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Characterization of the Complex of Human-like Collagen with Calcium

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Abstract

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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References

  1. Kessenich CR (2007) Supplementation for postmenopausal bone health. J Nurs Pract 3:155–168

    Article  Google Scholar 

  2. Finkelstein JS (2006) Calcium plus vitamin D for postmenopausal women-bone appetite? N Engl J Med 354:750–752

    Article  PubMed  CAS  Google Scholar 

  3. Ashmead (1992) The roles of amino acid chelates in animal nutrition. In: Ashmead HD. Noyes, Park Ridge, NJ, pp 479–481

    Google Scholar 

  4. Wang C, Lovell RT (1997) Organic selenium sources, selenomethionine and selenoyeast, have higher bioavailability than an inorganic selenium source, sodium selenite, in diets for channel catfish (Ictalurus punctatus). Aquaculture 152:223–234

    Article  CAS  Google Scholar 

  5. Apines MJ, Satoh S, Kiron V et al (2003) Availability of supplemental amino acid-chelated trace elements in diets containing tricalcium phosphate and phytate to rainbow trout, Oncorhynchus mykiss. Aquaculture 225:431–444

    Article  CAS  Google Scholar 

  6. Takeuchi Y, Nakayama K, Matsumoto T (1996) Differentiation and cell surface expression of transforming growth factor-beta receptors are regulated by interaction with matrix collagen in murine osteoblastic cells. J Biol Chem 271:3938–3944

    Article  PubMed  CAS  Google Scholar 

  7. Takeuchi Y, Suzawa M, Kikuchi T et al (1997) Differentiation transformation growth factor-beta receptor down-regulation by collagen-alpha 2 beta 1 integrin interaction is mediated by focal adhesion kinase and its downstream signals in murine osteoblastic cells. J Biol Chem 272:29309–29316

    Article  PubMed  CAS  Google Scholar 

  8. Wu J, Fujioka M, Sugimoto K et al (2004) Assessment of effectiveness of oral administration of collagen peptide on bone metabolism in growing and mature rats. J Bone Miner Metab 22:547–553

    Article  PubMed  CAS  Google Scholar 

  9. Koyama Y, Hirota A, Mori H et al (2001) Ingestion of gelatin has differential effect on bone mineral density and body weight in protein undernutrition. J Nutr Sci Vitaminol 47:84–86

    Article  PubMed  CAS  Google Scholar 

  10. Adam M, Spacek P, Hulejová H et al (1996) Postmenopausal osteoporosis. Treatment with calcitonin and a diet rich in collagen proteins. Cas Lek Cesk 135:74–78

    PubMed  CAS  Google Scholar 

  11. Bonjour JP (2005) Dietary protein: an essential nutrient for bone health. J Am Coll Nutr 24:526S–536S

    PubMed  CAS  Google Scholar 

  12. Jongjareonrak A, Benjakul S, Visessanguan W et al (2005) Isolation and characterisation of acid and pepsin-solubilised collagens from the skin of Brownstripe red snapper (Lutjanus vitta). Food Chem 93:475–484

    Article  CAS  Google Scholar 

  13. Yang XJ, Liang CY, Cai YL et al (2009) Recombinant human-like collagen modulated the growth of nano-hydroxyapatite on NiTi alloy. Mater Sci Eng C 29:25–28

    Article  CAS  Google Scholar 

  14. Wang Y, Cui FZ, Zhai Y et al (2006) Investigations of the initial stage of recombinant human-like collagen mineralization. Mater Sci Eng C 26:635–638

    Article  Google Scholar 

  15. Zhu CH, Fan DD, Ma XX et al (2009) Effects of chitosan on properties of novel human-like collagen/chitosan hybrid vascular scaffold. J Bioact Compat Polym 24:560–576

    Article  CAS  Google Scholar 

  16. Zhai Y, Cui FZ (2006) Recombinant human-like collagen directed growth of hydroxyapatite nanocrystals. J Cryst Growth 291:202–206

    Article  CAS  Google Scholar 

  17. Steinhardt J, Krijn J, Leidy JG (1971) Differences between bovine and human serum albumins. Binding isotherms, optical rotatory dispersion, viscosity, hydrogen ion titration, and fluorescence effects. Biochemistry 10:4005–4015

    Article  PubMed  CAS  Google Scholar 

  18. Yan MY, Li BF, Zhao X et al (2008) Characterization of acid-soluble collagen from the skin of walleye pollock (Theragra chalcogramma). Food Chem 107:1581–1586

    Article  CAS  Google Scholar 

  19. Sabio-Rey E, García-Barros FJ, Bernalte-García A et al (1999) A thermal and IR study of metal complexes of 2-amino-2-deoxy -D-glycero-L-gluco heptonic acid. Thermochim Acta 342:85–88

    Article  CAS  Google Scholar 

  20. Bandekar J (1992) Amide modes and protein conformation. Biochim Biophys Acta 1120:123–143

    Article  PubMed  CAS  Google Scholar 

  21. Lavialle F, Adams RG, Levin IW (1982) Infrared spectroscopic study of the secondary structure of melittin in water, 2-chloroethanol, and phospholipid bilayer dispersions. Biochemistry 21:2305–2312

