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Volumn 35, Issue 10, 2014, Pages 3427-3434

Deciphering the mechanism of protein interaction with silk fibroin for drug delivery systems

Author keywords

Drug delivery of biologics; Mechanism of interaction; Silk fibroin; Thermodynamics

Indexed keywords

DRUG DELIVERY CARRIER; DRUG DELIVERY SYSTEM; MODEL PROTEINS; NANOPARTICLE TRACKING ANALYSIS; PROTEIN INTERACTION; SILK FIBROIN; STATIC LIGHT SCATTERING; STRUCTURAL BREAKDOWN;

EID: 84893710225     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2013.12.083     Document Type: Article
Times cited : (30)

References (54)
  • 1
    • 79952987084 scopus 로고    scopus 로고
    • Silk fibroin as a vehicle for drug delivery applications
    • Wenk E., Merkle H.P., Meinel L. Silk fibroin as a vehicle for drug delivery applications. J Control Release 2011, 150:128-141.
    • (2011) J Control Release , vol.150 , pp. 128-141
    • Wenk, E.1    Merkle, H.P.2    Meinel, L.3
  • 3
    • 0033987939 scopus 로고    scopus 로고
    • Protein stability in controlled-release systems
    • Fu K., Klibanov A.M., Langer R. Protein stability in controlled-release systems. Nat Biotechnol 2000, 18:24-25.
    • (2000) Nat Biotechnol , vol.18 , pp. 24-25
    • Fu, K.1    Klibanov, A.M.2    Langer, R.3
  • 4
    • 34547432454 scopus 로고    scopus 로고
    • Control of in vitro tissue-engineered bone-like structures using human mesenchymal stem cells and porous silk scaffolds
    • Hofmann S., Hagenmueller H., Koch A.M., Mueller R., Vunjak-Novakovic G., Kaplan D.L., et al. Control of in vitro tissue-engineered bone-like structures using human mesenchymal stem cells and porous silk scaffolds. Biomaterials 2006, 28:1152-1162.
    • (2006) Biomaterials , vol.28 , pp. 1152-1162
    • Hofmann, S.1    Hagenmueller, H.2    Koch, A.M.3    Mueller, R.4    Vunjak-Novakovic, G.5    Kaplan, D.L.6
  • 6
    • 84865304712 scopus 로고    scopus 로고
    • Silk constructs for delivery of musculoskeletal therapeutics
    • Meinel L., Kaplan D.L. Silk constructs for delivery of musculoskeletal therapeutics. Adv Drug Deliv Rev 2012, 64:1111-1122.
    • (2012) Adv Drug Deliv Rev , vol.64 , pp. 1111-1122
    • Meinel, L.1    Kaplan, D.L.2
  • 8
    • 40649088814 scopus 로고    scopus 로고
    • Insulin-like growth factor I releasing silk fibroin scaffolds induce chondrogenic differentiation of human mesenchymal stem cells
    • Uebersax L., Merkle H.P., Meinel L. Insulin-like growth factor I releasing silk fibroin scaffolds induce chondrogenic differentiation of human mesenchymal stem cells. J Control Release 2008, 127:12-21.
    • (2008) J Control Release , vol.127 , pp. 12-21
    • Uebersax, L.1    Merkle, H.P.2    Meinel, L.3
  • 9
    • 54949157213 scopus 로고    scopus 로고
    • Silk fibroin spheres as a platform for controlled drug delivery
    • 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.
    • (2008) J Control Release , vol.132 , pp. 26-34
    • Wenk, E.1    Wandrey, A.J.2    Merkle, H.P.3    Meinel, L.4
  • 10
    • 79956207489 scopus 로고    scopus 로고
    • Silk fibroin biomaterials for controlled release drug delivery
    • Pritchard E.M., Kaplan D.L. Silk fibroin biomaterials for controlled release drug delivery. Expert Opin Drug Deliv 2011, 8:797-811.
    • (2011) Expert Opin Drug Deliv , vol.8 , pp. 797-811
    • Pritchard, E.M.1    Kaplan, D.L.2
  • 11
    • 84880947293 scopus 로고    scopus 로고
    • Mechanisms of monoclonal antibody stabilization and release from silk biomaterials
    • Guziewicz N.A., Massetti A.J., Perez-Ramirez B.J., Kaplan D.L. Mechanisms of monoclonal antibody stabilization and release from silk biomaterials. Biomaterials 2013, 34:7766-7775.
