多肽與亞鐵螯合的機理

多肽與金屬離子發生螯合的先決條件是多肽能夠為金屬離子提供電子對，肽的末端羧基或氨基中含有比較多的氮原子、氧原子和硫原子，鐵離子可與多肽在氨基、羧基等位點發生配位，以共價鍵形式結合。在肽鐵螯合機理的表征中，肽鐵結合的本質是亞鐵離子與多肽中特定的化學基團發生反應。通過傅里葉變換紅外光譜、質譜、核磁共振光譜等，比較金屬離子結合前后紅外吸收峰和波長的變化來識別肽的結合基團。多肽側鏈中的氮原子、氧原子、硫原子，可以提供孤對電子與亞鐵離子結合，氮原子是亞鐵離子的主要結合位點。通過紅外光譜研究黃皮種子抗氧化肽鐵螯合物的結合位點，發現主要通過羧基氧、氨基氮原子與亞鐵離子結合。雖然已經有很多關于肽鐵螯合位點的相關研究，但對肽鐵螯合的結構關系和動力學過程還需要更深入的探索。

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抗壞血酸亞鐵Ferrous Ascorbate、賴氨酸甘氨酸鎂Magnesium Lysinate Glycinate、甘氨酸谷氨酰胺鎂Magnesium Glycinate Glutamine、檸檬酸蘋果酸鎂Magnesium Citrate Malate、檸檬酸鍶Strontium Citrate、檸檬酸錳Manganese Citrate、檸檬酸銅Copper Citrate、天門冬氨酸鋰Lithium Aspartate、抗壞血酸錳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.