    Article  PubMed  CAS  Google Scholar 

  22. Farrell HM, Wickham ED, Unruh JJ et al (2001) Secondary structural studies of bovine caseins: temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization. Food Hydrocolloids 15:341–354

    Article  CAS  Google Scholar 

  23. Payne KJ, Veis A (1988) Fourier transform IR spectroscopy of collagen and gelatin solutions: deconvolution of the amide I band for conformational studies. Biopolymers 27:1749–1760

    Article  PubMed  CAS  Google Scholar 

  24. Jackson M, Choo L, Watson PH et al (1995) Beware of connective tissue proteins: assignment and implications of collagen absorptions in infrared spectra of human tissues. Biochim Biophys Acta 1270:1–6

    PubMed  Google Scholar 

  25. Plepis AMDG, Goissis G, Das-Gupta DK (1996) Dielectric and pyroelectric characterisation of anionic and native collagen. Polymer Eng Sci 36:2932–2938

    Article  Google Scholar 

  26. Doyle BB, Bendit EG, Blout ER (1975) Infrared spectroscopy of collagen and collagen-like polypeptides. Biopolymers 14:937–957

    Article  PubMed  CAS  Google Scholar 

  27. Muyonga JH, Cole CGB, Duodu KG (2004) Characterization of acid soluble collagen from skins of young and adult Nile perch (Lates niloticus). Food Chem 85:81–89

    Article  CAS  Google Scholar 

  28. Abe Y, Krimm S (1972) Normal vibrations of crystalline polyglycine I. Biopolymers 11:1817–1839

    Article  PubMed  CAS  Google Scholar 

  29. Li Y, Li YW, Du ZL et al (2008) Comparison of dynamic denaturation temperature of collagen with its static denaturation temperature and the configuration characteristics in collagen denaturation processes. Thermochim Acta 469:71–76

    Article  CAS  Google Scholar 

  30. Engel J (1987) Folding and unfolding of collagen triple helices. Adv Mater Res 4:145–161

    Google Scholar 

  31. Jenness DD, Sprecher C, Johnson WC Jr (1976) Circular dichroism of collagen, gelatin, and poly(proline) II in the vacuum ultraviolet. Biopolymers 15:513–521

    Article  PubMed  CAS  Google Scholar 

  32. Burger K (1973) In: Millar T, Allen DW (eds) Coordination chemistry: experimental methods. Akademiai Kiado, Budapest, pp 23–26

    Google Scholar 

  33. Mercê ALR, Fernandes E, Mangrich AS et al (2001) Fe(III)-galactomannan solid and aqueous complexes. Potentiometric, EPR spectroscopy and thermal data. J Braz Chem Soc 12:791–798

    Article  Google Scholar 

  34. Valenzuela-Calahorro C, Díaz-Díez MA, Sabio-Rey E et al (1992) Equilibria in aqueous solution between divalent cations and the α-amino acid 2-(benzy-lamino) -2-deoxy–glycero–gulo-heptonic acid. Polyhedron 11:563–566

    Article  CAS  Google Scholar 

  35. Díaz-Díez MA, Garcia-Barros FJ, Sabio-Rey E et al (1992) Coordination of divalent transition-metal ions to the α-amino acid 2-amino-2-deoxy-D-glycerol- D-gulo-heptonic acid in aqueous solution. J Inorg Biochem 48:129–134

    Article  Google Scholar 

Download references

Acknowledgments

This study was financially supported by the National High Technology Research and Development Program of China (2007AA03Z456), the National Natural Science Foundation of China (20776119, 21076169 and 31000019), the Xi'an Research and Development Program (NC08005 and YF07078), the Scientific Research Program of Shaanxi Provincial Department of Education, China (08JK452, 08JK453, JG08181, 2010JC21, 2010JS107, 2010JS108, 2010JK876 and 2010JS109), the Shaanxi Provincial Scientific Technology Research and Development Program (2007 K06-03, 2010JQ2012, SJ08B03), the Specialized Research Fund for the Doctoral Program of Higher Education of China (20096101120023 and 20096101110014), the NWU Graduate Innovation and Creativity Funds (09YSY26) and the Shaanxi Key Subject Program, China.

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Authors and Affiliations

  1. Shaanxi Key Laboratory of Degradable Biomedical Materials, School of Chemical Engineering, Northwest University, 710069, Xi’an, China

    Yuanyuan Yu & Daidi Fan

  2. Shaanxi R&D Center of Biomaterials and Fermentation Engineering, 710069, Xi’an, China

    Yuanyuan Yu & Daidi Fan

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  1. Yuanyuan Yu
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  2. Daidi Fan
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Correspondence to Daidi Fan.

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Yu, Y., Fan, D. Characterization of the Complex of Human-like Collagen with Calcium. Biol Trace Elem Res 145, 33–38 (2012). https://doi.org/10.1007/s12011-011-9167-x

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  • DOI: https://doi.org/10.1007/s12011-011-9167-x

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