多肽與亞鐵螯合的機(jī)理

多肽與金屬離子發(fā)生螯合的先決條件是多肽能夠?yàn)榻饘匐x子提供電子對(duì)，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(diǎn)發(fā)生配位，以共價(jià)鍵形式結(jié)合。在肽鐵螯合機(jī)理的表征中，肽鐵結(jié)合的本質(zhì)是亞鐵離子與多肽中特定的化學(xué)基團(tuán)發(fā)生反應(yīng)。通過(guò)傅里葉變換紅外光譜、質(zhì)譜、核磁共振光譜等，比較金屬離子結(jié)合前后紅外吸收峰和波長(zhǎng)的變化來(lái)識(shí)別肽的結(jié)合基團(tuán)。多肽側(cè)鏈中的氮原子、氧原子、硫原子，可以提供孤對(duì)電子與亞鐵離子結(jié)合，氮原子是亞鐵離子的主要結(jié)合位點(diǎn)。通過(guò)紅外光譜研究黃皮種子抗氧化肽鐵螯合物的結(jié)合位點(diǎn)，發(fā)現(xiàn)主要通過(guò)羧基氧、氨基氮原子與亞鐵離子結(jié)合。雖然已經(jīng)有很多關(guān)于肽鐵螯合位點(diǎn)的相關(guān)研究，但對(duì)肽鐵螯合的結(jié)構(gòu)關(guān)系和動(dòng)力學(xué)過(guò)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、?；撬嵛?/span>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.