Crosslinked hydrogels based on biological macromolecules with potential use in skin tissue engineering

International Journal of Biological Macromolecules

Volumn 84, Issue , 2016, Pages 174-181

  Vulpe, Raluca ^a,c   Popa, Marcel ^a,f   Picton, Luc ^b,c,d   Balan, Vera ^e   Dulong, Virginie ^b,c,d   Butnaru, Maria ^e   Verestiuc, Liliana ^e  

^a GHEORGHE ASACHI TECHNICAL UNIVERSITY OF IASI   (Romania)

^b NORMANDIE UNIVERSITÉ   (France)

^c UNIVERSITÉ DE ROUEN   (France)

^d Normandie Université   (France)

^e GRIGORE T POPA UNIVERSITY OF MEDICINE AND PHARMACY   (Romania)

^f ACADEMY OF ROMANIAN SCIENTISTS   (Romania)

Author keywords

Biocompatibility; Collagen; Hyaluronic acid; Hydrogels; Sericin

Indexed keywords

COLLAGEN; HYALURONIC ACID; SERICIN; BIOMATERIAL; CROSS LINKING REAGENT; HYDROGEL;

ARTICLE; CELL PROLIFERATION; CELL SWELLING; CELL VIABILITY; CHEMICAL STRUCTURE; CONTROLLED STUDY; CROSS LINKING; ENZYME DEGRADATION; HUMAN; HUMAN CELL; HYDROGEL; IN VITRO STUDY; INFRARED SPECTROSCOPY; MICROCALORIMETRY; PHYSICAL CHEMISTRY; SKIN FIBROBLAST; TISSUE ENGINEERING; ADSORPTION; CHEMISTRY; SKIN; TISSUE REGENERATION; TISSUE SCAFFOLD;

ADSORPTION; BIOCOMPATIBLE MATERIALS; COLLAGEN; CROSS-LINKING REAGENTS; GUIDED TISSUE REGENERATION; HYALURONIC ACID; HYDROGELS; SERICINS; SKIN; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TISSUE ENGINEERING; TISSUE SCAFFOLDS;

EID: 84950276847     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2015.12.019     Document Type: Article

References (38)

