Impact of silk biomaterial structure on proteolysis

Acta Biomaterialia

Volumn 11, Issue 1, 2015, Pages 212-221

  Brown, Joseph ^a   Lu, Chia Li ^a   Coburn, Jeannine ^a   Kaplan, David L ^a  

^a Tufts University   (United States)

Author keywords

Digestion; Films; Hydrogels; Protease; Silk

Indexed keywords

AMORPHOUS FILMS; DEGRADATION; ELECTROPHORESIS; ENZYME ACTIVITY; FOURIER TRANSFORM INFRARED SPECTROSCOPY; PROTEOLYSIS; SODIUM DODECYL SULFATE; SULFUR COMPOUNDS;

BIOMATERIAL STRUCTURES; COLLAGENASE; DIGESTION; MATRIX METALLOPROTEINASE (MMPS); MATRIX METALLOPROTEINASE-1; PROTEASE; PROTEINASE K; PROTEOLYTIC SUSCEPTIBILITY; SECONDARY STRUCTURES; SILK;

HYDROGELS;

CHYMOTRYPSIN A; COLLAGENASE; GELATINASE A; INTERSTITIAL COLLAGENASE; PEPTIDE FRAGMENT; PROTEINASE K; SILK FIBROIN; ARTIFICIAL MEMBRANE; BIOMATERIAL; HYDROGEL; PEPTIDE HYDROLASE; SILK;

ARTICLE; BOMBYX MORI; CONTROLLED STUDY; ENZYMATIC DEGRADATION; ENZYME ACTIVITY; ENZYME STRUCTURE; HYDROGEL; IN VITRO STUDY; INFRARED RADIATION; INFRARED SPECTROSCOPY; NONHUMAN; PEPTIDE MAPPING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; QUANTITATIVE ANALYSIS; SCANNING ELECTRON MICROSCOPY; SOLID STATE; SURFACE PROPERTY; WEIGHT REDUCTION; ARTIFICIAL MEMBRANE; CHEMISTRY; MATERIALS TESTING; MOLECULAR WEIGHT; PROTEIN CONFORMATION; PROTEIN DEGRADATION; ULTRASTRUCTURE;

BIOCOMPATIBLE MATERIALS; HYDROGELS; MATERIALS TESTING; MEMBRANES, ARTIFICIAL; MOLECULAR WEIGHT; PEPTIDE HYDROLASES; PROTEIN CONFORMATION; PROTEOLYSIS; SILK;

EID: 84925085870     PISSN: 17427061     EISSN: 18787568     Source Type: Journal    
DOI: 10.1016/j.actbio.2014.09.013     Document Type: Article

References (50)

