Controllable transition of silk fibroin nanostructures: An insight into in vitro silk self-assembly process

Acta Biomaterialia

Volumn 9, Issue 8, 2013, Pages 7806-7813

  Bai, S ^a,b   Liu, S ^a   Zhang, C ^a   Xu, W ^b   Lu, Q ^a   Han, H ^b   Kaplan, D L ^c   Zhu, H ^d  

^a SOOCHOW UNIVERSITY   (China)

^b MEDICAL COLLEGE OF SOOCHOW UNIVERSITY   (China)

^c Tufts University   (United States)

^d BEIJING INSTITUTE OF TECHNOLOGY   (China)

Author keywords

Biomaterials; Charge distribution; Nanofiber; Self assembly; Silk

Indexed keywords

ASSEMBLY; BIOLOGICAL MATERIALS; NANOFIBERS; SOLUTIONS; STRUCTURAL PROPERTIES;

CRITICAL FACTORS; HIERARCHICAL STRUCTURES; IN-VITRO; NANO-FIBRILS; SECONDARY CONFORMATION; SELF ASSEMBLY PROCESS; SILK; SILK FIBRES; SILK FIBROIN; SIMPLE++;

SELF ASSEMBLY;

NANOFIBER; NANOPARTICLE; SILK; SILK FIBROIN; BIOMATERIAL; FIBROIN; FIBROIN, SILKWORM; MACROMOLECULE;

AQUEOUS SOLUTION; ARTICLE; CHEMICAL STRUCTURE; CONFORMATION; IN VITRO STUDY; PRIORITY JOURNAL; VISCOSITY; CHEMISTRY; CRYSTALLIZATION; MACROMOLECULE; MATERIALS TESTING; PARTICLE SIZE; PHASE TRANSITION; PROCEDURES; SURFACE PROPERTY; SYNTHESIS; TENSILE STRENGTH; ULTRASTRUCTURE; YOUNG MODULUS; METHODOLOGY;

BIOCOMPATIBLE MATERIALS; CRYSTALLIZATION; ELASTIC MODULUS; FIBROINS; MACROMOLECULAR SUBSTANCES; MATERIALS TESTING; MOLECULAR CONFORMATION; NANOFIBERS; PARTICLE SIZE; PHASE TRANSITION; SURFACE PROPERTIES; TENSILE STRENGTH; VISCOSITY;

EID: 84891670112     PISSN: 17427061     EISSN: 18787568     Source Type: Journal    
DOI: 10.1016/j.actbio.2013.04.033     Document Type: Article

References (49)

