多肽与五金阴阳化合物造成了螯合的先决必备条件是多肽并能为五金阴阳化合物提高电子为了满足电子时代发展的需求  ，对  ，肽的尾部羧基或氨基中包含有较多的氮氧电子层、氧氧电子层和硫氧电子层   ，铁阴阳化合物可与多肽在氨基、羧基等位点造成了配位  ，以共价键类型根据在一起 。在肽铁螯合不可逆性的分析方法中  ，肽铁根据在一起的普遍性是亚铁阴阳化合物与多肽中某些的催化基团造成了的反应 。根据傅里叶变幻红外光谱图分析、质谱、核磁共鸣光谱图分析等  ，较五金阴阳化合物根据在一起前后轮红外吸引峰和光波波长的影响来区分肽的根据在一起基团 。多肽侧链中的氮氧水分子团、氧氧水分子团、硫氧水分子团  ，都可以提拱孤对手机与亚铁化合物配合  ，氮氧水分子团是亚铁化合物的重点配合位点 。经由红外光谱分析研究黄皮种子地址抗防氧化肽铁螯合物的配合位点  ，知道重点经由羧基氧、氨基氮氧水分子团与亚铁化合物配合 。固然开始有大多关与肽铁螯合位点的各种相关研究  ，但对肽铁螯合的型式的关联和扭矩学的时候还是需要深入入的研究 。

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抗坏血酸亚铁Ferrous Ascorbate、赖氨酸甘氨酸镁Magnesium Lysinate Glycinate、甘氨酸谷氨酰胺镁Magnesium Glycinate Glutamine、柠檬汁酸水果酸镁Magnesium Citrate Malate、百香果酸锶Strontium Citrate、檸檬酸锰Manganese Citrate、百香果酸铜Copper Citrate、天门冬氨酸锂Lithium Aspartate、抗坏血酸锰Manganese Ascorbate、牛磺酸硒Selenium Taurate 。

Mechanism of chelation of polypeptides with ferrous

The prerequisite for chelating polypeptides with metal ions is that polypeptides can provide electron pairs for metal ions. The terminal carboxyl group or amino group of peptides contains more nitrogen atoms, oxygen atoms and sulfur atoms, and iron ions can coordinate with polypeptides at amino and carboxyl groups and other sites to combine in the form of covalent bonds. In the characterization of peptide iron chelation mechanism, the essence of peptide iron binding is that ferrous ions react with specific chemical groups in peptides. By Fourier transform infrared spectroscopy, mass spectrometry and nuclear magnetic resonance spectroscopy, the changes of infrared absorption peak and wavelength before and after metal ion binding were compared to identify the binding groups of peptides. Nitrogen atoms, oxygen atoms and sulfur atoms in the side chain of the polypeptide can provide lone pair electrons to bind to ferrous ions, and nitrogen atoms are the main binding sites of ferrous ions. The binding sites of iron chelate of antioxidant peptide in Xanthophylla seeds were studied by infrared spectroscopy. It was found that the binding sites of ferrous ions were mainly through carboxyl oxygen and amino nitrogen atoms. Although there have been many studies on the iron chelation sites of peptides, the structural relationship and kinetic process of peptide iron chelation still need to be further explored.

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Ferrous Ascorbate, Magnesium Lysinate Glycinate, Magnesium lysinate Glycinate Glutamine, Magnesium citrate malate Citrate Malate, Strontium Citrate, Manganese Citrate, Copper Citrate, Lithium Aspartate, Manganese ascorbate Ascorbate, Selenium Taurate.