메뉴 건너뛰기




Volumn 8, Issue 11, 2012, Pages 4101-4110

Bioengineered surfaces to improve the blood compatibility of biomaterials through direct thrombin inactivation

Author keywords

Coagulation; Hemocompatibility; Protein adsorption; Surface functionalization; Thrombin

Indexed keywords

ADSORPTION; BIOMEDICAL EQUIPMENT; BLOOD; COAGULATION; DESORPTION; MASS SPECTROMETRY; RECOMBINANT PROTEINS; SELF ASSEMBLED MONOLAYERS;

EID: 84873959808     PISSN: 17427061     EISSN: 18787568     Source Type: Journal    
DOI: 10.1016/j.actbio.2012.07.020     Document Type: Article
Times cited : (21)

References (55)
  • 2
    • 2442501409 scopus 로고    scopus 로고
    • Biomaterial-Associated thrombosis: Roles of coagulation factors, complement, platelets and leukocytes
    • DOI 10.1016/j.biomaterials.2004.01.023, PII S0142961204000687
    • Gorbet MB, Sefton MV. Biomaterial-Associated thrombosis: roles of coagulation factors, complement, platelets and leukocytes. Biomaterials 2004;25:5681-703. (Pubitemid 38624449)
    • (2004) Biomaterials , vol.25 , Issue.26 , pp. 5681-5703
    • Gorbet, M.B.1    Sefton, M.V.2
  • 3
    • 79960501436 scopus 로고    scopus 로고
    • Nonthrombogenic approaches to cardiovascular bioengineering
    • Li S, Henry JJD. Nonthrombogenic approaches to cardiovascular bioengineering. Annu Rev Biomed Eng 2011;13:451-75.
    • (2011) Annu Rev Biomed Eng , vol.13 , pp. 451-475
    • Li, S.1    Henry, J.J.D.2
  • 4
    • 33645353328 scopus 로고    scopus 로고
    • Structure and interaction modes of thrombin
    • Bode W. Structure and interaction modes of thrombin. Blood Cells Mol Dis 2006;36:122-30.
    • (2006) Blood Cells Mol Dis , vol.36 , pp. 122-130
    • Bode, W.1
  • 5
    • 26444440564 scopus 로고    scopus 로고
    • Two-way interactions between inflammation and coagulation
    • DOI 10.1016/j.tcm.2005.07.004, PII S1050173805001234
    • Levi M, van derPoll T. Two-way interactions between inflammation and coagulation. Trends Cardiovasc Med 2005;15:254-9. (Pubitemid 41437908)
    • (2005) Trends in Cardiovascular Medicine , vol.15 , Issue.7 , pp. 254-259
    • Levi, M.1    Van Der Poll, T.2
  • 7
    • 0033199710 scopus 로고    scopus 로고
    • Coating-techniques to improve the hemocompatibility of artificial devices used for extracorporeal circulation
    • DOI 10.1016/S1010-7940(99)00210-9, PII S1010794099002109
    • Wendel HP, Ziemer G. Coating-techniques to improve the hemocompatibility of artificial devices used for extracorporeal circulation. Eur J Cardiothorac Surg 1999;16:342-50. (Pubitemid 29443972)
    • (1999) European Journal of Cardio-thoracic Surgery , vol.16 , Issue.3 , pp. 342-350
    • Wendel, H.P.1    Ziemer, G.2
  • 9
    • 34547741083 scopus 로고    scopus 로고
    • Current strategies towards hemocompatible coatings
    • DOI 10.1039/b703416b
    • Werner C, Maitz MF, Sperling C. Current strategies towards hemocompatible coatings. J Mater Chem 2007;17:3376-84. (Pubitemid 47231013)
    • (2007) Journal of Materials Chemistry , vol.17 , Issue.32 , pp. 3376-3384
    • Werner, C.1    Maitz, M.F.2    Sperling, C.3
  • 10
    • 62649146066 scopus 로고    scopus 로고
    • A systematic review of biocompatible cardiopulmonary bypass circuits and clinical outcome
    • Ranucci M, Balduini A, Ditta A, Boncilli A, Brozzi S. A systematic review of biocompatible cardiopulmonary bypass circuits and clinical outcome. Ann Thorac Surg 2009;87:1311-9.
