10.1186/2194-0517-2-11

Engineering of chitosan and collagen macromolecules using sebacic acid for clinical applications

  1. Microbiology Division, Central Leather Research Institute (CSIR, New Delhi), Chennai, Tamil Nadu, 20, IN
Cover Image

Published in Issue 2013-04-23

How to Cite

Sailakshmi, G., Mitra, T., & Gnanamani, A. (2013). Engineering of chitosan and collagen macromolecules using sebacic acid for clinical applications. Progress in Biomaterials, 2(1 (December 2013). https://doi.org/10.1186/2194-0517-2-11

Abstract

Abstract Transformation of natural polymers to three-dimensional (3D) scaffolds for biomedical applications faces a number of challenges, viz ., solubility, stability (mechanical and thermal), strength, biocompatibility, and biodegradability. Hence, intensive research on suitable agents to provide the requisite properties has been initiated at the global level. In the present study, an attempt was made to engineer chitosan and collagen macromolecules using sebacic acid, and further evaluation of the mechanical stability and biocompatible property of the engineered scaffold material was done. A 3D scaffold material was prepared using chitosan at 1.0% ( w / v ) and sebacic acid at 0.2% ( w / v ); similarly, collagen at 0.5% ( w / v ) and sebacic acid at 0.2% ( w / v ) were prepared individually by freeze-drying technique. Analysis revealed that the engineered scaffolds displayed an appreciable mechanical strength and, in addition, were found to be biocompatible to NIH 3T3 fibroblast cells. Studies on the chemistry behind the interaction and the characteristics of the cross-linked scaffold materials suggested that non-covalent interactions play a major role in deciding the property of the said polymer materials. The prepared scaffold was suitable for tissue engineering application as a wound dressing material.

Keywords

  • Chitosan,
  • Collagen,
  • Sebacic acid,
  • Mechanical strength,
  • Biocompatible

