Enhancing collagen stability through nanostructures containing chromium(III) oxide

Colloids and Surfaces B: Biointerfaces

Volumn 100, Issue , 2012, Pages 36-41

  Sangeetha, Selvam ^a   Ramamoorthy, Usha ^a   Sreeram, Kalarical Janardhanan ^a   Nair, Balachandran Unni ^a  

^a CENTRAL LEATHER RESEARCH INSTITUTE   (India)

Author keywords

Circular dichroism; Collagen; Copolymer; Nanostructures; Self assembly; Stress analysis

Indexed keywords

BIOMEDICAL APPLICATIONS; CHROMIUM OXIDES; COLLAGEN FIBRES; COLLAGEN STABILITY; CROSSLINKS; DRUG RELEASE; FTIR; FUNCTIONALIZATIONS; LEATHER INDUSTRIES; MECHANICAL DEGRADATION; METAL OXIDE NANOPARTICLES; METAL OXIDES; NANOPARTICULES; POLYMERIC MATRICES; POLYPHENOLS; RATE-LIMITING STEPS; SMART APPLICATIONS; STANDARD PROTOCOLS; THREE-DIMENSIONAL ARCHITECTURE;

ALDEHYDES; CHROMIUM; COPOLYMERS; DEGRADATION; DICHROISM; DIMETHYL SULFOXIDE; FUNCTIONAL GROUPS; MEDICAL APPLICATIONS; METAL IONS; METALLIC COMPOUNDS; NANOPARTICLES; NANOSTRUCTURES; ORGANIC ACIDS; PHENOLS; POLYMERS; POLYSTYRENES; SELF ASSEMBLY; STABILIZATION; STRESS ANALYSIS; VISCOSITY MEASUREMENT;

COLLAGEN;

CHROMIC OXIDE; CHROMIUM DERIVATIVE; COLLAGEN; COPOLYMER; DIMETHYL SULFOXIDE; FUNCTIONAL GROUP; NANOMATERIAL; POLYACRYLIC ACID; POLYMER; POLYSTYRENE; POLYSTYRENE BLOCK POLYACRYLIC ACID COPOLYMER; UNCLASSIFIED DRUG;

AQUEOUS SOLUTION; ARTICLE; CHEMICAL ANALYSIS; CHEMICAL REACTION; CHEMICAL STRUCTURE; CONTROLLED STUDY; DRUG RELEASE; ENCAPSULATION; INFRARED SPECTROSCOPY; MECHANICAL STABILITY; MOLECULAR STABILITY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN INTERACTION; PROTEIN STABILITY; STRESS ANALYSIS; THERMOSTABILITY; VISCOSITY;

ACRYLATES; BIOCOMPATIBLE MATERIALS; CHROMIUM COMPOUNDS; CIRCULAR DICHROISM; COLLAGEN; DELAYED-ACTION PREPARATIONS; DIFFUSION; MICROSCOPY, ELECTRON, TRANSMISSION; NANOSTRUCTURES; POLYSTYRENES; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SURFACE PROPERTIES; TEMPERATURE; VISCOSITY;

EID: 84863210450     PISSN: 09277765     EISSN: 18734367     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2012.05.015     Document Type: Article

References (41)