    • (2009) Ann Thorac Surg , vol.87 , pp. 1311-1319
    • Ranucci, M.1    Balduini, A.2    Ditta, A.3    Boncilli, A.4    Brozzi, S.5
  • 11
    • 0036588770 scopus 로고    scopus 로고
    • Direct thrombin inhibitors
    • DOI 10.1016/S0049-3848(02)00093-2, PII S0049384802000932
    • Weitz JI, Crowther M. Direct thrombin inhibitors. Thromb Res 2002;106:V275-84. (Pubitemid 35279149)
    • (2002) Thrombosis Research , vol.106 , Issue.3
    • Weitz, J.I.1    Crowther, M.2
  • 13
    • 0031149316 scopus 로고    scopus 로고
    • Covalent linkage of recombinant hirudin to poly(ethylene terephthalate) (Dacron): Creation of a novel antithrombin surface
    • DOI 10.1016/S0142-9612(96)00193-7, PII S0142961296001937
    • Phaneuf MD, Berceli SA, Bide MJ, Quist WC, LoGerfo FW. Covalent linkage of recombinant hirudin to poly(ethylene terephthalate) (Dacron): creation of a novel antithrombin surface. Biomaterials 1997;18:755-65. (Pubitemid 27197482)
    • (1997) Biomaterials , vol.18 , Issue.10 , pp. 755-765
    • Phaneuf, M.D.1    Berceli, S.A.2    Bide, M.J.3    Quist, W.C.4    LoGerfo, F.W.5
  • 14
    • 0031282113 scopus 로고    scopus 로고
    • Covalent immobilization of hirudin improves the haemocompatibility of polylactide-polyglycolide in vitro
    • DOI 10.1016/S0142-9612(97)00079-3, PII S0142961297000793
    • Seifert B, Romaniuk P, Groth T. Covalent immobilization of hirudin improves the haemocompatibility of polylactide-polyglycolide in vitro. Biomaterials 1997;18:1495-502. (Pubitemid 27496638)
    • (1997) Biomaterials , vol.18 , Issue.22 , pp. 1495-1502
    • Seifert, B.1    Romaniuk, P.2    Groth, Th.3
  • 15
    • 0031852871 scopus 로고    scopus 로고
    • Covalent linkage of recombinant hirudin to a novel ionic poly(carbonate) urethane polymer with protein binding sites: Determination of surface antithrombin activity
    • DOI 10.1046/j.1525-1594.1998.05091.x
    • Phaneuf MD, Szycher M, Berceli SA, Dempsey DJ, Quist WC, LoGerfo FW. Covalent linkage of recombinant hirudin to a novel ionic poly(carbonate) urethane polymer with protein binding sites: determination of surface antithrombin activity. Artif Organs 1998;22:657-65. (Pubitemid 28357927)
    • (1998) Artificial Organs , vol.22 , Issue.8 , pp. 657-665
    • Phaneuf, M.D.1    Szycher, M.2    Berceli, S.A.3    Dempsey, D.J.4    Quist, W.C.5    LoGerfo, F.W.6
  • 16
    • 0031811070 scopus 로고    scopus 로고
    • Evaluation of a novel hirudin-coated polyester graft to physiologic flow conditions: Hirudin bioavailability and thrombin uptake
    • DOI 10.1016/S0741-5214(98)70014-X
    • Berceli SA, Phaneuf MD, LoGerfo FW, Patterson RB. Evaluation of a novel hirudin-coated polyester graft to physiologic flow conditions: hirudin bioavailability and thrombin uptake. J Vasc Surg 1998;27:1117-27. (Pubitemid 28289900)
    • (1998) Journal of Vascular Surgery , vol.27 , Issue.6 , pp. 1117-1127
