메뉴 건너뛰기




Volumn 19, Issue 9, 2010, Pages 1639-1648

Interaction of an ionic complementary peptide with a hydrophobic graphite surface

Author keywords

Adsorption; Graphite; Ionic complementarity; Peptide

Indexed keywords

GLUTAMIC ACID; GRAPHITE; IONIC COMPLEMENTARY PEPTIDE; LYSINE; PEPTIDE; PEPTIDE DERIVATIVE; PEPTIDE EAK 1611; UNCLASSIFIED DRUG;

EID: 77956380613     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.444     Document Type: Article
Times cited : (26)

References (39)
  • 1
    • 0000189822 scopus 로고
    • Adsorption of complex proteins at interfaces
    • Andrade JD, Hlady V, Wei AP (1992) Adsorption of complex proteins at interfaces. Pure Appl Chem 64: 1777-1781.
    • (1992) Pure Appl Chem , vol.64 , pp. 1777-1781
    • Andrade, J.D.1    Hlady, V.2    Wei, A.P.3
  • 2
    • 0032487118 scopus 로고    scopus 로고
    • Relative importance of surface wettability and charged functional groups on NIH 3T3 fibroblast attachment, spreading, and cytoskeletal organization
    • DOI 10.1002/(SICI)1097-4636(19980905)41:3<422::AID-JBM12>3.0.CO;2-K
    • Webb K, Hlady V, Tresco PA (1998) Relative importance of surface wettability and charged functional groups on NIH 3T3 fibroblast attachment, spreading, and cytoskeletal organization. J Biomed Mater Res 41:422-430. (Pubitemid 28300107)
    • (1998) Journal of Biomedical Materials Research , vol.41 , Issue.3 , pp. 422-430
    • Webb, K.1    Hlady, V.2    Tresco, P.A.3
  • 3
    • 0001181097 scopus 로고
    • Surface chemical modifications of materials which influence animal cell adhesion: A review
    • Schamberger PC, Gardella JA Jr (1994) Surface chemical modifications of materials which influence animal cell adhesion: a review. Colloid Surf B Biointerfaces 2: 209-223.
    • (1994) Colloid Surf B Biointerfaces , vol.2 , pp. 209-223
    • Schamberger, P.C.1    Gardella Jr., J.A.2
  • 4
    • 33745004875 scopus 로고    scopus 로고
    • The effect of RGD fluorosurfactant polymer modification of ePTFE on endothelial cell adhesion, growth, and function
    • DOI 10.1016/j.biomaterials.2006.05.009, PII S0142961206004480
    • Larsen CC, Kligman F, Kottke-Marchant K, Marchant RE (2006) The effect of RGD fluorosurfactant polymer modification of ePTFE on endothelial cell adhesion, growth, and function. Biomaterials 27:4846-4855. (Pubitemid 43866918)
    • (2006) Biomaterials , vol.27 , Issue.28 , pp. 4846-4855
    • Larsen, C.C.1    Kligman, F.2    Kottke-Marchant, K.3    Marchant, R.E.4
  • 5
    • 0035124829 scopus 로고    scopus 로고
    • Bioactive immobilization of r-hirudin on CVD-coated metallic implant devices
    • DOI 10.1016/S0142-9612(00)00244-1, PII S0142961200002441
    • Lahann J, Klee D, Pluester W, Hoecker H (2001) Bioactive immobilization of r-hirudin on CVD-coated metallic implant devices. Biomaterials 22:817-826. (Pubitemid 32143795)
    • (2001) Biomaterials , vol.22 , Issue.8 , pp. 817-826
    • Lahann, J.1    Klee, D.2    Pluester, W.3    Hoecker, H.4
  • 7
    • 33645380798 scopus 로고    scopus 로고
    • Tumor targeting by surface-modified protein microspheres
    • Toublan FJ, Boppart S, Suslick KS (2006) Tumor targeting by surface-modified protein microspheres. J Am Chem Soc 128:3472-3473.
    • (2006) J Am Chem Soc , vol.128 , pp. 3472-3473
    • Toublan, F.J.1    Boppart, S.2    Suslick, K.S.3
  • 9
    • 0030026989 scopus 로고    scopus 로고
