Coordination of divalent transition-metal ions to the α-amino acid 2-amino-2-deoxy-D-glycero-D-gulo-heptonic acid in aqueous solution

Díez, M.A. Díaz; Barros, F.J.G.; Rey, Eduardo Sabio; Calahorro, C. Valenzuela

doi:10.1016/0162-0134(92)80022-n

Cited by 8 publications

(2 citation statements)

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“…Once dehydrated, the complex decomposes in the 238-800°C temperature range. This behavior is similar to that found in other amino acid complexes [34,35]. There is a very large mass loss, which takes place between 238°C and 527°C.…”

Section: Thermogravimetric Analysissupporting

confidence: 87%

Characterization of the Complex of Human-like Collagen with Calcium

Fan

2011

Biol Trace Elem Res

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The calcium complex of human-like collagen (HLC) was generated in aqueous solution, purified by dialysis or ultrafiltration, and isolated by freeze-drying. Evidence for interactions between HLC and calcium(II) was obtained through measurements of the complex's fluorescence and UV-visible spectra, the interpretation of its Fourier transform infrared spectroscopy and circular dichroism spectra, thermogravimetric (TG) analysis, and differential scanning calorimetry (DSC). The HLC-Ca complex is considered a new chemical compound in which HLC retains its helical structure and the calcium ion is linked to the protein via C=O and N-H groups. Additionally, TG and DSC measurements indicate that the HLC-Ca complex is thermodynamically more stable than free HLC. The results obtained provide important evidence for the further study of the interactions of HLC with Ca(II).

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Section: Thermogravimetric Analysissupporting

confidence: 87%

Characterization of the Complex of Human-like Collagen with Calcium

Fan

2011

Biol Trace Elem Res

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“…Once dehydrated, the complex decomposes in the 280-800°C temperature range. This behavior is similar to that found in other amino acid complexes [18,19]. There is a very large mass loss, which takes place between 280°C and 330°C.…”

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confidence: 87%

Interaction of Human-Like Collagen with Copper (II): Effect on Thermal Characteristics

2013

AMR

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This work describes the aqueous-solution technique preparation and characterization of the complex between human-like collagen and copper (II). Pure human-like collagen and the copper complex were characterized by thermo gravimetric (TG) and differential scanning calorimetry (DSC) analysis. The TG curves and DSC data reveal the significant thermal differences between pure protein and the copper complex, demonstrating the formation of a new chemical compound, which is different from the free HLC and with more stable thermodynamic properties.

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Complexes of copper(II) with sugar ?-amino acids as ligands

Dı́az-Dı́ez

García-Barros

Híges-Rolando

et al. 1995

Transition Met Chem

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Complexes of Cu II with 2-(benzylamino)-2-deoxy-Dglycero-D-talo heptonic acid (BnMa) and 2-(benzylamino)-2-deoxy-D-glycero-L-gluco heptonic acid (BnGa) were prepared and characterized by elemental analysis, thermal data, i.r., electronic and e.s.r, spectra, magnetic susceptibility measurements, and X-ray powder diffraction. The metal:ligand stoichiometry of these complexes is 1:2 and coordination around Cu n seems to be octahedral, with the ligands bound through the N atom of the amino group and O atoms of the bridging carboxylate group.

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Coordination of divalent transition-metal ions to the α-amino acid 2-amino-2-deoxy-D-glycero-D-gulo-heptonic acid in aqueous solution

Cited by 8 publications

References 10 publications

Characterization of the Complex of Human-like Collagen with Calcium

Characterization of the Complex of Human-like Collagen with Calcium

Interaction of Human-Like Collagen with Copper (II): Effect on Thermal Characteristics

Complexes of copper(II) with sugar ?-amino acids as ligands

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