Investigation of manganese(II)-insulin complexes using electrospray ionization mass spectrometry

Manganese is a trace element in human nutrition. It is involved in many enzymes, proteins and biological activities. Mn(II) ion has the capable of binding to protein or peptides. Insulin is a blood glucose-lowering peptide hormone and it is secreted by the pancreatic β-cells. In this study, the bind...

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Veröffentlicht in:International journal of biological macromolecules 2018-12, Vol.120 (Pt A), p.557-565
Hauptverfasser: Gülfen, Mustafa, Özdemir, Abdil, Lin, Jung-Lee, Chen, Chung-Hsuan
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container_end_page 565
container_issue Pt A
container_start_page 557
container_title International journal of biological macromolecules
container_volume 120
creator Gülfen, Mustafa
Özdemir, Abdil
Lin, Jung-Lee
Chen, Chung-Hsuan
description Manganese is a trace element in human nutrition. It is involved in many enzymes, proteins and biological activities. Mn(II) ion has the capable of binding to protein or peptides. Insulin is a blood glucose-lowering peptide hormone and it is secreted by the pancreatic β-cells. In this study, the binding capability of Mn(II) ions to insulin was studied using ESI-MS, nano-ESI-MS and MS/MS methods. The binding of Mn(II) ions to insulin molecule was studied by examining the effect of pH, the molar ratio of Mn(II) ions to insulin, the flow rate with nano-ESI system and MS/MS spectrometry. The ESI-MS measurements showed that the Mn(II)-insulin complexation mostly produces ML and M2L type complexes. The highest binding ratio was found at pH 7. The complex formation equilibrium constants of Mn(II)-insulin were calculated as Kf1: 1.03 ± 0.12 × 104 and Kf2: 1.93 ± 0.17 × 103. The nano-ESI-MS and MS/MS measurements exhibited strong and specific binding of Mn(II) ions to insulin molecule. It was concluded from all the ESI-MS measurements that Mn(II) ion has a high affinity to insulin molecule to form stable complexes. [Display omitted]
doi_str_mv 10.1016/j.ijbiomac.2018.08.122
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It is involved in many enzymes, proteins and biological activities. Mn(II) ion has the capable of binding to protein or peptides. Insulin is a blood glucose-lowering peptide hormone and it is secreted by the pancreatic β-cells. In this study, the binding capability of Mn(II) ions to insulin was studied using ESI-MS, nano-ESI-MS and MS/MS methods. The binding of Mn(II) ions to insulin molecule was studied by examining the effect of pH, the molar ratio of Mn(II) ions to insulin, the flow rate with nano-ESI system and MS/MS spectrometry. The ESI-MS measurements showed that the Mn(II)-insulin complexation mostly produces ML and M2L type complexes. The highest binding ratio was found at pH 7. The complex formation equilibrium constants of Mn(II)-insulin were calculated as Kf1: 1.03 ± 0.12 × 104 and Kf2: 1.93 ± 0.17 × 103. The nano-ESI-MS and MS/MS measurements exhibited strong and specific binding of Mn(II) ions to insulin molecule. It was concluded from all the ESI-MS measurements that Mn(II) ion has a high affinity to insulin molecule to form stable complexes. 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source MEDLINE; ScienceDirect Journals (5 years ago - present)
subjects Animals
Cations, Divalent
Cattle
Coordination Complexes - chemistry
Equilibrium
Hydrogen-Ion Concentration
Insulin
Insulin - chemistry
Kinetics
Manganese - chemistry
Manganese-insulin complexes
Mass spectrometry
Protein Binding
Spectrometry, Mass, Electrospray Ionization
Tandem Mass Spectrometry
title Investigation of manganese(II)-insulin complexes using electrospray ionization mass spectrometry
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