    • Protein adsorption on solid surfaces
    • Hlady H, Buijs J (1996) Protein adsorption on solid surfaces. Curr Opin Biotechnol 7:72-77.
    • (1996) Curr Opin Biotechnol , vol.7 , pp. 72-77
    • Hlady, H.1    Buijs, J.2
  • 10
    • 0035807149 scopus 로고    scopus 로고
    • A survey of structure-property relationships of surfaces that resist the adsorption of protein
    • DOI 10.1021/la010384m
    • Ostuni E, Chapman RG, Holmlin RE, Takayama S, Whitesides GM (2003) A survey of structure-property relationships of surfaces that resist the adsorption of protein. Langmuir 17:5605-5620. (Pubitemid 35330800)
    • (2001) Langmuir , vol.17 , Issue.18 , pp. 5605-5620
    • Ostuni, E.1    Chapman, R.G.2    Holmlin, R.E.3    Takayama, S.4    Whitesides, G.M.5
  • 11
    • 0037453543 scopus 로고    scopus 로고
    • Kosmotropes form the basis of protein-resistant surfaces
    • Kane RS, Deschatelets P, Whitesides GM (2003) Kosmotropes form the basis of protein-resistant surfaces. Langmuir 19:2388-2391.
    • (2003) Langmuir , vol.19 , pp. 2388-2391
    • Kane, R.S.1    Deschatelets, P.2    Whitesides, G.M.3
  • 12
    • 1342302795 scopus 로고    scopus 로고
    • The interaction of proteins with solid surfaces
    • Gray JJ (2004) The interaction of proteins with solid surfaces. Curr Opin Struct Biol 14:110-115.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 110-115
    • Gray, J.J.1
  • 13
    • 0032533193 scopus 로고    scopus 로고
    • Formation of adsorbed protein layers
    • Malmsten M (1998) Formation of adsorbed protein layers. J Colloid Interface Sci 207:186-199.
    • (1998) J Colloid Interface Sci , vol.207 , pp. 186-199
    • Malmsten, M.1
  • 14
    • 0033885458 scopus 로고    scopus 로고
    • On the molecular basis of fouling resistance
    • Morra M (2000) On the molecular basis of fouling resistance. J Biomater Sci Polym Ed 11:547-569.
    • (2000) J Biomater Sci Polym Ed , vol.11 , pp. 547-569
    • Morra, M.1
  • 15
  • 16
    • 79960304962 scopus 로고
    • Protein adsorption on polymer surfaces: Calculation of adsorption energies
    • Lu DR, Park K (1990) Protein adsorption on polymer surfaces: Calculation of adsorption energies. J Biomater Sci Polym Ed 1:243-260.
    • (1990) J Biomater Sci Polym Ed , vol.1 , pp. 243-260
    • Lu, D.R.1    Park, K.2
  • 17
    • 0000964469 scopus 로고
    • Modeling of protein adsorption on polymer surface: Computation of adsorption potential
    • Noinville V, Vidalmadjar C, Sebille B (1995) Modeling of protein adsorption on polymer surface: computation of adsorption potential. J Phys Chem 99:1516-1522.
    • (1995) J Phys Chem , vol.99 , pp. 1516-1522
    • Noinville, V.1    Vidalmadjar, C.2    Sebille, B.3
  • 18
    • 0037013360 scopus 로고    scopus 로고
    • A Brownian dynamics study of the initial stages of hen egg-white lysozyme adsorption at a solid surface
    • Ravichandran S, Madura JD, Talbot JA (2001) A Brownian dynamics study of the initial stages of hen egg-white lysozyme adsorption at a solid surface. J Phys Chem B 105:3610-3613.
    • (2001) J Phys Chem B , vol.105 , pp. 3610-3613
    • Ravichandran, S.1    Madura, J.D.2    Talbot, J.A.3
  • 19
    • 66249119965 scopus 로고    scopus 로고
    • Molecular simulation of protein-surface interactions: Benefits, problems, solutions, and future directions
    • Review