1. Hu X., Cebe P., Weiss A.S., Omenetto F., Kaplan D.L. Protein-based composite materials. Mater. Today 2012, 15:208-215.
2. Gagner J.E., Kim W., Chaikof E.L. Designing protein-based biomaterials for medical applications. Acta Biomater. 2014, 10:1542-1557.
3. s). Int. J. Mol. Sci. 2013, 14:1870-1889.
4. Dash R., Ghosh S.K., Kaplan D.L., Kundu S.C. Purification and biochemical characterization of a 70kDa sericin from tropical tasar silkworm, Antheraea mylitta. Comp. Biochem. Phys. B 2007, 147:129-134.
5. Padamwar M.N., Pawar A.P. Silk sericin and its applications: a review. J. Sci. Ind. Res. India 2004, 63:323-329.
6. Aramwit P., Siritientong T., Kanokpanont S., Srichana T. Formulation and characterization of silk sericin-PVA scaffold crosslinked with genipin. Int. J. Biol. Macromol. 2010, 47:668-675.
7. Yun H., Oh H., Kim M.K., Kwak H.W., Lee J.Y., Um I.C., et al. Extraction conditions of Antheraea mylitta sericin with high yields and minimum molecular weight degradation. Int. J. Biol. Macromol. 2013, 52:59-65.
8. Aramwit P., Siritientong T., Srichana T. Potential applications of silk sericin, a natural protein from textile industry by-products. Waste Manag. Res. 2012, 30:217-224.
9. Kundu S.C., Dash B.C., Dash R., Kaplan D.L. Natural protective glue protein, sericin bioengineered by silkworms: potential for biomedical and biotechnological applications. Prog. Polym. Sci. 2015, 33:998-1012.
10. Lallepak L., Mario G., Guang Y., Qun W. Silk sericin: a versatile material for tissue engineering and drug delivery. Biotechnol. Adv. 2015, 33:1855-1867.
11. Allison D.D., Grande-Allen K.J. Review. Hyaluronan: a powerful tissue engineering tool. Tissue Eng. 2006, 12:2131-2140.
12. Lungu A., Albu M.G., Stancu I.C., Florea N.M., Vasile E., Iovu H. Superporous collagen-sericin scaffolds. J. Appl. Polym. Sci. 2013, 2269-2279.
13. Mandal B., Priya A.S., Kundu S.C. Novel silk sericin/gelatin 3-D scaffolds and 2-D films: fabrication and characterization for potential tissue engineering applications. Acta Biomater. 2009, 5:3007-3020.
14. Akturk O., Tezcaner A., Bilgili H., Deveci M.S., Gecit M.R., Keskin D. Evaluation of sericin/collagen membranes as prospective wound dressing biomaterial. J. Biosci. Bioeng. 2011, 112:279-288.
15. Nayak S., Dey S., Kundu S.C. Skin equivalent tissue-engineered construct: co-cultured cocoons. PLoS One 2013, 8:1-17.
16. Zhang Q., Dong P., Chen L., Wang X., Lu S. Genipin-cross-linked thermosensitive silk sericin/poly(N-isopropulacrylamide) hydrogels for cell proliferation and rapid detachment. J. Biomed. Mater. Res. A 2014, 102A:76-83.
17. Dinescu S., Galateanu B., Albu M., Lungu A., Radu E., Hermenean A., Costache M. Biocompatibility assessment of novel collagen-sericin scaffolds improved with hyaluronic acid and chondroitin sulfate for cartilage regeneration. Biomed. Res. Int. 2013, 1-11.
18. Olde Damink L.H.H., Dijkstra O.J., van Luyn M.J.A., van Wachem P.B., Niewenhuis P., Feijen J. Cross-linking of dermal sheep collagen using a water soluble carbodiimide. Biomaterials 1996, 17:765-773.
19. Park S.N., Park J.C., Kim H.O., Song M.J., Suh H. Characterization of porous collagen/hyaluronic acid scaffold modified by 1-ethyl-3(3-dimethylaminopropyl) carbodiimides cross-linking. Biomaterials 2002, 23:1205-1212.
20. Park S.N., Lee H.J., Lee K.H., Suh H. Biological characterization of EDC-crosslinked collagen-hyaluronic acid matrix in dermal tissue restoration. Biomaterials 2003, 24:1631-1641.
21. Davidenko N., Campbell J.J., Thian E.S., Watson C.J., Cameron R.E. Collagen-hyaluronic acid scaffolds for adipose tissue engineering. Acta Biomater. 2010, 6:3957-3968.
22. Aramwit P., Palapinyo S., Srichana T., Chottanapund C., Muangman P. Silk sericin ameliorates wound healing and its clinical efficacy in burn wounds. Arch. Dermatol. Res. 2013, 305:585-594.
23. Powell H.M., Boyce S.T. EDC cross-linking improves skin substitute strength and stability. Biomaterials 2006, 27:5821-5827.
24. Velmurugan P., Jonnalagadda R.R., Nair B.U. Biochemical and biophysical characterization of EDC treated rattus type I collagen. Process. Biochem. 2013, 48:1059-1064.
25. Hermanson G.T. Zero-length crosslinkers. Bioconjugate Techniques 2013, Thermo Fisher Scientific: Rockford, IL, USA, pp. 229-258. 3rd edition.
26. Huang S., Fu X. Naturally derived materials-based cell and drug delivery systems in skin regeneration. J. Control. Release 2010, 142:149-159.
27. Kamolz L.P., Wild T. Wound bed preparation: the impact of debridement and wound cleansing. Wound Med. 2013, 1:44-50.
28. Aruffo A., Stamenkovic I., Melnick M., Underhill C.B., Seed B. CD44 is the principal cell surface receptor for hyaluronate. Cell 1990, 61:1303-1313.
29. Vasi A.M., Popa M.I., Butnaru M., Dodi G., Verestiuc L. Chemical functionalization of hyaluronic acid for drug delivery applications. Mater. Sci. Eng. C 2014, 38:177-185.
30. Zhao H., Brown P.H., Schuck P. On the distribution of protein refractive index increments. Biophys. J. 2011, 100:2309-2317.
31. Ali G., Rihouey C., Le Cherf D., Picton L. Effect of carboxymethyl groups on degradation of modified pullulan by pullulanase from Klebsiella pneumonia. Carbohydr. Polym. 2013, 93:109-115.
32. Nam K., Kimura T., Kishida A. Controlling coupling reaction of EDC and NHS for preparation of collagen gels using ethanol/water co-solvents. Macromol. Biosci. 2008, 8:32-37.
33. Pieper J.S., Oosterhof A., Dijkstra P.J., Veerkamp J.H., van Kuppevelt T.H. Peparation and characterization of porous crosslinked collagenous matrices containing bioavailable chondroitin sulphate. Biomaterials 1999, 20:847-859.
34. Yin J., Tomycz L., Bonner G., Wang D.I.C. A simple and rapid assay of collagen-like polymer in crude lysate from Escherichia coli. J. Microbiol. Methods 2002, 49:321-323.
35. Li J., Ren N., Qiu J., Jiang H., Zhao H., Wang G., Boughton R.I., Wang Y., Liu H. Carbodiimide crosslinked collagen from porcine dermal matrix for high-strength tissue engineering scaffolds. Int. J. Biol. Macromol. 2013, 61:69-74.
36. Leone G., Consumi M., Lamponi S., Magnani A. New hyaluronan derivate with prolonged half-life for ophtalmological formulation. Carbohydr. Polym. 2012, 88:799-808.
37. Gelinsky M., Welzel P.B., Simon P., Bernhardt A., Konig U. Porous three-dimensional scaffolds of mineralized collagen: preparation and properties of a biomimetic nanocomposite material for tissue engineering of bone. Chem. Eng. J. 2008, 137:84-96.
38. Potorac S., Popa M., Picton L., Dulong V., Verestiuc L., Le Cerf D. Collagen functionalized with unsaturated cyclic anhydrides-interactions in solution and solid state. Biopolymers 2013, 101:228-236.