1. Gautieri A., Vesentini S., Redaelli A., Buehler M.J. Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up. Nano Lett. 2011, 11:757-766.
2. Kadler K.E., Baldock C., Bella J., Boot-Handford R.P. Collagens at a glance. J. Cell Sci. 2007, 120:1955-1958.
3. Brown Eleanor M. Collagen networks: nature and beyond. Advances in Biopolymers 2006, vol. 935. American Chemical Society, pp. 36-51.
4. Tomihata K., Burczak K., Shiraki K., Ikada Y. Cross-linking and biodegradation of native and denatured collagen. Polymers of Biological and Biomedical Significance 1993, vol. 540. American Chemical Society, pp. 275-286.
5. Lynn A.K., Yannas I.V., Bonfield W. Antigenicity and immunogenicity of collagen. J. Biomed. Mater. Res. Part B: Appl. Biomater. 2004, 71B:343-354.
6. O'Grady J.E., Bordon D.M. Global regulatory registration requirements for collagen-based combination products: points to consider. Adv. Drug Deliv. Rev. 2003, 55:1699-1721.
7. Stenzel Kurt H., Miyata T., Kohno I., Schlear Susan D., Rubin Albert L. Collagen Surfaces in Biomedical Applications. Applied Chemistry at Protein Interfaces 1975, vol. 145. American Chemical Society, pp. 26-40.
8. Olde Damink L.H.H., Dijkstra P.J., van Luyn M.J.A., van Wachem P.B., Nieuwenhuis P., Feijen J. Cross-linking of dermal sheep collagen using a water-soluble carbodiimide. Biomaterials 1996, 17:765-773.
9. Zeeman R., Dijkstra P.J., van Wachem P.B., van Luyn M.J.A., Hendriks M., Cahalan P.T., Feijen J. Successive epoxy and carbodiimide cross-linking of dermal sheep collagen. Biomaterials 1999, 20:921-931.
10. Stupp S.I. Self-assembly and biomaterials. Nano Lett. 2010, 10:4783-4786.
11. Castaneda L., Valle J., Yang N., Pluskat S., Slowinska K. Collagen cross-linking with Au nanoparticles. Biomacromolecules 2008, 9:3383-3388.
12. Homenick C.M., de Silveira G., Sheardown H., Adronov A. Pluronics as crosslinking agents for collagen: novel amphiphilic hydrogels. Polym. Int. 2011, 60:458-465.
13. Teixeira S., Yang L., Dijkstra P.J., Ferraz M.P., Monteiro F.J. Heparinized hydroxyapatite/collagen three-dimensional scaffolds for tissue engineering. J. Mater. Sci.: Mater. Med. 2010, 21:2385-2392.
14. Hong J., Kharenko O.A., Ogawa M.Y. Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up. Inorg. Chem. 2006, 45:9974-9984.
15. Koide T. Triple helical collagen-like peptides: engineering and applications in matrix biology. Connect. Tissue Res. 2005, 46:131-141.
16. Przybyla D.E., Chmielewski J. Higher-order assembly of collagen peptides into nano- and microscale materials. Biochemistry 2010, 49:4411-4419.
17. Cejas M.A., Kinney W.A., Chen C., Leo G.C., Tounge B.A., Vinter J.G., Joshi P.P., Maryanoff B.E. Collagen-related peptides:  self-assembly of short, single strands into a functional biomaterial of micrometer scale. J. Am. Chem. Soc. 2007, 129:2202-2203.
18. Kotch F.W., Raines R.T. Self-assembly of synthetic collagen triple helices. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:3028-3033.
19. Paramonov S.E., Gauba V., Hartgerink J.D. Synthesis of collagen-like peptide polymers by native chemical ligation. Macromolecules 2005, 38:7555-7561.
20. Przybyla D.E., Chmielewski J. Metal-triggered radial self-assembly of collagen peptide fibers. J. Am. Chem. Soc. 2008, 130:12610-12611.
21. Brodsky B., Thiagarajan G., Madhan B., Kar K. Triple-helical peptides: an approach to collagen conformation, stability, and self-association. Biopolymers 2008, 89:345-353.
22. Hwang E.S., Thiagarajan G., Parmar A.S., Brodsky B. Interruptions in the collagen repeating tripeptide pattern can promote supramolecular association. Protein Sci. 2010, 19:1053-1064.
