메뉴 건너뛰기




Volumn 1830, Issue 8, 2013, Pages 4030-4039

Rejoining of cut wounds by engineered gelatin-keratin glue

Author keywords

Caffeic acid; Gelatin; Incision wound; Keratin; Rheology; Tissue adhesive

Indexed keywords

1 (3 DIMETHYLAMINOPROPYL) 3 ETHYLCARBODIIMIDE; CAFFEIC ACID; CYANOACRYLATE; FIBRIN GLUE; GELATIN; KERATIN; PERIODATE; TISSUE ADHESIVE;

EID: 84877807318     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.04.009     Document Type: Article
Times cited : (31)

References (47)
  • 3
    • 0025499381 scopus 로고
    • In vitro toxicity test of 2-cyanoacrylate polymers by cell culture method
    • DOI 10.1002/jbm.820241007
    • Y.-C. Tseng, Y. Tabata, S.-H. Hyon, and Y. Ikada In vitro toxicity test of 2-cyanoacrylate polymers by cell culture method J. Biomed. Mater. Res. 24 1990 1355 1367 (Pubitemid 20293550)
    • (1990) Journal of Biomedical Materials Research , vol.24 , Issue.10 , pp. 1355-1367
    • Tseng, Y.-C.1    Tabata, Y.2    Hyon, S.-H.3    Ikada, Y.4
  • 5
    • 0003355894 scopus 로고
    • Chemical and physical characterization of barnacle cement
    • J.S. Otness, and D.G. Medcalf Chemical and physical characterization of barnacle cement Comp. Biochem. Physiol. B 43 1972 443 449
    • (1972) Comp. Biochem. Physiol. B , vol.43 , pp. 443-449
    • Otness, J.S.1    Medcalf, D.G.2
  • 6
    • 0033017306 scopus 로고    scopus 로고
    • Mussel byssus and biomolecular materials
    • DOI 10.1016/S1367-5931(99)80018-0
    • T.J. Deming Mussel byssus and biomolecular materials Curr. Opin. Chem. Biol. 3 1999 100 105 (Pubitemid 29118988)
    • (1999) Current Opinion in Chemical Biology , vol.3 , Issue.1 , pp. 100-105
    • Deming, T.J.1
  • 7
    • 78149416493 scopus 로고    scopus 로고
    • Biocompatibility of adhesive complex coacervates modeled after the sandcastle glue of Phragmatopoma californica for craniofacial reconstruction
    • B.D. Winslow, H. Shao, R.J. Stewart, and P.A. Tresco Biocompatibility of adhesive complex coacervates modeled after the sandcastle glue of Phragmatopoma californica for craniofacial reconstruction Biomaterials 31 2010 9373 9381
    • (2010) Biomaterials , vol.31 , pp. 9373-9381
    • Winslow, B.D.1    Shao, H.2    Stewart, R.J.3    Tresco, P.A.4
  • 10
    • 35148886304 scopus 로고    scopus 로고
    • Tissue glues and nonsuturing techniques
    • N.F. Pursifull, and A.F. Morey Tissue glues and nonsuturing techniques Curr. Opin. Urol. 17 2007 396
    • (2007) Curr. Opin. Urol. , vol.17 , pp. 396
    • Pursifull, N.F.1    Morey, A.F.2
  • 11
    • 0037196121 scopus 로고    scopus 로고
    • Free radical scavenging and antioxidative activity of caffeic acid amide and ester analogues: Structure-activity relationship
    • DOI 10.1021/jf010830b
    • S. Son, and B.A. Lewis Free radical scavenging and antioxidative activity of caffeic acid amide and ester analogues: structure-activity relationship J. Agric. Food Chem. 50 2002 468 472 (Pubitemid 34106663)
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , Issue.3 , pp. 468-472
    • Son, S.1    Lewis, B.A.2
  • 12
    • 34347351367 scopus 로고    scopus 로고
    • Free radical scavenging and antioxidative activities of caffeic acid phenethyl ester (CAPE) and its related compounds in solution and membranes: A structure-activity insight
    • DOI 10.1016/j.foodchem.2007.03.049, PII S030881460700297X
    • W.M. Wu, L. Lu, Y. Long, T. Wang, L. Liu, Q. Chen, and R. Wang Free radical scavenging and antioxidative activities of caffeic acid phenethyl ester (CAPE) and its related compounds in solution and membranes: a structure activity insight Food Chem. 105 2007 107 115 (Pubitemid 47016817)
    • (2007) Food Chemistry , vol.105 , Issue.1 , pp. 107-115