    • Berceli, S.A.1    Phaneuf, M.D.2    LoGerfo, F.W.3    Patterson, R.B.4
  • 17
    • 0033042998 scopus 로고    scopus 로고
    • In vivo assessment of a novel Dacron surface with covalently bound recombinant hirudin
    • DOI 10.1016/S1054-8807(99)00005-8, PII S1054880799000058
    • Wyers MC, Phaneuf MD, Rzucidlo EM, Contreras MA, Logerfo FW, Quist WC. In vivo assessment of a novel Dacron surface with covalently bound recombinant hirudin. Cardiovasc Pathol 1999;8:153-9. (Pubitemid 29290830)
    • (1999) Cardiovascular Pathology , vol.8 , Issue.3 , pp. 153-159
    • Wyers, M.C.1    Phaneuf, M.D.2    Rzucidlo, E.M.3    Contreras, M.A.4    Logerfo, F.W.5    Quist, W.C.6
  • 19
    • 0034781883 scopus 로고    scopus 로고
    • Surface characterization and platelet adhesion studies on polyethylene surface with hirudin immobilization
    • Lin JC, Tseng SM. Surface characterization and platelet adhesion studies on polyethylene surface with hirudin immobilization. J Mater Sci Mater Med 2001;12:827-32.
    • (2001) J Mater Sci Mater Med , vol.12 , pp. 827-832
    • Lin, J.C.1    Tseng, S.M.2
  • 20
    • 77956650277 scopus 로고    scopus 로고
    • Surface modification with PEG and hirudin for protein resistance and thrombin neutralization in blood contact
    • Alibeik S, Zhu S, Brash JL. Surface modification with PEG and hirudin for protein resistance and thrombin neutralization in blood contact. Colloids Surf B Biointerfaces 2010;81:389-96.
    • (2010) Colloids Surf B Biointerfaces , vol.81 , pp. 389-396
    • Alibeik, S.1    Zhu, S.2    Brash, J.L.3
  • 21
    • 0025346345 scopus 로고
    • Design and characterization of hirulogs: A novel class of bivalent peptide inhibitors of thrombin
    • DOI 10.1021/bi00482a021
    • Maraganore JM, Bourdon P, Jablonski J, Ramachandran KL, Fenton Ii JW. Design and characterization of hirulogs: A novel class of bivalent peptide inhibitors of thrombin. Biochemistry 1990;29:7095-101. (Pubitemid 20241158)
    • (1990) Biochemistry , vol.29 , Issue.30 , pp. 7095-7101
    • Maraganore, J.M.1    Bourdon, P.2    Jablonski, J.3    Ramachandran, K.L.4    Fenton II, J.W.5
  • 22
    • 0033990761 scopus 로고    scopus 로고
    • Peptide modified gold-coated polyurethanes as thrombin scavenging surfaces
    • Sun X, Sheardown H, Tengvall P, Brash JL. Peptide modified gold-coated polyurethanes as thrombin scavenging surfaces. J Biomed Mater Res 2000;49:66-78.
    • (2000) J Biomed Mater Res , vol.49 , pp. 66-78
    • Sun, X.1    Sheardown, H.2    Tengvall, P.3    Brash, J.L.4
  • 23
    • 77649271932 scopus 로고    scopus 로고
    • The effect of immobilization of thrombin inhibitors onto self-Assembled monolayers on the adsorption and activity of thrombin
    • Freitas SC, Barbosa MA, Martins MCL. The effect of immobilization of thrombin inhibitors onto self-Assembled monolayers on the adsorption and activity of thrombin. Biomaterials 2010;31:3772-80.