23. Ramasami T. Approach towards a unified theory for tanning: Wilson's dream. J. Am. Leather Chemists Assoc. 2001, 96:290-304.
24. Sreeram K.J., Ramasami T. Sustaining tanning process through conservation, recovery and better utilization of chromium. Resour. Conservation Recycl. 2003, 38:185-212.
25. Balamurugan K., Rajaram R., Ramasami T. Caspase-3: its potential involvement in Cr(III)-induced apoptosis of lymphocytes. Mol. Cell. Biochem. 2004, 259:43-51.
26. Balamurugan K., Rajaram R., Ramasami T., Narayanan S. Chromium(III)-induced apoptosis of lymphocytes: death decision by ROS and Src-family tyrosine kinases. Free Radic. Biol. Med. 2002, 33:1622-1640.
27. Rajaram R., Nair B.U., Ramasami T. Chromium(III) induced abnormalities in human lymphocyte cell-proliferation - evidence for apoptosis. Biochem. Biophys. Res. Commun. 1995, 210:434-440.
28. Hedberg Y., Gustafsson J., Karlsson H.L., Moller L., Wallinder I.O. Bioaccessibility, bioavailability and toxicity of commercially relevant iron- and chromium-based particles: in vitro studies with an inhalation perspective. Part. Fibre Toxicol. 2010, 7:14.
29. Kim B.-S., Qiu J.-M., Wang J.-P., Taton T.A. Magnetomicelles: composite nanostructures from magnetic nanoparticles and cross-linked amphiphilic block copolymers. Nano Lett. 2005, 5:1987-1991.
30. Xu C., Wayland B.B., Fryd M., Winey K.I., Composto R.J. pH-Responsive nanostructures assembled from amphiphilic block copolymers. Macromolecules 2006, 39:6063-6070.
31. Chandrakasan G., Torchia D.A., Piez K.A. Preparation of intact monomeric collagen from rat tail tendon and skin and the structure of the nonhelical ends in solution. J. Biol. Chem. 1976, 251:6062-6067.
32. Watanabe K., Tezuka Y., Ishii T. Configuration between re-formed collagen triple helices and artificially introduced cross-links in gelatin gels. Macromolecules 1997, 30:7910-7913.
33. Brown F.R., Carver J.P., Blout E.R. Low temperature circular dichroism of poly (glycyl-l-prolyl-l-alanine). J. Mol. Biol. 1969, 39:307-313.
34. Brown F.R., Di Corato A., Lorenzi G.P., Blout E.R. Synthesis and structural studies of two collagen analogues: poly (l-prolyl-l-seryl-glycyl) and poly (l-prolyl-l-alanyl-glycyl). J. Mol. Biol. 1972, 63:85-99.
35. Brodsky-Doyle B., Leonard K.R., Reid K.B. Circular-dichroism and electron-microscopy studies of human subcomponent C1q before and after limited proteolysis by pepsin. Biochem. J. 1976, 159:279-286.
36. Feng Y.B., Melacini G., Taulane J.P., Goodman M. Collagen-based structures containing the peptoid residue N-isobutylglycine (Nleu): synthesis and biophysical studies of Gly-Pro-Nleu sequences by circular dichroism, ultraviolet absorbance, and optical rotation. Biopolymers 1996, 39:859-872.
37. Nutting G.C., Borasky R. Microscopic methods for determining shrinkage temperature of collagen and leather. J. Am. Leather Chemists Assoc. 1949, 44:831-839.
38. Zhang Z.K., Li G.Y., Shi B. Physicochemical properties of collagen, gelatin and collagen hydrolysate derived from bovine limed split wastes. J. Soc. Leather Technologists Chemists 2006, 90:23-28.
39. Silver F.H., Ebrahimi A., Snowhill P.B. Viscoelastic properties of self-assembled type I collagen fibers: molecular basis of elastic and viscous behaviors. Connect. Tissue Res. 2002, 43:569-580.
40. Sulea D., Albu M.G., Ghica M.V., Brazdaru L., Leca M., Popa L. Characterization and in vitro release of chlorhexidine digluconate contained in type I collagen porous matrices. Rev. Roum. Chim. 2011, 56:65-71.
41. Sulea D., Ghica M.V., Micutz M., Albu M.G., Brazdaru L., Staicu T., Leca M., Popa L. Characterization and in vitro release of chlorhexidine digluconate comprised in type I collagen hydrogels. Rev. Roum. Chim. 2010, 55:543-551.