    • (2013) Biomaterials , vol.34 , pp. 7766-7775
    • Guziewicz, N.A.1    Massetti, A.J.2    Perez-Ramirez, B.J.3    Kaplan, D.L.4
  • 12
    • 84988044475 scopus 로고    scopus 로고
    • Spider silk: evolution and 400 million years of spinning, waiting, snagging, and mating
    • Vollrath F. Spider silk: evolution and 400 million years of spinning, waiting, snagging, and mating. Nature 2010, 466:319.
    • (2010) Nature , vol.466 , pp. 319
    • Vollrath, F.1
  • 13
    • 0035967162 scopus 로고    scopus 로고
    • Liquid crystalline spinning of spider silk
    • Vollrath F., Knight D.P. Liquid crystalline spinning of spider silk. Nature 2001, 410:541-548.
    • (2001) Nature , vol.410 , pp. 541-548
    • Vollrath, F.1    Knight, D.P.2
  • 14
    • 72149093757 scopus 로고    scopus 로고
    • The use of sulfonated silk fibroin derivatives to control binding, delivery and potency of FGF-2 in tissue regeneration
    • Wenk E., Murphy A.R., Kaplan D.L., Meinel L., Merkle H.P., Uebersax L. The use of sulfonated silk fibroin derivatives to control binding, delivery and potency of FGF-2 in tissue regeneration. Biomaterials 2010, 31:1403-1413.
    • (2010) Biomaterials , vol.31 , pp. 1403-1413
    • Wenk, E.1    Murphy, A.R.2    Kaplan, D.L.3    Meinel, L.4    Merkle, H.P.5    Uebersax, L.6
  • 16
    • 0000896026 scopus 로고
    • Characteristics of the structure of silk fibroins and its application to enzyme immobilization
    • Asakura T. Characteristics of the structure of silk fibroins and its application to enzyme immobilization. Bio Ind 1987, 4:878-886.
    • (1987) Bio Ind , vol.4 , pp. 878-886
    • Asakura, T.1
  • 18
    • 70349783566 scopus 로고    scopus 로고
    • Spider silk: from soluble protein to extraordinary fiber
    • Heim M., Keerl D., Scheibel T. Spider silk: from soluble protein to extraordinary fiber. Angew Chem Int Ed 2009, 48:3584-3596.
    • (2009) Angew Chem Int Ed , vol.48 , pp. 3584-3596
    • Heim, M.1    Keerl, D.2    Scheibel, T.3
  • 19
    • 23444450224 scopus 로고    scopus 로고
    • Protein fibers as performance proteins: new technologies and applications
    • Scheibel T. Protein fibers as performance proteins: new technologies and applications. Curr Opin Biotechnol 2005, 16:427-433.
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 427-433
    • Scheibel, T.1
  • 20
    • 44949167731 scopus 로고    scopus 로고
    • Silk fibroin protein from mulberry and non-mulberry silkworms: cytotoxicity, biocompatibility and kinetics of L929 murine fibroblast adhesion
    • Acharya C., Ghosh S.K., Kundu S.C. Silk fibroin protein from mulberry and non-mulberry silkworms: cytotoxicity, biocompatibility and kinetics of L929 murine fibroblast adhesion. J Mater Sci Mater Med 2008, 19:2827-2836.
    • (2008) J Mater Sci Mater Med , vol.19 , pp. 2827-2836
    • Acharya, C.1    Ghosh, S.K.2    Kundu, S.C.3
  • 22
    • 70349968105 scopus 로고    scopus 로고
    • Electrospinning of collagen/biopolymers for regenerative medicine and cardiovascular tissue engineering
    • Sell S.A., McClure M.J., Garg K., Wolfe P.S., Bowlin G.L. Electrospinning of collagen/biopolymers for regenerative medicine and cardiovascular tissue engineering. Adv Drug Deliv Rev 2009, 61:1007-1019.
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 1007-1019
    • Sell, S.A.1    McClure, M.J.2    Garg, K.3    Wolfe, P.S.4    Bowlin, G.L.5
  • 23
    • 33748975682 scopus 로고    scopus 로고
    • Stem cell-based tissue engineering with silk biomaterials
    • Wang Y., Kim H.-J., Vunjak-Novakovic G., Kaplan D.L. Stem cell-based tissue engineering with silk biomaterials. Biomaterials 2006, 27:6064-6082.