    • (2010) Biomaterials , vol.31 , pp. 3772-3780
    • Freitas, S.C.1    Barbosa, M.A.2    Martins, M.C.L.3
  • 24
    • 45849130590 scopus 로고    scopus 로고
    • Isolation, cloning and structural characterisation of boophilin, a multifunctional Kunitz-type proteinase inhibitor from the cattle tick
    • Macedo-Ribeiro S, Almeida C, Calisto BM, Friedrich T, Mentele R, Stürzebecher J, et al. Isolation, cloning and structural characterisation of boophilin, a multifunctional Kunitz-type proteinase inhibitor from the cattle tick. PLoS One 2008;3:e1624.
    • (2008) PLoS One , vol.3
    • Macedo-Ribeiro, S.1    Almeida, C.2    Calisto, B.M.3    Friedrich, T.4    Mentele, R.5    Stürzebecher, J.6
  • 25
    • 84862486593 scopus 로고    scopus 로고
    • Expression and functional characterization of boophilin, a thrombin inhibitor from Rhipicephalus (Boophilus) microplus midgut
    • Soares TS, Watanabe RMO, Tanaka-Azevedo AM, Torquato RJS, Lu S, Figueiredo AC, et al. Expression and functional characterization of boophilin, a thrombin inhibitor from Rhipicephalus (Boophilus) microplus midgut. Vet Parasitol 2012;187:521-8.
    • (2012) Vet Parasitol , vol.187 , pp. 521-528
    • Soares, T.S.1    Watanabe, R.M.O.2    Tanaka-Azevedo, A.M.3    Torquato, R.J.S.4    Lu, S.5    Figueiredo, A.C.6
  • 26
    • 1942481178 scopus 로고
    • Formation of monolayer films by the spontaneous assembly of organic thiols from solution onto gold
    • Bain CD, Troughton EB, Tao YT, Evall J, Whitesides GM, Nuzzo RG. Formation of monolayer films by the spontaneous assembly of organic thiols from solution onto gold. J Am Chem Soc 1989;111:321-35.
    • (1989) J Am Chem Soc , vol.111 , pp. 321-335
    • Bain, C.D.1    Troughton, E.B.2    Tao, Y.T.3    Evall, J.4    Whitesides, G.M.5    Nuzzo, R.G.6
  • 27
    • 0344629191 scopus 로고    scopus 로고
    • Albumin adsorption on Cibacron Blue F3G-A immobilized onto oligo(ethylene glycol)-terminated self-Assembled monolayers
    • DOI 10.1023/A:1026394431100
    • Martins MCL, Naeemi E, Ratner BD, Barbosa MA. Albumin adsorption on Cibacron Blue F3G-A immobilized onto oligo(ethylene glycol)-terminated selfassembled monolayers. J Mater Sci Mater Med 2003;14:945-54. (Pubitemid 37500248)
    • (2003) Journal of Materials Science: Materials in Medicine , vol.14 , Issue.11 , pp. 945-954
    • Martins, Ma.C.L.1    Naeemi, E.2    Ratner, B.D.3    Barbosa, M.A.4
  • 28
  • 29
    • 0043210642 scopus 로고    scopus 로고
    • Factors that determine the protein resistance of oligoether self-Assembled monolayers - Internal hydrophilicity, terminal hydrophilicity, and lateral packing density
    • DOI 10.1021/ja034820y
    • Herrwerth S, Eck W, Reinhardt S, Grunze M. Factors that determine the protein resistance of oligoether self-Assembled monolayers-internal hydrophilicity, terminal hydrophilicity, and lateral packing density. J Am Chem Soc 2003;125:9359-66. (Pubitemid 36936053)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.31 , pp. 9359-9366
    • Herrwerth, S.1    Eck, W.2    Reinhardt, S.3    Grunze, M.4
  • 30
    • 0025286440 scopus 로고
    • Biotin-binding proteins: Overview and prospects
    • DOI 10.1016/0076-6879(90)84258-I
    • Bayer EA, Wilchek M, Meir W, Edward AB. Biotin-binding proteins: overview and prospects. Methods Enzymol 1990;184:49-51. (Pubitemid 20219730)
    • (1990) Methods in Enzymology , vol.184 , pp. 49-51
    • Bayer, E.A.1    Wilchek, M.2
  • 32
    • 0036808537 scopus 로고    scopus 로고
    • FindPept, a tool to identify unmatched masses in peptide mass fingerprinting protein identification
    • DOI 10.1002/1615-9861(200210)2 :10<1435::AID-PROT1435>3.0.CO;2-9
    • Gattiker A, Bienvenut WV, Bairoch A, Gasteiger E. FindPept, a tool to identify unmatched masses in peptide mass fingerprinting protein identification. Proteomics 2002;2:1435-44. (Pubitemid 35340024)
    • (2002) Proteomics , vol.2 , Issue.10 , pp. 1435-1444
    • Gattiker, A.1    Bienvenut, W.V.2    Bairoch, A.3    Gasteiger, E.4
  • 33
    • 85030498807 scopus 로고
    • Iodine-125 A guide to radioiodination techniques
    • Iodine-125. A guide to radioiodination techniques. Little Chalfont: Amersham Life Science, 1993.