    • Wu, W.-M.1    Lu, L.2    Long, Y.3    Wang, T.4    Liu, L.5    Chen, Q.6    Wang, R.7
  • 13
    • 7744221596 scopus 로고    scopus 로고
    • Novel and therapeutic effect of caffeic acid and caffeic acid phenyl ester on hepatocarcinoma cells: Complete regression of hepatoma growth and metastasis by dual mechanism
    • DOI 10.1096/fj.04-2126com
    • T.W. Chung, S.K. Moon, Y.C. Chang, J.H. Ko, Y.C. Lee, G. Cho, S.H. Kim, J.G. Kim, and C.H. Kim Novel and therapeutic effect of caffeic acid and caffeic acid phenyl ester on hepatocarcinoma cells: complete regression of hepatoma growth and metastasis by dual mechanism FASEB J. 18 2004 1670 1681 (Pubitemid 39463706)
    • (2004) FASEB Journal , vol.18 , Issue.14 , pp. 1670-1681
    • Chung, T.-W.1    Moon, S.-K.2    Chang, Y.-C.3    Ko, J.-H.4    Lee, Y.-C.5    Cho, G.6    Kim, S.-H.7    Kim, J.-G.8    Kim, C.-H.9
  • 14
    • 0028939986 scopus 로고
    • Mussel adhesive plaque protein gene is a novel member of epidermal growth factor-like gene family
    • K. Inoue, Y. Takeuchi, D. Miki, and S. Odo Mussel adhesive plaque protein gene is a novel member of epidermal growth factor-like gene family J. Biol. Chem. 270 1995 6698 6701
    • (1995) J. Biol. Chem. , vol.270 , pp. 6698-6701
    • Inoue, K.1    Takeuchi, Y.2    Miki, D.3    Odo, S.4
  • 15
    • 70350208796 scopus 로고    scopus 로고
    • Films based on human hair keratin as substrates for cell culture and tissue engineering
    • S. Reichl Films based on human hair keratin as substrates for cell culture and tissue engineering Biomaterials 30 2009 6854 6866
    • (2009) Biomaterials , vol.30 , pp. 6854-6866
    • Reichl, S.1
  • 16
    • 1642389170 scopus 로고    scopus 로고
    • Novel approach to fabricate keratin sponge scaffolds with controlled pore size and porosity
    • DOI 10.1016/j.biomaterials.2003.11.018, PII S0142961203010846
    • K. Katoh, T. Tanabe, and K. Yamauchi Novel approach to fabricate keratin sponge scaffolds with controlled pore size and porosity Biomaterials 25 2004 4255 4262 (Pubitemid 38388586)
    • (2004) Biomaterials , vol.25 , Issue.18 , pp. 4255-4262
    • Katoh, K.1    Tanabe, T.2    Yamauchi, K.3
  • 17
    • 35348929350 scopus 로고    scopus 로고
    • The use of keratin biomaterials derived from human hair for the promotion of rapid regeneration of peripheral nerves
    • DOI 10.1016/j.biomaterials.2007.08.023, PII S0142961207006643
    • P. Sierpinski, J. Garrett, J. Ma, P. Apel, D. Klorig, T. Smith, L.A. Koman, A. Atala, and M. Van Dyke The use of keratin biomaterials derived from human hair for the promotion of rapid regeneration of peripheral nerves Biomaterials 29 2008 118 128 (Pubitemid 47599650)
    • (2008) Biomaterials , vol.29 , Issue.1 , pp. 118-128
    • Sierpinski, P.1    Garrett, J.2    Ma, J.3    Apel, P.4    Klorig, D.5    Smith, T.6    Koman, L.A.7    Atala, A.8    Van Dyke, M.9
  • 18
    • 57349116158 scopus 로고    scopus 로고
    • Effect of keratin-gelatin and bFGF-gelatin composite film as a sandwich layer for full-thickness skin mesh graft in experimental dogs
    • S. Thilagar, N.A. Jothi, A.R.S. Omar, M.Y. Kamaruddin, and S. Ganabadi Effect of keratin-gelatin and bFGF-gelatin composite film as a sandwich layer for full-thickness skin mesh graft in experimental dogs J. Biomed. Mater. Res. B 88B 2009 12 16
    • (2009) J. Biomed. Mater. Res. B , vol.88 B , pp. 12-16
    • Thilagar, S.1    Jothi, N.A.2    Omar, A.R.S.3    Kamaruddin, M.Y.4    Ganabadi, S.5
  • 19
    • 80052888794 scopus 로고    scopus 로고
    • Preparation and characterization of hair keratin/gelatin blend films
    • S. Prasong, and T. Wasan Preparation and characterization of hair keratin/gelatin blend films Pak. J. Biol. Sci. 14 2011 351 356