1. Omenetto FG, Kaplan DL. New opportunities for an ancient material. Science 2010;329(5991):528-31.
2. Gosline JM, Demont ME, Denny MW. The structure and properties of spider silk. Endeavour 1986;10:37-43.
3. Jin HJ, Kaplan DL. Mechanism of silk processing in insects and spiders. Nature 2003;424:1057-61.
4. Hagn F, Eisoldt L, Hardy JG, Vendrely C, Coles M, Scheibel T, et al. A conserved spider silk domain acts as a molecular switch that controls fibre assembly. Nature 2010;465:239-42.
5. Vollrath F, Madsen B, Shao ZZ. The effect of spinning conditions on the mechanics of a spider's dragline silk. Proc Biol Sci 2001;268(1483):2339-46.
6. Lefevre T, Rousseau ME, Pezolet M. Protein secondary structure and orientation in silk as revealed by Raman spectromicroscopy. Biophys J 2007;92(8):2885-95.
7. Thiel BL, Guess KB, Viney C. Non-periodic lattice crystals in the hierarchical microstructure of spider (major ampullate) silk. Biopolymers 1997;41(7):703-19.
8. Du N, Liu XY, Narayanan J, Li L, Lim MLM, Li DQ. Design of superior spider silk: from nanostructure to mechanical properties. Biophys J 2006;91(12):4528-35.
9. Lee SM, Pippel E, Gosele U, Dresbach C, Qin Y, Chandran CV, et al. Greatly increased toughness of infiltrated spider silk. Science 2009;324(5926):488-92.
10. Keten S, Xu ZP, Ihle B, Buehler MJ. Nanoconfinement controls stiffness, strength and mechanical toughness of b-sheet crystals in silk. Nat Mater 2010;9:359-67.
11. Jiang CY, Wang XY, Gunawidjaja R, Lin YH, Gupta MK, Kaplan DL, et al. Mechanical properties of robust ultrathin silk fibroin films. Adv Funct Mater 2007;17(13):2229-37.
12. Liu HF, Fan HB, Wang Y, Toh SL, Goh JCH. The interaction between a combined knitted silk scaffold and microporous silk sponge with human mesenchymal stem cells for ligament tissue engineering. Biomaterials 2008;29(6):662-74.
13. Wang XQ, Wenk E, Matsumoto A, Meinel L, Li CM, Kaplan DL. Silk microspheres for encapsulation and controlled release. J Control Release 2007;117(3):360-70.
14. Rockwood DN, Preda RC, Yucel T, Wang XQ, Lovett ML, Kaplan DL. Materials fabrication from Bombyx mori silk fibroin. Nat Protoc 2011;6:1612-31.
15. Yao DY, Dong S, Lu Q, Hu X, Kaplan DL, Zhang BB, et al. Salt-leached silk scaffolds with tunable mechanical properties. Biomacromolecules 2012;13(11):3723-9.
16. Vollrath F, Knight DP. Liquid crystalline spinning of spider silk. Nature 2001;410:541-8.
17. Putthanarat S, Stribeck N, Fossey SA, Eby RK, Adams WW. Investigation of the nanofibrils of silk fibers. Polymer 2000;41(21):7735-47.
18. Perez-Rigueiro J, Viney C, Llorca J, Elices M. Silkworm silk as an engineering material. J Appl Polym Sci 1998;70(12):2439-47.
19. Xia XX, Xu QB, Hu X, Qin GK, Kaplan DL. Tunable self-assembly of genetically engineered silk-elastin-like protein polymers. Biomacromolecules 2011;12(11):3844-50.
20. Arcidiacono S, Mello CM, Butler M, Welsh E, Soares JW, Allen A, et al. Aqueous processing and fiber spinning of recombinant spider silks. Macromolecules 2002;35(4):1262-6.
21. Stark M, Grip S, Rising A, Hedhammar M, Engstrom W, Hjalm G, et al. Macroscopic fibers self-assembled from recombinant miniature spider silk proteins. Biomacromolecules 2007;8(5):1695-701.
22. Greving I, Cai MZ, Vollrath F, Schniepp HC. Shear-induced self-assembly of native silk proteins into fibrils studied by atomic force microscopy. Biomacromolecules 2012;13(3):676-82.
23. Gong ZG, Huang L, Yang YH, Chen X, Shao ZZ. Two distinct b-sheet fibrils from silk protein. Chem Commun 2009;48:7506-8.
24. Zhang F, Zuo BQ, Fan ZH, Xie ZG, Lu Q, Zhang XG, et al. Mechanisms and control of silk-based electrospinning. Biomacromolecules 2012;13(3): 798-804.
25. Wittmer CR, Hu X, Gauthier P, Weisman S, Kaplan DL, Sutherland TD. Production, structure and in vitro degradation of electrospun honeybee silk nanofibers. Acta Biomater 2011;7(10):3789-95.