    • (1993) Little Chalfont: Amersham Life Science
  • 35
    • 68549112719 scopus 로고    scopus 로고
    • Protein adsorption and clotting time of pHEMA hydrogels modified with C18 ligands to adsorb albumin selectively and reversibly
    • Gonçalves IC, Martins MCL, Barbosa MA, Ratner BD. Protein adsorption and clotting time of pHEMA hydrogels modified with C18 ligands to adsorb albumin selectively and reversibly. Biomaterials 2009;30:5541-51.
    • (2009) Biomaterials , vol.30 , pp. 5541-5551
    • Gonçalves, I.C.1    Martins, M.C.L.2    Barbosa, M.A.3    Ratner, B.D.4
  • 36
    • 0035448605 scopus 로고    scopus 로고
    • A simple and rapid laboratory method for determination of haemostasis potential in plasma: II. Modifications for use in routine laboratories and research work
    • DOI 10.1016/S0049-3848(01)00332-2, PII S0049384801003322
    • He S, Antovic A, Blombäck M. A simple and rapid laboratory method for determination of haemostasis potential in plasma: II. Modifications for use in routine laboratories and research work. Thromb Res 2001;103:355-61. (Pubitemid 32831470)
    • (2001) Thrombosis Research , vol.103 , Issue.5 , pp. 355-361
    • He, S.1    Antovic, A.2    Blomback, M.3
  • 37
    • 72149091729 scopus 로고    scopus 로고
    • A turbidimetric assay for the measurement of clotting times of procoagulant venoms in plasma
    • O'Leary MA, Isbister GK. A turbidimetric assay for the measurement of clotting times of procoagulant venoms in plasma. J Pharmacol Toxicol Methods 2010;61:27-31.
    • (2010) J Pharmacol Toxicol Methods , vol.61 , pp. 27-31
    • O'Leary, M.A.1    Isbister, G.K.2
  • 39
    • 0036161285 scopus 로고    scopus 로고
    • A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation
    • DOI 10.1016/S0927-7765(01)00236-3, PII S0927776501002363
    • Höök F, Vörös J, Rodahl M, Kurrat R, Böni P, Ramsden JJ, et al. A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation. Colloids Surf B Biointerfaces 2002;24:155-70. (Pubitemid 34119110)
    • (2002) Colloids and Surfaces B: Biointerfaces , vol.24 , Issue.2 , pp. 155-170
    • Hook, F.F.1    Voros, J.2    Rodahl, M.3    Kurrat, R.4    Boni, P.5    Ramsden, J.J.6    Textor, M.7    Spencer, N.D.8    Tengvall, P.9    Gold, J.10    Kasemo, B.11
  • 40
    • 33847196810 scopus 로고    scopus 로고
    • Aptamer-based detection of plasma proteins by an electrochemical assay coupled to magnetic beads
    • Centi S, Tombelli S, Minunni M, Mascini M. Aptamer-based detection of plasma proteins by an electrochemical assay coupled to magnetic beads. Anal Chem 2007;79:1466-73.