    • (2006) Biomaterials , vol.27 , pp. 6064-6082
    • Wang, Y.1    Kim, H.-J.2    Vunjak-Novakovic, G.3    Kaplan, D.L.4
  • 24
    • 8544278195 scopus 로고    scopus 로고
    • Bone morphogenetic protein-2 decorated silk fibroin films induce osteogenic differentiation of human bone marrow stromal cells
    • Karageorgiou V., Meinel L., Hofmann S., Malhotra A., Volloch V., Kaplan D. Bone morphogenetic protein-2 decorated silk fibroin films induce osteogenic differentiation of human bone marrow stromal cells. J Biomed Mater Res Part A 2004, 71A:528-537.
    • (2004) J Biomed Mater Res Part A , vol.71 A , pp. 528-537
    • Karageorgiou, V.1    Meinel, L.2    Hofmann, S.3    Malhotra, A.4    Volloch, V.5    Kaplan, D.6
  • 25
    • 79251593187 scopus 로고    scopus 로고
    • Lyophilized silk fibroin hydrogels for the sustained local delivery of therapeutic monoclonal antibodies
    • Guziewicz N., Best A., Perez-Ramirez B., Kaplan D.L. Lyophilized silk fibroin hydrogels for the sustained local delivery of therapeutic monoclonal antibodies. Biomaterials 2011, 32:2642-2650.
    • (2011) Biomaterials , vol.32 , pp. 2642-2650
    • Guziewicz, N.1    Best, A.2    Perez-Ramirez, B.3    Kaplan, D.L.4
  • 28
    • 0037120758 scopus 로고    scopus 로고
    • Effect of secondary structure on the potential of mean force for poly-l-lysine in the α-helix and β-sheet conformations
    • Grigsby J.J., Blanch H.W., Prausnitz J.M. Effect of secondary structure on the potential of mean force for poly-l-lysine in the α-helix and β-sheet conformations. Biophys Chem 2002, 99:107-116.
    • (2002) Biophys Chem , vol.99 , pp. 107-116
    • Grigsby, J.J.1    Blanch, H.W.2    Prausnitz, J.M.3
  • 29
    • 84862756371 scopus 로고    scopus 로고
    • Physicochemical characterization of complex drug substances: evaluation of structural similarities and differences of protamine sulfate from various sources
    • Awotwe-Otoo D., Agarabi C., Keire D., Lee S., Raw A., Yu L., et al. Physicochemical characterization of complex drug substances: evaluation of structural similarities and differences of protamine sulfate from various sources. AAPS J 2012, 14:619-626.
    • (2012) AAPS J , vol.14 , pp. 619-626
    • Awotwe-Otoo, D.1    Agarabi, C.2    Keire, D.3    Lee, S.4    Raw, A.5    Yu, L.6
  • 30
    • 8744301723 scopus 로고    scopus 로고
    • Engineering cartilage-like tissue using human mesenchymal stem cells and silk protein scaffolds
    • Meinel L., Hofmann S., Karageorgiou V., Zichner L., Langer R., Kaplan D., et al. Engineering cartilage-like tissue using human mesenchymal stem cells and silk protein scaffolds. Biotechnol Bioeng 2004, 88:379-391.
    • (2004) Biotechnol Bioeng , vol.88 , pp. 379-391
    • Meinel, L.1    Hofmann, S.2    Karageorgiou, V.3    Zichner, L.4    Langer, R.5    Kaplan, D.6
  • 32
    • 1942519360 scopus 로고    scopus 로고
    • The efficiency of different salts to screen charge interactions in proteins: a Hofmeister effectα
    • Perez-Jimenez R., Godoy-Ruiz R., Ibarra-Molero B., Sanchez-Ruiz J.M. The efficiency of different salts to screen charge interactions in proteins: a Hofmeister effectα. Biophys J 2004, 86:2414-2429.
    • (2004) Biophys J , vol.86 , pp. 2414-2429
    • Perez-Jimenez, R.1    Godoy-Ruiz, R.2    Ibarra-Molero, B.3    Sanchez-Ruiz, J.M.4
  • 33
    • 84872852374 scopus 로고    scopus 로고
    • Introductory lecture: interpreting and predicting Hofmeister salt ion and solute effects on biopolymer and model processes using the solute partitioning model
    • Record M.T., Guinn E., Pegram L., Capp M. Introductory lecture: interpreting and predicting Hofmeister salt ion and solute effects on biopolymer and model processes using the solute partitioning model. Faraday Discuss 2013, 160:9-44.
