期刊介绍: The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.
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