氨基酸组成分析显示  ，当多肽中含有酸性或碱性氨基酸残基时  ，其与铁离子表现出良好的结合性 。Glu 和Asp含有活性侧链基团  ，有助于形成肽-金属复合物 。 例如  ，Lys、 Asp和Glu中含有羧基、氨基、胍基等  ，这些侧链基团通过静电作用或配位作用  ，与金属离子结合  ，从而使多肽具有一定的铁亚铁离子联系特性 。Glu 和 Asp因包括环状形式  ，都可以与亚铁等轻合金阴离子通过  ，进行安稳的轻合金螯合物 。有探究看到  ，包括很不错亚铁螯合意识的多肽基本还与Cys、Arg、Ser等酪氨酸拥有密实的去联系  ，可能会是小肽和亚铁铝亚铁离子使用配位键、铝亚铁离子键的充分意义而变成新的有机化合物  ，螯合化学反应的首要通过位点是氨基、羧基和肽键  ，谷氨酸（Glu 和 Asp）、天冬氨酸（Asp）和半胱氨酸（Cys）操作了螯合想法  。

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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、柠檬汁酸苹果6手机酸镁Magnesium Citrate Malate、柚子酸锶Strontium Citrate、檸檬酸锰Manganese Citrate、柠檬汁酸铜Copper Citrate、天门冬氨酸锂Lithium Aspartate、抗坏血酸锰Manganese Ascorbate、牛磺酸硒Selenium Taurate 。

Different amino acid structures affect ferrous chelation ability

Amino acid composition analysis showed that when the polypeptide contained acidic or basic amino acid residues, it showed good binding with iron ions. Glu and Asp contain active side chain groups that contribute to the formation of peptide-metal complexes. For example, Lys, Asp and Glu contain carboxyl, amino, guanidine, etc. These side chain groups bind to metal ions through electrostatic interaction or coordination, so that the polypeptide has a certain iron ion binding ability. Because of their ring structure, Glu and Asp can combine with ferrous ions to form stable metal chelates. Some studies have found that peptides with good ferrous chelating ability are usually closely related to amino acids such as Cys, Arg and Ser, which may be due to the interaction of small peptides and ferrous ions through coordination bonds and ionic bonds to form new substances. The main binding sites of chelating reactions are amino, carboxyl and peptide bonds. Glutamic acid (Glu and Asp), aspartate (Asp) and cysteine (Cys) were involved in the chelation reaction.

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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.