    • (2013) Faraday Discuss , vol.160 , pp. 9-44
    • Record, M.T.1    Guinn, E.2    Pegram, L.3    Capp, M.4
  • 34
    • 33751408436 scopus 로고    scopus 로고
    • Interactions between macromolecules and ions: the Hofmeister series
    • Zhang Y., Cremer P.S. Interactions between macromolecules and ions: the Hofmeister series. Curr Opin Chem Biol 2006, 10:658-663.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 658-663
    • Zhang, Y.1    Cremer, P.S.2
  • 35
  • 37
  • 38
    • 26944459231 scopus 로고    scopus 로고
    • Silk implants for the healing of critical size bone defects
    • Meinel L., Fajardo R., Hofmann S., Langer R., Chen J., Snyder B., et al. Silk implants for the healing of critical size bone defects. Bone 2005, 37:688-698.
    • (2005) Bone , vol.37 , pp. 688-698
    • Meinel, L.1    Fajardo, R.2    Hofmann, S.3    Langer, R.4    Chen, J.5    Snyder, B.6
  • 40
    • 0000778476 scopus 로고
    • Crystallisation-coacervation-flocculation
    • Elsevier, Amsterdam, H.R. Kruyt (Ed.)
    • Bungenberg de Jong H.G. Crystallisation-coacervation-flocculation. Colloid science 1949, 232-258. Elsevier, Amsterdam. H.R. Kruyt (Ed.).
    • (1949) Colloid science , pp. 232-258
    • Bungenberg de Jong, H.G.1
  • 41
    • 84875659123 scopus 로고    scopus 로고
    • Polyelectrolyte molecular weight and salt effects on the phase behavior and coacervation of aqueous solutions of poly(acrylic acid) sodium salt and poly(allylamine) hydrochloride
    • Chollakup R., Beck J.B., Dirnberger K., Tirrell M., Eisenbach C.D. Polyelectrolyte molecular weight and salt effects on the phase behavior and coacervation of aqueous solutions of poly(acrylic acid) sodium salt and poly(allylamine) hydrochloride. Macromolecules 2013, 46:2376-2390.
    • (2013) Macromolecules , vol.46 , pp. 2376-2390
    • Chollakup, R.1    Beck, J.B.2    Dirnberger, K.3    Tirrell, M.4    Eisenbach, C.D.5
  • 43
    • 84869069148 scopus 로고    scopus 로고
    • Thermodynamic characterization of polypeptide complex coacervation
    • Priftis D., Laugel N., Tirrell M. Thermodynamic characterization of polypeptide complex coacervation. Langmuir 2012, 28:15947-15957.
    • (2012) Langmuir , vol.28 , pp. 15947-15957
    • Priftis, D.1    Laugel, N.2    Tirrell, M.3
  • 44
    • 0346243607 scopus 로고    scopus 로고
    • Protein-polysaccharide interactions: phase-ordering kinetics, thermodynamic and structural aspects
    • Turgeon S.L., Beaulieu M., Schmitt C., Sanchez C. Protein-polysaccharide interactions: phase-ordering kinetics, thermodynamic and structural aspects. Curr Opin Colloid Interface Sci 2003, 8:401-414.
    • (2003) Curr Opin Colloid Interface Sci , vol.8 , pp. 401-414
    • Turgeon, S.L.1    Beaulieu, M.2    Schmitt, C.3    Sanchez, C.4
  • 45
    • 79957934865 scopus 로고    scopus 로고
    • Interactions of a cationic antimicrobial (ε-polylysine) with an anionic biopolymer (pectin): an isothermal titration calorimetry, microelectrophoresis, and turbidity study
    • Chang Y., McLandsborough L., McClements D.J. Interactions of a cationic antimicrobial (ε-polylysine) with an anionic biopolymer (pectin): an isothermal titration calorimetry, microelectrophoresis, and turbidity study. J Agric Food Chem 2011, 59:5579-5588.
    • (2011) J Agric Food Chem , vol.59 , pp. 5579-5588
    • Chang, Y.1    McLandsborough, L.2    McClements, D.J.3
  • 46
    • 0042364941 scopus 로고    scopus 로고
    • Mechanism of silk processing in insects and spiders
    • Jin H.-J., Kaplan D.L. Mechanism of silk processing in insects and spiders. Nature 2003, 424:1057-1061.