References

  1. Unknown (2009) Advanced Chemistry Development, Inc.
  2. Austero et al. (2012) New crosslinkers for electrospun chitosan fibre mats (pp. 2551-2562) https://doi.org/10.1098/rsif.2012.0241
  3. Bhumkar and Pokharkar (2006) Studies on effect of pH on crosslinking of chitosan with sodium tripolyphosphate: a technical note (pp. 1-6) https://doi.org/10.1208/pt070250
  4. Bubnis and Ofner (1992) The determination of ε-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid (pp. 129-133) https://doi.org/10.1016/0003-2697(92)90513-7
  5. El-Tahlawy et al. (2006) Novel method for preparation of cyclodextrin/grafted chitosan and its application (pp. 385-392) https://doi.org/10.1016/j.carbpol.2005.08.057
  6. Friess (1998) Collagen—biomaterial for drug delivery (pp. 113-136) https://doi.org/10.1016/S0939-6411(98)00017-4
  7. Gough et al. (2002) Cytotoxicity of glutaraldehyde crosslinked collagen/poly (vinyl alcohol) films is by the mechanism of apoptosis (pp. 121-130) https://doi.org/10.1002/jbm.10145
  8. Iwasaki et al. (2011) Chitosan-based hyaluronic acid hybrid polymer fibers as a scaffold biomaterial for cartilage tissue engineering (pp. 100-113) https://doi.org/10.3390/polym3010100
  9. Jin et al. (2004) Novel chitosan-based films cross-linked by Genipin with improved physical properties (pp. 162-168) https://doi.org/10.1021/bm034286m
  10. Jorge-Herrero et al. (1999) Influence of different chemical cross-linking treatments on the properties of bovine pericardium and collagen (pp. 539-545) https://doi.org/10.1016/S0142-9612(98)90205-8
  11. Ko et al. (2010) Novel synthesis strategies for natural polymer and composite biomaterials as potential scaffolds for tissue engineering (pp. 1981-1997) https://doi.org/10.1098/rsta.2010.0009
  12. Lawrie et al. (2007) Interactions between alginate and chitosan biopolymers characterized using FTIR and XPS (pp. 2533-2541) https://doi.org/10.1021/bm070014y
  13. Ligler et al. (2001) Development of uniform chitosan thin-film layers on silicon chips (pp. 5082-5084) https://doi.org/10.1021/la010148b
  14. Liu et al. (1996) Mechanisms for the transport of α, β-dicarboxylates through the mitochondrial inner membrane (pp. 25338-25344) https://doi.org/10.1074/jbc.271.41.25338
  15. Lopez et al. (2008) A kinetic study on the thermal behaviour of chitosan (pp. 633-639) https://doi.org/10.1007/s10973-007-8321-3
  16. Majumder et al. (2011) Simulated microgravity promoted differentiation of bipotential murine oval liver stem cells by modulating BMP4/Notch1 signaling (pp. 1898-1908) https://doi.org/10.1002/jcb.23110
  17. Miles et al. (2005) The increase in denaturation temperature following cross-linking of type-I collagen is caused by dehydration of the fibres (pp. 551-556) https://doi.org/10.1016/j.jmb.2004.12.001
  18. Milosavljevic et al. (2010) Chitosan, itaconic acid and poly(vinyl alcohol) hybrid polymer networks of high degree of swelling and good mechanical strength (pp. 686-694)
  19. Mitra et al. (2011) Preparation and characterization of a thermostable and biodegradable biopolymers using natural cross-linker (pp. 276-285) https://doi.org/10.1016/j.ijbiomac.2010.11.011
  20. Mitra et al. (2012) Preparation and characterization of malonic acid cross-linked chitosan and collagen 3D scaffolds: an approach on non-covalent interactions (pp. 1309-1321) https://doi.org/10.1007/s10856-012-4586-6
  21. Morris et al. (2009) Autodock4 and AutoDockTools4: automated docking with selective receptor flexibility (pp. 2785-2791) https://doi.org/10.1002/jcc.21256
  22. Mossmann (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays (pp. 55-63) https://doi.org/10.1016/0022-1759(83)90303-4
  23. Nam et al. (2008) Controlling coupling reaction of EDC and NHS for preparation of type-I collagen gels using ethanol/water co-solvents (pp. 32-37) https://doi.org/10.1002/mabi.200700206
  24. Ohkawa et al. (2004) Electrospinning of chitosan (pp. 1600-1605) https://doi.org/10.1002/marc.200400253
  25. Olde Damink et al. (1995) Glutaraldehyde as a cross-linking agent for collagen-based biomaterials (pp. 460-472) https://doi.org/10.1007/BF00123371
  26. Olde Damink et al. (1995) Influence of ethylene oxide gas treatment on the in vitro degradation behavior of dermal sheep type-I collagen (pp. 149-155) https://doi.org/10.1002/jbm.820290203
  27. Parenteau-Bareil et al. (2010) Collagen-based biomaterials for tissue engineering applications (pp. 1863-1887) https://doi.org/10.3390/ma3031863
  28. Pavia et al. (2001) Thomson Learning, Inc
  29. Peng et al. (2006) Preparation and evaluation of porous chitosan/collagen scaffolds for periodontal tissue engineering (pp. 207-220) https://doi.org/10.1177/0883911506065100
  30. Petite et al. (1990) Use of the acyl azide method for cross-linking type-I collagen-rich tissues such as pericardium (pp. 179-187) https://doi.org/10.1002/jbm.820240205
  31. Rinaudo (2010) New way to crosslink chitosan in aqueous solution (pp. 1537-1544) https://doi.org/10.1016/j.eurpolymj.2010.04.012
  32. Saito et al. (2008) Characterization of alkali-treated type-I collagen gels prepared by different crosslinkers (pp. 1297-1305) https://doi.org/10.1007/s10856-007-3239-7
  33. Schauer et al. (2003) Color changes in chitosan and poly(allyl amine) films upon metal binding (pp. 250-257) https://doi.org/10.1016/S0040-6090(03)00055-5
  34. Schiffman and Schauer (2007) Cross-linking chitosan nanofibers (pp. 594-601) https://doi.org/10.1021/bm060804s
  35. Schmidt and Baier (2000) Acellular vascular tissues: natural biomaterials for tissue repair and tissue engineering (pp. 2215-2231) https://doi.org/10.1016/S0142-9612(00)00148-4
  36. Shanmugasundaram et al. (2004) Comparative physico-chemical and in vitro properties of fibrillated collagen scaffolds from different sources (pp. 247-264) https://doi.org/10.1177/0885328204040945
  37. Sheu et al. (2001) Characterization of type-I collagen gel solutions and type-I collagen matrices for cell culture (pp. 1713-1719) https://doi.org/10.1016/S0142-9612(00)00315-X
  38. Tamada and Langer (1992) The development of polyanhydrides for drug delivery applications (pp. 315-353) https://doi.org/10.1163/156856292X00402
  39. Tual et al. (2000) Transport properties of chitosan membranes: influence of crosslinking (pp. 1521-1529) https://doi.org/10.1002/(SICI)1099-0488(20000601)38:11<1521::AID-POLB120>3.0.CO;2-#
  40. Usha and Ramasami (2000) Effect of crosslinking agents (basic chromium sulfate and formaldehyde) on the thermal and thermomechanical stability of rat tail tendon type-I collagen fibre (pp. 59-66) https://doi.org/10.1016/S0040-6031(00)00518-9
  41. Vijayaraghavan et al. (2010) Biocompatibility of choline salts as crosslinking agents for collagen based biomaterials (pp. 294-296) https://doi.org/10.1039/B910601D
  42. Wang et al. (2002) A tough biodegradable elastomer (pp. 602-606) https://doi.org/10.1038/nbt0602-602
  43. Weadock et al. (1995) Physical crosslinking of type-I collagen fibers: comparison of ultraviolet irradiation and dehydrothermal treatment (pp. 1373-1379) https://doi.org/10.1002/jbm.820291108
  44. Wei et al. (1992) The cross linking of chitosan fibers (pp. 2187-2193) https://doi.org/10.1002/pola.1992.080301013