1. Wang Y, Kim H-J, Vunjak-Novakovic G, Kaplan DL. Stem cell-based tissue engineering with silk biomaterials. Biomaterials 2006;27(36):6064-82.
2. Numata K, Kaplan DL. Silk-based gene carriers with cell membrane destabilizing peptides. Biomacromolecules 2010;11:3189-95.
3. Lammel AS, Hu X, Park S-H, Kaplan DL, Scheibel TR. Controlling silk fibroin particle features for drug delivery. Biomaterials 2010;31(16):4583-91.
4. Wharram SE, Zhang X, Kaplan DL, McCarthy SP. Electrospun silk material systems for wound healing. Macromol Biosci 2010;10(3):246-57.
5. Yamada H, Igarashi Y, Takasu Y, Saito H, Tsubouchi K. Identification of fibroin-derived peptides enhancing the proliferation of cultured human skin fibroblasts. Biomaterials 2004;25(3):467-72.
6. Zhou CZ, Confalonieri F, Medina N, Zivanovic Y, Esnault C, Yang T, et al. Fine organization of Bombyx mori fibroin heavy chain gene. Nucleic Acids Res 2000;28(12):2413-9.
7. Zhou CZ, Confalonieri F, Jacquet M, Perasso R, Li ZG, Janin J. Silk fibroin: structural implications of a remarkable amino acid sequence. Proteins 2001;44(2):119-22.
8. Vepari C, Kaplan D. Silk as a biomaterial. Prog Polym Sci 2007;32(8-9):991-1007.
9. Tibbitt MW, Anseth KS. Hydrogels as extracellular matrix mimics for 3D cell culture. Biotechnol Bioeng 2009;103(4):655-63.
10. Eppley BL, Dadvand B. Injectable soft-tissue fillers: clinical overview. Plast Reconstr Surg 2006;118(4):98e-106e.
11. Jackson JK, Zhao J, Wong W, Burt HM. The inhibition of collagenase induced degradation of collagen by the galloyl-containing polyphenols tannic acid, epigallocatechin gallate and epicatechin gallate. J Mater Sci Mater Med 2010;21(5):1435-43.
12. Jones D, Tezel A, Borrell M. In vitro resistance to degradation of hyaluronic acid dermal fillers by ovine testicular hyaluronidase. Dermatol Surg 2010;36:804-9.
13. Altman GH, Diaz F, Jakuba C, Calabro T, Horan RL, Chen J, et al. Silk-based biomaterials. Biomaterials 2003;24:401-16.
14. Yucel T, Cebe P, Kaplan DL. Vortex-induced injectable silk fibroin hydrogels. Biophys J 2009;97(7):2044-50.
15. Wang X, Kluge J, Leisk GG, Kaplan DL. Sonication-induced gelation of silk fibroin for cell encapsulation. Biomaterials 2008;29(8):1054-64.
16. Horan RL, Antle K, Collette AL, Wang Y, Huang J, Moreau JE, et al. In vitro degradation of silk fibroin. Biomaterials 2005;26(17):3385-93.
17. Kim U-J, Park J, Li C, Jin H-J, Valluzzi R, Kaplan DL. Structure and properties of silk hydrogels. Biomacromolecules 2004;5(3):786-92.
18. Fini M, Motta A, Torricelli P, Giavaresi G, Nicoli Adini N, Tschon M. The healing of confined critical size cancellous defects in the presence of silk fibroin hydrogel. Biomaterials 2005;26(17):3527-36.
19. Kim U-J, Park J, Kim HJ, Wada M, Kaplan DL. Three-dimensional aqueousderived biomaterial scaffolds from silk fibroin. Biomaterials 2005;26(15):2775-85.
20. Arai T, Freddi G, Innocenti R, Tsukada M. Biodegradation of Bombyx mori silk fibroin fibers and films. J Appl Polym Sci 2003;91:2383-90.
21. Li M, Ogiso M, Minoura N. Enzymatic degradation behavior of porous silk fibroin sheets. Biomaterials 2003;24(2):357-65.
22. Numata K, Cebe P, Kaplan DL. Mechanism of enzymatic degradation of beta-sheet crystals. Biomaterials 2010;31(10):2926-33.
23. Curran S, Murray G. Matrix metalloproteinases in tumour invasion and metastasis. J Pathol 1999;189:300-8.
24. Nagase H. Matrix metalloproteinases. J Biol Chem 1999;274(31):21491-4.
25. Talukdar S, Mandal M, Hutmacher DW, Russell PJ, Soekmadji C, Kundu SC. Engineered silk fibroin protein 3D matrices for in vitro tumor model. Biomaterials 2011;32(8):2149-59.
26. Sofia S, McCarthy MB, Gronowicz G, Kaplan DL. Functionalized silk-based biomaterials for bone formation. J Biomed Mater Res 2001;54(1):139-48.
27. Lu Q, Hu X, Wang X, Kluge J, Lu S, Cebe P, et al. Water-insoluble silk films with silk I structure. Acta Biomater 2010;6(4):1380-7.