26. Lu Q, Zhu HS, Zhang CC, Zhang F, Zhang B, Kaplan DL. Silk self-assembly mechanisms and control from thermodynamics to kinetics. Biomacromolecules 2012;13(3):826-32.
27. Numata K, Yamazaki S, Naga N. Biocompatible and biodegradable dual-drug release system based on silk hydrogel containing silk nanoparticles. Biomacromolecules 2012;13(5):1383-9.
28. Mathur AB, Gupta V. Silk fibroin-derived nanoparticles for biomedical applications. Nanomedicine 2010;5(5):807-20.
29. Lu Q, Huang YL, Li MZ, Zuo BQ, Lu SZ, Wang JN, et al. Silk fibroin electrogelation mechanisms. Acta Biomater 2011;7(6):2394-400.
30. Leclerc J, Lefevre T, Pottier F, Morency LP, Lapointe-Verreault C, Gagne SM, et al. Structure and pH-induced alterations of recombinant and natural spider silk proteins in solution. Biopolymers 2012;97(6):337-46.
31. Dicko C, Knight D, Kenney JM, Vollrath F. Secondary structures and conformational changes in flagelliform, cylindrical, major, and minor ampullate silk proteins. Temperature and concentration effects. Biomacromolecules 2004;5(6):2105-15.
32. Dicko C, Knight D, Kenney JM, Vollrath F. Structural conformation of spidroin in solution: a synchrotron radiation circular dichroism study. Biomacromolecules 2004;5(3):758-67.
33. Yang YH, Shao ZZ, Chen X, Zhou P. Optical spectroscopy to investigate the structure of regenerated Bombyx mori silk fibroin in solution. Biomacromolecules 2004;5(3):773-9.
34. Li XG, Wu LY, Huang MR, Shao HL, Hu XC. Conformational transition and liquid crystalline state of regenerated silk fibroin in water. Biopolymers 2007;89(6):497-505.
35. Holland C, Terry AE, Porter D, Vollrath F. Natural and unnatural silks. Polymer 2007;48(12):3388-92.
36. Chen P, Kim HS, Park CY, Kim HS, Chin IJ, Jin HJ. pH-Triggered transition of silk fibroin from spherical micelles to nanofibrils in water. Macromol Res 2008;16:539-43.
37. Golinska MD, Pham TTH, Werten MWT, Wolf FAA, Stuart MAC, Gucht JVD. Fibril formation by pH and temperature responsive silk-elastin block copolymers. Biomacromolecules 2013;14(1):48-55.
38. Lammel AS, Hu X, Park SH, Kaplan DL, Scheibel TR. Controlling silk fibroin particle features for drug delivery. Biomaterials 2010;31(16):4583-91.
39. Liebmann B, Hummerich D, Scheibel T, Fehr M. Formulation of poorly watersoluble substances using self-assembling spider silk protein. Colloids Surf A 2008;331:126-32.
40. Eisoldt L, Hardy JG, Heim M, Scheibel TR. The role of salt and shear on the storage and assembly of spider silk proteins. J Struct Biol 2010;170(2): 413-9.
41. 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(3):840-5.
42. Hu X, Shmelev K, Sun L, Gil ES, Park SH, Cebe P, et al. Regulation of silk material structure by temperature-controlled water vapor annealing. Biomacromolecules 2011;12(5):1686-96.
43. Terry AE, Knight DP, Porter D, Vollrath F. pH Induced changes in the rheology of silk fibroin solution from the middle division of Bombyx mori silkworm. Biomacromolecules 2004;5(3):768-72.
44. An B, Jenkins JE, Sampath S, Holland GP, Hinman M, Yarger JL, et al. Reproducing natural spider silks' copolymer behavior in synthetic silk mimics. Biomacromolecules 2012;13(12):3938-48.
45. Holland C, Porter D, Vollrath F. Comparing the rheology of mulberry and "wild" silkworm spinning dopes. Biopolymers 2012;97(6):362-7.
46. Holland C, Terry AE, Porter D, Vollrath F. Comparing the rheology of native spider and silkworm spinning dope. Nat Mater 2006;5:870-4.
47. Matsumoto A, Lindsay A, Abedian B, Kaplan DL. Silk fibroin solution properties related to assembly and structure. Macromol Biosci 2008;8(11):1006-18.
48. Ebenstein DM, Wahl KJ. Anisotropic nanomechanical properties of Nephila clavipes dragline silk. J Mater Res 2006;21(8):2035-44.
49. Zhang CC, Song DW, Lu Q, Hu X, Kaplan DL, Zhu HS. Flexibility regeneration of silk fibroin in vitro. Biomacromolecules 2012;13(7):2148-53.