    • (2011) Pak. J. Biol. Sci. , vol.14 , pp. 351-356
    • Prasong, S.1    Wasan, T.2
  • 20
    • 77953241457 scopus 로고    scopus 로고
    • Amine coupling through EDC/NHS: A practical approach
    • M.J.E. Fischer Amine coupling through EDC/NHS: a practical approach Methods Mol. Biol. 627 2010 55 73
    • (2010) Methods Mol. Biol. , vol.627 , pp. 55-73
    • Fischer, M.J.E.1
  • 21
    • 0036581543 scopus 로고    scopus 로고
    • A rapid extraction procedure of human hair proteins and identification of phosphorylated species
    • DOI 10.1248/bpb.25.569
    • A. Nakamura, M. Arimoto, K. Takeuchi, and T. Fujii A rapid extraction procedure of human hair proteins and identification of phosphorylated species Biol. Pharm. Bull. 25 2002 569 572 (Pubitemid 39663250)
    • (2002) Biological and Pharmaceutical Bulletin , vol.25 , Issue.5 , pp. 569-572
    • Nakamura, A.1    Arimoto, M.2    Takeuchi, K.3    Fujii, T.4
  • 22
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • J. Adler-Nissen Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid J. Agric. Food Chem. 27 1979 1256 1262
    • (1979) J. Agric. Food Chem. , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 23
    • 61549096567 scopus 로고    scopus 로고
    • Silk fibroin/polyacrylamide semi-interpenetrating network hydrogels for controlled drug release
    • B.B. Mandal, S. Kapoor, and S.C. Kundu Silk fibroin/polyacrylamide semi-interpenetrating network hydrogels for controlled drug release Biomaterials 30 2009 2826 2836
    • (2009) Biomaterials , vol.30 , pp. 2826-2836
    • Mandal, B.B.1    Kapoor, S.2    Kundu, S.C.3
  • 25
    • 29244439335 scopus 로고    scopus 로고
    • Fast-gelling injectable blend of hyaluronan and methylcellulose for intrathecal, localized delivery to the injured spinal cord
    • DOI 10.1016/j.biomaterials.2005.11.015, PII S0142961205010410
    • D. Gupta, C.H. Tator, and M.S. Shoichet Fast-gelling injectable blend of hyaluronan and methylcellulose for intrathecal, localized delivery to the injured spinal cord Biomaterials 27 2006 2370 2379 (Pubitemid 41821815)
    • (2006) Biomaterials , vol.27 , Issue.11 , pp. 2370-2379
    • Gupta, D.1    Tator, C.H.2    Shoichet, M.S.3
  • 26
    • 0034641671 scopus 로고    scopus 로고
    • Cross-linking in adhesive quinoproteins: Studies with model decapeptides
    • L.A. Burzio, and J.H. Waite Cross-linking in adhesive quinoproteins: studies with model decapeptides Biochemistry 39 2000 11147 11153
    • (2000) Biochemistry , vol.39 , pp. 11147-11153
    • Burzio, L.A.1    Waite, J.H.2
  • 27
    • 0037841311 scopus 로고    scopus 로고
    • Effect of oxidation rate on cross-linking of mussel adhesive proteins
    • DOI 10.1021/bm025707n
    • S. Haemers, G.J.M. Koper, and G. Frens Effect of oxidation rate on cross-linking of mussel adhesive proteins Biomacromolecules 4 2003 632 640 (Pubitemid 36701233)
    • (2003) Biomacromolecules , vol.4 , Issue.3 , pp. 632-640
    • Haemers, S.1    Koper, G.J.M.2    Frens, G.3
  • 28
    • 2342517486 scopus 로고    scopus 로고
    • Cross-linking the protein precursor of marine mussel adhesives: Bulk measurements and reagents for curing
    • J. Monahan, and J.J. Wilker Cross-linking the protein precursor of marine mussel adhesives: bulk measurements and reagents for curing Langmuir 20 2004 3724 3729
    • (2004) Langmuir , vol.20 , pp. 3724-3729
    • Monahan, J.1    Wilker, J.J.2
  • 30
    • 8444230519 scopus 로고    scopus 로고
    • Glutaraldehyde: Behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking
    • I. Migneault, C. Dartiguenave, M.J. Bertrand, and K.C. Waldron Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking Biotechniques 37 2004 790 806
    • (2004) Biotechniques , vol.37 , pp. 790-806