28. Dong A, Huang P, Caughey WS. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 1990;29(13):3303-8.
29. Byler DM, Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 1986;25(3):469-87.
30. Hu X, Kaplan D, Cebe P. Determining beta-sheet crystallinity in fibrous proteins by thermal analysis and infrared spectroscopy. Macromolecules 2006;39(18):6161-70.
31. De Jongh HH, Goormaghtigh E, Ruysschaert JM. The different molar absorptivities of the secondary structure types in the amide I region: an attenuated total reflection infrared study on globular proteins. Anal Biochem 1996;242(1):95-103.
32. Turpeenniemi-Hujanen T. Gelatinases (MMP-2 and -9) and their natural inhibitors as prognostic indicators in solid cancers. Biochimie 2005;87(3-4):287-97.
33. Bello L, Lucini V, Carrabba G, Giussani C, Machluf M, Pluderi M, et al. Simultaneous inhibition of glioma angiogenesis, cell proliferation, and invasion by a naturally occurring fragment of human metalloproteinase-2. Cancer Res 2001;61:8730-6.
34. Inoue S, Tanaka K, Arisaka F, Kimura S, Ohtomo K, Mizuno S. Silk fibroin of Bombyx mori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6:6:1 molar ratio. J Biol Chem 2000;275(51):40517-28.
35. Wray LS, Hu X, Gallego J, Georgakoudi I, Omenetto FG, Schmidt D, et al. Effect of processing on silk-based biomaterials: reproducibility and biocompatibility. J Biomed Mater Res Part B 2011;99(1):89-101.
36. Saarinen J, Welgus HG, Flizar C, Kalkkinen N, Helin J. N-glycan structures of matrix metalloproteinase-1 derived from human fibroblasts and from HT-1080 fibrosarcoma cells. Eur J Biochem 1999;259(3):829-40.
37. Petibois C, Cazorla G, Cassaigne A, Déléris G. Plasma protein contents determined by Fourier-transform infrared spectrometry. Clin Chem 2001;47(4):730-8.
38. Petibois C, Gionnet K, Gonc¸alves M, Perromat A, Moenner M, Déléris G. Analytical performances of FT-IR spectrometry and imaging for concentration measurements within biological fluids, cells, and tissues. Analyst 2006;131(5):640-7.
39. Lee J-E, Park J-C, Hwang Y-S, Kim JK, Kim J-G, Suh H. Characterization of UV-irradiated dense/porous collagen membranes: morphology, enzymatic degradation, and mechanical properties. Yonsei Med J 2001;42(2):172-9.
40. Rault I, Frei V, Herbage D, Abdul-Malak N, Huc A. Evaluation of different chemical methods for cross-linking collagen gel, films and sponges. J Mater Sci Mater Med 1996;7(4):215-21.
41. Boon ME, Ruijgrok JM, Vardaxis MJ. Collagen implants remain supple not allowing fibroblast ingrowth. Biomaterials 1995;16(14):1089-93.
42. Jin H-J, Park J, Karageorgiou V, Kim U-J, Valluzzi R, Cebe P, et al. Water-stable silk films with reduced β-sheet content. Adv Funct Mater 2005;15(8):1241-7.
43. Kong J, Yu S. Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim Biophys Sin 2007;39(8):549-59.
44. Ebeling W, Hennrich N, Klockow M, Metz H, Orth HD, Lang H. Proteinase K from tritirachium album limber. Eur J Biochem 1974;47(1):91-7.
45. Sweeney PJ, Walker JM. Proteinase K. In: Burrell M, editor. Enzymes of molecular biology. Totowa, NJ: Humana Press; 1993. p. 305-11.
46. Bauer C-A. Active centers of Streptomyces griseus protease 1, Streptomyces griseus protease 3, and α-chymotrypsin: enzyme-substrate interactions. Am Chem Soc 1978;17(2):375-80.
47. Appel W. Chymotrypsin: molecular and catalytic properties. Clin Biochem 1986;19(6):317-22.
48. Yu AE, Murphy AN, Stetler-Stevenson WG. 72-kDa gelatinase (gelatinase A): structure, activation, regulation, and substrate specificity. In: Parks W, Mecham R, editors. Matrix metalloproteinases. New York: Academic Press; 1998. p. 85-113.
49. Pardo A, Selman M. MMP-1: the elder of the family. Int J Biochem Cell Biol 2005;37(2):283-8.
50. Fernandez-Patron C, Stewart KG, Zhang Y, Koivunen E, Radomski MW, Davidge ST. Vascular matrix metalloproteinase-2-dependent cleavage of calcitonin gene-related peptide Promotes Vasoconstriction. Circ Res 2000;87(8):670-6.