Controlling silk fibroin particle features for drug delivery

Biomaterials

Volumn 31, Issue 16, 2010, Pages 4583-4591

  Lammel, Andreas S ^a   Hu, Xiao ^b,c   Park, Sang Hyug ^b,c   Kaplan, David L ^b,c   Scheibel, Thomas R ^d  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b Tufts University   (United States)

^c TUFTS UNIVERSITY   (United States)

^d UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

Beta sheet; Drug delivery; Self assembly; Silk

Indexed keywords

BETA SHEET; CHARGE-CHARGE INTERACTIONS; CONTROLLABLE SIZE; CRYSTAL VIOLET; EFFECT OF IONIC STRENGTH; ELECTROSTATIC INTERACTIONS; IN-VITRO; INTERMOLECULAR INTERACTIONS; KOSMOTROPIC SALTS; MODEL DRUGS; PARTICLE FORMATIONS; PHYSICAL STABILITY; POST TREATMENT; POTASSIUM PHOSPHATE; PREPARATION METHOD; PROCESSABILITY; PROMISING MATERIALS; RELEASE KINETICS; RHODAMINE B; SALTING OUT; SECONDARY STRUCTURES; SILK FIBROIN; SILK PROTEINS; SMALL MOLECULES;

BIOCOMPATIBILITY; BIODEGRADATION; CHEMICAL STABILITY; CRYSTAL STRUCTURE; CRYSTALLINE MATERIALS; DRUG DELIVERY; DRUG INTERACTIONS; DYES; ETHANOL; IONIC STRENGTH; METHANOL; PHOSPHATES; SELF ASSEMBLY; SILK; ZETA POTENTIAL;

PH EFFECTS;

ALCIAN BLUE; ALCOHOL; CRYSTAL VIOLET; METHANOL; POTASSIUM DIHYDROGEN PHOSPHATE; RHODAMINE B; SILK FIBROIN;

ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED DRUG RELEASE; CONTROLLED STUDY; DRUG DELIVERY SYSTEM; DRUG FORMULATION; IN VITRO STUDY; IONIC STRENGTH; PH; PRIORITY JOURNAL; ZETA POTENTIAL;

ALCIAN BLUE; BIOCOMPATIBLE MATERIALS; COLORING AGENTS; DRUG CARRIERS; DRUG DELIVERY SYSTEMS; FIBROINS; FLUORESCENT DYES; MATERIALS TESTING; PARTICLE SIZE; PROTEIN STRUCTURE, SECONDARY; RHODAMINES; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 77950065443     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2010.02.024     Document Type: Article

References (60)