    • Migneault, I.1    Dartiguenave, C.2    Bertrand, M.J.3    Waldron, K.C.4
  • 31
    • 4143088311 scopus 로고    scopus 로고
    • Mechanical properties of biomimetic tissue adhesive based on the microbial transglutaminase-catalyzed crosslinking of gelatin
    • DOI 10.1021/bm034529a
    • M.K. McDermott, T. Chen, C.M. Williams, K.M. Markley, and G.F. Payne Mechanical properties of biomimetic tissue adhesive based on the microbial transglutaminase-catalyzed crosslinking of gelatin Biomacromolecules 5 2004 1270 1279 (Pubitemid 39089726)
    • (2004) Biomacromolecules , vol.5 , Issue.4 , pp. 1270-1279
    • McDermott, M.K.1    Chen, T.2    Williams, C.M.3    Markley, K.M.4    Payne, G.F.5
  • 34
    • 0344013443 scopus 로고    scopus 로고
    • Plant phenolics as cross-linkers of gelatin gels and gelatin-based coacervates for use as food ingredients
    • G. Strauss, and S.M. Gibson Plant phenolics as cross-linkers of gelatin gels and gelatin-based coacervates for use as food ingredients Food Hydrocolloids 18 2004 81 89
    • (2004) Food Hydrocolloids , vol.18 , pp. 81-89
    • Strauss, G.1    Gibson, S.M.2
  • 37
    • 84984085461 scopus 로고
    • Circular dichroism of the random polypeptide chain
    • M.L. Tiffany, and S. Krimm Circular dichroism of the random polypeptide chain Biopolymers 8 1969 347 359
    • (1969) Biopolymers , vol.8 , pp. 347-359
    • Tiffany, M.L.1    Krimm, S.2
  • 38
    • 0025343528 scopus 로고
    • Synthetic fragments and analogues of elastin. II. Conformational studies
    • A.M. Tamburro, V. Guantieri, L. Pandolfo, and A. Scopa Synthetic fragments and analogues of elastin. II. Conformational studies Biopolymers 29 1990 855 870 (Pubitemid 20140817)
    • (1990) Biopolymers , vol.29 , Issue.4-5 , pp. 855-870
    • Tamburro, A.M.1    Guantieri, V.2    Pandolfo, L.3    Scopa, A.4
  • 39
    • 59849108384 scopus 로고    scopus 로고
    • Structural transition during thermal denaturation of collagen in the solution and film states
    • G. Shanmugam, and P.L. Polavarapu Structural transition during thermal denaturation of collagen in the solution and film states Chirality 21 2009 152 159
    • (2009) Chirality , vol.21 , pp. 152-159
    • Shanmugam, G.1    Polavarapu, P.L.2
  • 40
    • 0002251831 scopus 로고
    • Circular dichroism and conformation of unordered polypeptides
    • R.W. Woody Circular dichroism and conformation of unordered polypeptides Adv. Biophys. Chem. 2 1992 37 79
    • (1992) Adv. Biophys. Chem. , vol.2 , pp. 37-79
    • Woody, R.W.1
  • 41
    • 36849156983 scopus 로고
    • Sensitivity of circular dichroism to protein tertiary structure class
    • P. Manavalan, and W.C. Johnson Sensitivity of circular dichroism to protein tertiary structure class Nature 305 1983 831 832
    • (1983) Nature , vol.305 , pp. 831-832
    • Manavalan, P.1    Johnson, W.C.2
  • 44
    • 24344476349 scopus 로고    scopus 로고
    • Enzymatically cross linked hydrogels and their adhesive strength to biosurfaces
    • B.H. Hu, and P.B. Messersmith Enzymatically cross linked hydrogels and their adhesive strength to biosurfaces Orthod. Craniofac. Res. 8 2005 145 149
    • (2005) Orthod. Craniofac. Res. , vol.8 , pp. 145-149
    • Hu, B.H.1    Messersmith, P.B.2
  • 46
    • 0032890526 scopus 로고    scopus 로고
    • Activities of plant-derived phenols in a fibroblast cell culture model
    • DOI 10.1021/np9801559
    • M.M. Koganov, O.V. Dueva, and B.L. Tsorin Activities of plant-derived phenols in a fibroblast cell culture model J. Nat. Prod. 62 1999 481 483 (Pubitemid 29165229)
    • (1999) Journal of Natural Products , vol.62 , Issue.3 , pp. 481-483
    • Koganov, M.M.1    Dueva, O.V.2    Tsorin, B.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.