    • (2003) Nature , vol.424 , pp. 1057-1061
    • Jin, H.-J.1    Kaplan, D.L.2
  • 47
    • 25144460975 scopus 로고    scopus 로고
    • Analysis of protein-surfactant interactions-a titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant
    • Nielsen A.D., Arleth L., Westh P. Analysis of protein-surfactant interactions-a titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant. Biochim Biophys Acta-Proteins Proteomics 2005, 1752:124-132.
    • (2005) Biochim Biophys Acta-Proteins Proteomics , vol.1752 , pp. 124-132
    • Nielsen, A.D.1    Arleth, L.2    Westh, P.3
  • 48
    • 84893694005 scopus 로고    scopus 로고
    • U.S.Food and Drug Administration
    • FDA, Silver Spring, MD, Available from: URL:
    • U.S.Food and Drug Administration Generally recognized as safe (GRAS) - alphabetical list of SCOGS substances 2013, FDA, Silver Spring, MD, Available from: URL:. http://www.fda.gov/Food/IngredientsPackagingLabeling/GRAS/SCOGS/ucm084104.htm.
    • (2013) Generally recognized as safe (GRAS) - alphabetical list of SCOGS substances
  • 49
    • 34250832168 scopus 로고    scopus 로고
    • The amphiphilic properties of spider silks are important for spinning
    • Exler J.H., Huemmerich D., Scheibel T. The amphiphilic properties of spider silks are important for spinning. Angew Chem Int Ed 2007, 46:3559-3562.
    • (2007) Angew Chem Int Ed , vol.46 , pp. 3559-3562
    • Exler, J.H.1    Huemmerich, D.2    Scheibel, T.3
  • 50
    • 40449126548 scopus 로고    scopus 로고
    • Hydrophobic and Hofmeister effects on the adhesion of spider silk proteins onto solid substrates: an AFM-based single-molecule study
    • Geisler M., Pirzer T., Ackerschott C., Lud S., Garrido J., Scheibel T., et al. Hydrophobic and Hofmeister effects on the adhesion of spider silk proteins onto solid substrates: an AFM-based single-molecule study. Langmuir 2008, 24:1350-1355.
    • (2008) Langmuir , vol.24 , pp. 1350-1355
    • Geisler, M.1    Pirzer, T.2    Ackerschott, C.3    Lud, S.4    Garrido, J.5    Scheibel, T.6
  • 51
    • 77951974343 scopus 로고    scopus 로고
    • The role of salt and shear on the storage and assembly of spider silk proteins
    • Eisoldt L., Hardy J.G., Heim M., Scheibel T.R. The role of salt and shear on the storage and assembly of spider silk proteins. J Struct Biol 2010, 170:413-419.
    • (2010) J Struct Biol , vol.170 , pp. 413-419
    • Eisoldt, L.1    Hardy, J.G.2    Heim, M.3    Scheibel, T.R.4
  • 52
    • 0034978997 scopus 로고    scopus 로고
    • Changes in element composition along the spinning duct in a Nephila spider
    • Knight D.P., Vollrath F. Changes in element composition along the spinning duct in a Nephila spider. Naturwissenschaften 2001, 88:179-182.
    • (2001) Naturwissenschaften , vol.88 , pp. 179-182
    • Knight, D.P.1    Vollrath, F.2
  • 53
    • 0026923132 scopus 로고
    • Self-assembly in aqueous block copolymer solutions
    • Malmsten M., Lindman B. Self-assembly in aqueous block copolymer solutions. Macromolecules 1992, 25:5440-5445.
    • (1992) Macromolecules , vol.25 , pp. 5440-5445
    • Malmsten, M.1    Lindman, B.2
  • 54
    • 34248577169 scopus 로고    scopus 로고
    • Poly(ethylene oxide)-poly(propylene oxide) block copolymer micelles as drug delivery agents: improved hydrosolubility, stability and bioavailability of drugs
    • Chiappetta D.A., Sosnik A. Poly(ethylene oxide)-poly(propylene oxide) block copolymer micelles as drug delivery agents: improved hydrosolubility, stability and bioavailability of drugs. Eur J Pharm Biopharm 2007, 66:303-317.
    • (2007) Eur J Pharm Biopharm , vol.66 , pp. 303-317
    • Chiappetta, D.A.1    Sosnik, A.2


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