1. Langer R. New methods of drug delivery. Science 1990, 249:1527-1533.
2. Freiberg S., Zhu X.X. Polymer microspheres for controlled drug release. Int J Pharm 2004, 282:1-18.
3. Edlund U., Albertsson A.C. Degradable polymer microspheres for controlled drug delivery. Degradable aliphatic polyesters 2002, 67-112. Springer, Berlin. A.C. Albertsson (Ed.).
4. Langer R., Peppas N.A. Advances in biomaterials, drug delivery, and bionanotechnology. AIChE J 2003, 49:2990-3006.
5. Daniel S.K. Microparticles and nanoparticle s for drug delivery. Biotechnol Bioeng 2007, 96:203-209.
6. Vandelli M.A., Rivasi F., Guerra P., Forni F., Arletti R. Gelatin microspheres crosslinked with, -glyceraldehyde as a potential drug delivery system: preparation, characterisation, in vitro and in vivo studies. Int J Pharm 2001, 215:175-184.
7. Arshady R. Review: biodegradable microcapsular drug delivery systems: manufacturing methodology, release control and targeting prospects. J Bioact Compat Polym 1990, 5:315-342.
8. George A.D., Thomas B.G., Vinod P.S. Cross-linking of gelatin capsules and its relevance to their in vitro-in vivo performance. J Pharm Sci 1994, 83:915-921.
9. George M., Abraham T.E. Polyionic hydrocolloids for the intestinal delivery of protein drugs: alginate and chitosan - a review. J Control Release 2006, 114:1-14.
10. Liu X., Sun Q., Wang H., Zhang L., Wang J.-Y. Microspheres of corn protein, zein, for an ivermectin drug delivery system. Biomaterials 2005, 26(1):109-115.
11. Won Y.-W., Kim Y.-H. Recombinant human gelatin nanoparticles as a protein drug carrier. J Control Release 2008, 127:154-161.
12. Sahin S., Selek H., Ponchel G., Ercan M.T., Sargon M., Hincal A.A., et al. Preparation, characterization and in vivo distribution of terbutaline sulfate loaded albumin microspheres. J Control Release 2002, 82:345-358.
13. Latha M.S., Rathinam K., Mohanan P.V., Jayakrishnan A. Bioavailability of theophylline from glutaraldehyde cross-linked casein microspheres in rabbits following oral administration. J Control Release 1995, 34:1-7.
14. Allmeling C., Jokuszies A., Reimers K., Kall S., Choi C.Y., Brandes G., et al. Spider silk fibres in artificial nerve constructs promote peripheral nerve regeneration. Cell Prolif 2008, 41:408-420.
15. Vollrath F., Barth P., Basedow A., Engström W., List H. Local tolerance to spider silks and protein polymers in vivo. In Vivo 2002, 16:229-234.
16. Hardy J.G., Römer L.M., Scheibel T.R. Polymeric materials based on silk proteins. Polymer 2008, 49:4309-4327.
17. Altman G.H., Diaz F., Jakuba C., Calabro T., Horan R.L., Chen J., et al. Silk-based biomaterials. Biomaterials 2003, 24:401-416.
18. Horan R.L., Antle K., Collette A.L., Wang Y., Huang J., Moreau J.E., et al. In vitro degradation of silk fibroin. Biomaterials 2005, 26:3385-3393.
19. Hofmann S., Wong Po Foo C.T., Rossetti F., Textor M., Vunjak-Novakovic G., Kaplan D.L., et al. Silk fibroin as an organic polymer for controlled drug delivery. J Control Release 2006, 111:219-227.
20. Wang Y., Rudym D.D., Walsh A., Abrahamsen L., Kim H.-J., Kim H.S., et al. In vivo degradation of three-dimensional silk fibroin scaffolds. Biomaterials 2008, 29:3415-3428.
21. Huang F., Sun L., Zheng J. In vitro and in vivo characterization of a silk fibroin-coated polyester vascular prosthesis. Artif Organs 2008, 32:932-941.
22. Lammel A., Keerl D., Römer L., Scheibel T. Proteins: polymers of natural origin. Recent advances in biomaterials research 2008, 1-22. Transworld Research Network, Trivandrum. J. Hu (Ed.).
23. Heim M., Keerl D., Scheibel T. Spider silk: from soluble protein to extraordinary fibers. Angew Chem Int Ed Engl 2009, 48:3584-3596.
24. Heim M., Römer L., Scheibel T. Hierarchical structures made of protein. Chem Soc Rev 2010, 39:156-164.
25. Donath E., Sukhorukov G.B., Caruso F., Davis S.A., Möhwald H. Novel hollow polymer shells by colloid-templated assembly of polyelectrolytes. Angew Chem Int Ed Engl 1998, 37:2201-2205.
26. Hermanson K.D., Huemmerich D., Scheibel T., Bausch A.R. Engineered microcapsules fabricated from reconstituted spider silk. Adv Mater 2007, 19:1810-1815.
27. Wang X., Wenk E., Matsumoto A., Meinel L., Li C., Kaplan D.L. Silk microspheres for encapsulation and controlled release. J Control Release 2007, 117:360-370.
28. Wenk E., Wandrey A.J., Merkle H.P., Meinel L. Silk fibroin spheres as a platform for controlled drug delivery. J Control Release 2008, 132:26-34.
29. Gobin A.S., Rhea R., Newman R.A., Mathur A.B. Silk-fibroin-coated liposomes for long-term and targeted drug delivery. Int J Nanomedicine 2006, 1:81-87.
30. Rubino O.P., Kowalsky R., Swarbrick J. Albumin microspheres as a drug delivery system: relation among turbidity ratio, degree of cross-linking, and drug release. Pharm Res 1993, 10:1059-1065.