    • (2007) Anal Chem , vol.79 , pp. 1466-1473
    • Centi, S.1    Tombelli, S.2    Minunni, M.3    Mascini, M.4
  • 42
    • 33746216936 scopus 로고    scopus 로고
    • Fibrinogen adsorption, platelet adhesion and activation on mixed hydroxyl-/methyl-terminated self-Assembled monolayers
    • DOI 10.1016/j.biomaterials.2006.06.010, PII S0142961206005515
    • Rodrigues SN, Goncalves IC, Martins MCL, Barbosa MA, Ratner BD. Fibrinogen adsorption, platelet adhesion and activation on mixed hydroxyl-/methylterminated self-Assembled monolayers. Biomaterials 2006;27:5357-67. (Pubitemid 44093714)
    • (2006) Biomaterials , vol.27 , Issue.31 , pp. 5357-5367
    • Rodrigues, S.N.1    Goncalves, I.C.2    Martins, M.C.L.3    Barbosa, M.A.4    Ratner, B.D.5
  • 44
    • 0029958045 scopus 로고    scopus 로고
    • The shape of thrombomodulin and interactions with thrombin as determined by electron microscopy
    • DOI 10.1074/jbc.271.49.31485
    • Weisel JW, Nagaswami C, Young TA, Light DR. The shape of thrombomodulin and interactions with thrombin as determined by electron microscopy. J Biol Chem 1996;271:31485-90. (Pubitemid 26408605)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.49 , pp. 31485-31490
    • Weisel, J.W.1    Nagaswami, C.2    Young, T.A.3    Light, D.R.4
  • 45
    • 77955056080 scopus 로고    scopus 로고
    • Surfaces having dual fibrinolytic and protein resistant properties by immobilization of lysine on polyurethane through a PEG spacer
    • Chen H, Zhang Y, Li D, Hu X, Wang L, McClung WG, et al. Surfaces having dual fibrinolytic and protein resistant properties by immobilization of lysine on polyurethane through a PEG spacer. J Biomed Mater Res A 2009;90:940-6.
    • (2009) J Biomed Mater Res A , vol.90 , pp. 940-946
    • Chen, H.1    Zhang, Y.2    Li, D.3    Hu, X.4    Wang, L.5    McClung, W.G.6
  • 46
    • 67349247514 scopus 로고    scopus 로고
    • Lysine-PEG-modified polyurethane as a fibrinolytic surface effect of PEG chain length on protein interactions, platelet interactions and clot lysis
    • Li D, Chen H, Glenn McClung W, Brash JL. Lysine-PEG-modified polyurethane as a fibrinolytic surface. Effect of PEG chain length on protein interactions, platelet interactions and clot lysis. Acta Biomater 2009;5:1864-71.
    • (2009) Acta Biomater , vol.5 , pp. 1864-1871
    • Li, D.1    Chen, H.2    Glenn, M.W.3    Brash, J.L.4
  • 47
    • 77956635746 scopus 로고    scopus 로고
    • Surface modification with an antithrombin-heparin complex for anticoagulation: Studies on a model surface with gold as substrate
    • Sask KN, Zhitomirsky I, Berry LR, Chan AKC, Brash JL. Surface modification with an antithrombin-heparin complex for anticoagulation: studies on a model surface with gold as substrate. Acta Biomater 2010;6:2911-9.
    • (2010) Acta Biomater , vol.6 , pp. 2911-2919
    • Sask, K.N.1    Zhitomirsky, I.2    Berry, L.R.3    Chan, A.K.C.4    Brash, J.L.5
  • 48
    • 0001482119 scopus 로고
    • Competitive adsorption at hydrophobic surfaces from binary protein systems
    • Malmsten M, Lassen B. Competitive adsorption at hydrophobic surfaces from binary protein systems. J Colloid Interface Sci 1994;166:490-8.
