Document Detail

Formation and characterization of iron-binding phosphorylated human-like collagen as a potential iron supplement.
MedLine Citation:
PMID:  23910354     Owner:  NLM     Status:  In-Data-Review    
Iron incorporated into food can induce precipitation and unwanted interaction with other components in food. Iron-binding proteins represent a possibility to avoid these problems and other side effects, as the iron is protected. However, there are several technical problems associated with protein-iron complex formation. In this paper, the iron-binding phosphorylated human-like collagen (Fe-G6P-HLC) was prepared under physiological conditions through phosphorylated modification. One molecule of Fe-G6P-HLC possesses about 24 atoms of Fe. Spectroscopy analysis, differential scanning calorimetry (DSC) and equilibrium dialysis techniques were employed to investigate the characteristics of the Fe-G6P-HLC. The binding sites (nb) and apparent association constant (Kapp) between iron and phosphorylated HLC were measured at nb=23.7 and log Kapp=4.57, respectively. The amount of iron (Fe(2+) sulfate) binding to phosphorylated HLC was found to be a function of pH and phosphate content. In addition, the solubility and thermal stability of HLC were not significantly affected. The results should facilitate the utilization of HLC as a bioactive iron supplement in the food and medical industry and provide an important theoretical evidence for the application of HLC chelates.
Jianjun Deng; Fei Chen; Daidi Fan; Chenhui Zhu; Xiaoxuan Ma; Wenjiao Xue
Related Documents :
21454594 - Structural basis of recognition of pathogen-associated molecular patterns and inhibitio...
24688634 - The use of hammett constants to understand the non-covalent binding of aromatics.
8858994 - Recovery of dopamine transporter binding and function after intrastriatal administratio...
23796134 - Single-molecule atomic force microscopy unravels the binding mechanism of a burkholderi...
19528664 - Structural insights into what glycan arrays tell us about how glycan-binding proteins i...
3019634 - Effects of n-ethylmaleimide on gonadotropin and beta-adrenergic receptor function coupl...
Publication Detail:
Type:  Journal Article     Date:  2013-06-28
Journal Detail:
Title:  Materials science & engineering. C, Materials for biological applications     Volume:  33     ISSN:  1873-0191     ISO Abbreviation:  Mater Sci Eng C Mater Biol Appl     Publication Date:  2013 Oct 
Date Detail:
Created Date:  2013-08-05     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101484109     Medline TA:  Mater Sci Eng C Mater Biol Appl     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  4361-8     Citation Subset:  IM    
Copyright Information:
© 2013.
Shaanxi Key Laboratory of Degradable Biomedical Materials, College of Chemical Engineering, Northwest University, Xi'an 710069, China; Shaanxi R&D Center of Biomaterials and Fermentation Engineering, College of Chemical Engineering, Xi'an 710069, China.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Tailored degradation of biocompatible poly(3-hydroxybutyrate-co-3-hydroxyvalerate)/calcium silicate/...
Next Document:  Biomimetic composite scaffolds based mineralization of hydroxyapatite on electrospun calcium-contain...