31. MacAdam A.B., Shafi Z.B., James S.L., Marriott C., Martin G.P. Preparation of hydrophobic and hydrophilic albumin microspheres and determination of surface carboxylic acid and amino residues. Int J Pharm 1997, 151:47-55.
32. Weber C., Coester C., Kreuter J., Langer K. Desolvation process and surface characterisation of protein nanoparticles. Int J Pharm 2000, 194:91-102.
33. Brick M.C., Palmer H.J., Whitesides T.H. Formation of colloidal dispersions of organic materials in aqueous media by solvent shifting. Langmuir 2003, 19:6367-6380.
34. Zhang Y.-Q., Shen W.-D., Xiang R.-L., Zhuge L.-J., Gao W.-J., Wang W.-B. Formation of silk fibroin nanoparticles in water-miscible organic solvent and their characterization. J Nanopart Res 2007, 9:885-900.
35. Allémann E., Gurny R., Doelker E. Preparation of aqueous polymeric nanodispersions by a reversible salting-out process: influence of process parameters on particle size. Int J Pharm 1992, 87:247-253.
36. Reza A. Microspheres and microcapsules, a survey of manufacturing techniques part II: coacervation. Polymer Eng Sci 1990, 30:905-914.
37. Reza A. Microspheres and microcapsules, a survey of manufacturing techniques: part III: solvent evaporation. Polymer Eng Sci 1990, 30:915-924.
38. Horn D., Rieger J. Organic nanoparticles in the aqueous phase - theory, experiment, and use. Angew Chem Int Ed Engl 2001, 40:4330-4361.
39. Cao Z., Chen X., Yao J., Huang L., Shao Z. The preparation of regenerated silk fibroin microspheres. Soft Matter 2007, 3:910-915.
40. Slotta U.K., Rammensee S., Gorb S., Scheibel T. An engineered spider silk protein forms microspheres. Angew Chem Int Ed Engl 2008, 47:4592-4594.
41. Lammel A., Schwab M., Slotta U., Winter G., Scheibel T. Processing conditions for the formation of spider silk microspheres. ChemSusChem 2008, 1:413-416.
42. Rammensee S., Slotta U., Scheibel T., Bausch A.R. Assembly mechanism of recombinant spider silk proteins. Proc Natl Acad Sci U S A 2008, 105:6590-6595.
43. Liebmann B., Hümmerich D., Scheibel T., Fehr M. Formulation of poorly water-soluble substances using self-assembling spider silk protein. Colloids Surf A 2008, 331:126-132.
44. Lammel A, Schwab M, Hofer M, Winter G, Scheibel T. Spider silk submicroparticles for controlled drug delivery, submitted for publication.
45. Sofia S., McCarthy M.B., Gronowicz G., Kaplan D.L. Functionalized silk-based biomaterials for bone formation. J Biomed Mater Res 2001, 54:139-148.
46. Hu X., Kaplan D.L., Cebe P. Determining beta-sheet crystallinity in fibrous proteins by thermal analysis and infrared spectroscopy. Macromolecules 2006, 39:6161-6170.
47. Foo C.W.P., Bini E., Hensman J., Knight D.P., Lewis R.V., Kaplan D.L. Role of pH and charge on silk protein assembly in insects and spiders. Appl Phys A 2006, 82:223-233.
48. Wang X., Kluge J.A., Leisk G.G., Kaplan D.L. Sonication-induced gelation of silk fibroin for cell encapsulation. Biomaterials 2008, 29:1054-1064.
49. Tanaka K., Kajiyama N., Ishikura K., Waga S., Kikuchi A., Ohtomo K., et al. Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori. Biochim Biophys Acta 1999, 1432:92-103.
50. Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982, 157:105-132.
51. Swiss Institute of Bioinformatics ExPASy proteomics server Available from URL:. http://www.expasy.ch/.
52. Jin H.-J., Kaplan D.L. Mechanism of silk processing in insects and spiders. Nature 2003, 424:1057-1061.
53. Terry A.E., Knight D.P., Porter D., Vollrath F. pH Induced changes in therheology of silk fibroin solution from the middle division of Bombyx mori silkworm. Biomacromolecules 2004, 5:768-772.
54. Mita K., Ichimura S., James T.C. Highly repetitive structure and its organization of the silk fibroin gene. J Mol Evol 1994, 38:583-592.
55. Sponner A., Unger E., Grosse F., Weisshart K. Conserved C-termini of spidroins are secreted by the major ampullate glands and retained in the silk thread. Biomacromolecules 2004, 5:840-845.
56. Bini E., Knight D.P., Kaplan D.L. Mapping domain structures in silks from insects and spiders related to protein assembly. J Mol Biol 2004, 335:27-40.
57. Chen P., Kim H.S., Park C.-Y., Kim H.-S., Chin I.-J., Jin H.-J. pH-Triggered transition of silk fibroin from spherical micelles to nanofibrils in water. Macromol Res 2008, 16:539-543.
58. Eisoldt L, Hardy J, Heim M, Scheibel T. The role of salt and shear on the storage and assembly of spider silk proteins. J Struct Biol, in press, doi:10.1016/j.jsb.2009.12.027. doi:10.1016/j.jsb.2009.12.027.
59. Heim M, Ackerschott C, Scheibel T. Characterisation of recombinantly produced spider flagelliform domains. J Struct Biol, in press, doi:10.1016/j.jsb.2009.12.025. doi:10.1016/j.jsb.2009.12.025.
60. Hagn F, Eisoldt L, Hardy J, Vendrely C, Coles M, Scheibel T., et al. A highly conserved spider silk domain acts as a molecular switch that controls fibre assembly. Nature, in press.