    • (1994) J Colloid Interface Sci , vol.166 , pp. 490-498
    • Malmsten, M.1    Lassen, B.2
  • 49
    • 33646345346 scopus 로고    scopus 로고
    • Hemocompatibility evaluation of poly(glycerol-sebacate) in vitro for vascular tissue engineering
    • DOI 10.1016/j.biomaterials.2006.04.010, PII S0142961206003176
    • Motlagh D, Yang J, Lui KY, Webb AR, Ameer GA. Hemocompatibility evaluation of poly(glycerol-sebacate) in vitro for vascular tissue engineering. Biomaterials 2006;27:4315-24. (Pubitemid 43674174)
    • (2006) Biomaterials , vol.27 , Issue.24 , pp. 4315-4324
    • Motlagh, D.1    Yang, J.2    Lui, K.Y.3    Webb, A.R.4    Ameer, G.A.5
  • 50
    • 79953840315 scopus 로고    scopus 로고
    • Immobilization of an antithrombin-heparin complex on gold: Anticoagulant properties and platelet interactions
    • Sask KN, McClung WG, Berry LR, Chan AKC, Brash JL. Immobilization of an antithrombin-heparin complex on gold: Anticoagulant properties and platelet interactions. Acta Biomater 2010;7:2029-34.
    • (2010) Acta Biomater , vol.7 , pp. 2029-2034
    • Sask, K.N.1    Mcclung, W.G.2    Berry, L.R.3    Chan, A.K.C.4    Brash, J.L.5
  • 51
    • 80055116539 scopus 로고    scopus 로고
    • Surface modification with polyethylene glycol-corn trypsin inhibitor conjugate to inhibit the contact factor pathway on blood-contacting surfaces
    • Alibeik S, Zhu S, Yau JW, Weitz JI, Brash JL. Surface modification with polyethylene glycol-corn trypsin inhibitor conjugate to inhibit the contact factor pathway on blood-contacting surfaces. Acta Biomater 2011;7: 4177-86.
    • (2011) Acta Biomater , vol.7 , pp. 4177-4186
    • Alibeik, S.1    Zhu, S.2    Yau, J.W.3    Weitz, J.I.4    Brash, J.L.5
  • 53
    • 0019752371 scopus 로고
    • Assay of coagulation proteases using peptide chromogenic and fluorogenic substrates
    • Lottenberg R, Christensen U, Jackson CM, Coleman PL. Assay of coagulation proteases using peptide chromogenic and fluorogenic substrates. Methods Enzymol 1981;80(Pt C):341-61.
    • (1981) Methods Enzymol , vol.80 , Issue.PART C , pp. 341-361
    • Lottenberg, R.1    Christensen, U.2    Jackson, C.M.3    Coleman, P.L.4
  • 54
    • 0001553437 scopus 로고    scopus 로고
    • Oriented Immobilization of Proteins
    • Rao SV, Anderson KW, Bachas LG. Oriented immobilization of proteins. Mikrochim Acta 1998;128:127-43. (Pubitemid 128476578)
    • (1998) Mikrochimica Acta , vol.128 , Issue.3 , pp. 127-143
    • Rao, S.V.1    Anderson, K.W.2    Bachas, L.G.3
  • 55
    • 0037051019 scopus 로고    scopus 로고
    • Biomedical surface science: Foundations to frontiers
    • DOI 10.1016/S0039-6028(01)01587-4, PII S0039602801015874
    • Castner DG, Ratner BD. Biomedical surface science. Foundations to frontiers. Surf Sci 2002;500:28-60. (Pubitemid 34228498)
    • (2002) Surface Science , vol.500 , Issue.1-3 , pp. 28-60
    • Castner, D.G.1    Ratner, B.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.