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).

通过奥斯本法从鹰嘴豆 ( Cicer arietinum L. ) 种子中获得的蛋白质组分的胰蛋白酶水解产物与锌离子相互作用，并通过能量色散 X 射线 (EDX) 技术监测螯合结果。谷蛋白水解物（GluHyd）与锌离子反应，锌含量相对较高。为此，对谷蛋白水解物（GluHyd-Zn）的锌络合物进行了更深入的研究，在凝胶过滤后获得的含锌较多的第二级分中鉴定出了11种肽。肽 HKERVQLHIIPTAVGK 显示出相对较高的螯合能力 (57.86 ± 2.14%)。根据ICP-OS分析结果，1mg肽可螯合381.61±133.39μg锌，肽与锌的摩尔比约为1:4。光谱方法证明，该肽的侧链和C端羧基大部分参与螯合，氨基侧链的N原子、组氨酸的咪唑基和N端都被金属离子一定程度地占据。使用分子操作环境 (MOE) 软件完成锌-肽相互作用的建模。对接结果与实验数据具有相关性。

HKERVQLHIIPTAVGK-Zn复合物的ACE2抑制作用(IC ₅₀  = 1.5 mg/mL)优于HKERVQLHIIPTAVGK (IC ₅₀  = 2.2 mg/mL)。