    • Latour RA (2008) Molecular simulation of protein-surface interactions: Benefits, problems, solutions, and future directions (Review). Biointerphases 3:FC2-FC12.
    • (2008) Biointerphases , vol.3
    • Latour, R.A.1
  • 20
    • 72449127421 scopus 로고    scopus 로고
    • Nanodroplets activated and guided folding of graphene nanostructures
    • Patra N, Wang B, Král P (2009) Nanodroplets activated and guided folding of graphene nanostructures. Nano Lett 9:3766-3771.
    • (2009) Nano Lett , vol.9 , pp. 3766-3771
    • Patra, N.1    Wang, B.2    Král, P.3
  • 21
    • 72449139518 scopus 로고    scopus 로고
    • Nanotechnology: Soggy origgami
    • Crespi VH (2009) Nanotechnology: Soggy origgami. Nature 462:858-859.
    • (2009) Nature , vol.462 , pp. 858-859
    • Crespi, V.H.1
  • 22
    • 77954072403 scopus 로고    scopus 로고
    • Tension at the surface: Which phase is more important, liquid or vapor?
    • Prpich AM, Sheng Y, Wang W, Biswas ME, Chen P (2009) Tension at the surface: Which phase is more important, liquid or vapor? PLoS One 4:e8281.
    • (2009) PLoS One , vol.4
    • Prpich, A.M.1    Sheng, Y.2    Wang, W.3    Biswas, M.E.4    Chen, P.5
  • 23
    • 0026940917 scopus 로고
    • Cell-type-specific adhesion mechanisms mediated by fibronectin adsorbed to chemically derivatized substra
    • Lewandowska K, Pergament E, Sukenik CN, Culp LA (1992) Cell-type-specific adhesion mechanisms mediated by fibronectin adsorbed to chemically derivatized substra. J Biomed Mater Res 26:1343-1363.
    • (1992) J Biomed Mater Res , vol.26 , pp. 1343-1363
    • Lewandowska, K.1    Pergament, E.2    Sukenik, C.N.3    Culp, L.A.4
  • 24
    • 0037699014 scopus 로고    scopus 로고
    • Concentration effect on the aggregation of a self-assembling oligopeptide
    • Fung SY, Keyes C, Duhamel J, Chen P (2003) Concentration effect on the aggregation of a self-assembling oligopeptide. Biophy J 85:537-548. (Pubitemid 36763513)
    • (2003) Biophysical Journal , vol.85 , Issue.1 , pp. 537-548
    • Fung, S.Y.1    Keyes, C.2    Duhamel, J.3    Chen, P.4
  • 25
    • 0141483558 scopus 로고    scopus 로고
    • Effect of amino acid sequence and pH on nanofiber formation of self-assembling peptides EAK16-II and EAK16-IV
    • DOI 10.1021/bm0341374
    • Hong Y, Legge RL, Zhang S, Chen P (2003) Effect of amino acid sequence and pH on nanofiber formation with self-assembling peptides EAK16-II and EAK16-IV. Biomacromolecules 4:1433-1442. (Pubitemid 37203310)
    • (2003) Biomacromolecules , vol.4 , Issue.5 , pp. 1433-1442
    • Hong, Y.1    Legge, R.L.2    Zhang, S.3    Chen, P.4
  • 26
    • 4143071284 scopus 로고    scopus 로고
    • Self-assembly of the ionic peptide EAK16: The effect of charge distributions on self-assembly
    • DOI 10.1529/biophysj.103.038166
    • Jun S, Hong Y, Immamura H, Ha BY, Bechhoefer J, Chen P (2004) Self assembly of the ionic peptide EAK16: The effect of charge districutions on self-assembly. Biophy J 87:1249-1259. (Pubitemid 39095101)
    • (2004) Biophysical Journal , vol.87 , Issue.2 , pp. 1249-1259
    • Jun, S.1    Hong, Y.2    Imamura, H.3    Ha, B.-Y.4    Bechhoefer, J.5    Chen, P.6
  • 27
    • 35048825244 scopus 로고    scopus 로고
    • Surface-assisted assembly of an ionic-complementary peptide: Controllable growth of nanofibers
    • DOI 10.1021/ja073168u
    • Yang H, Fung SY, Pritzker M, Chen P (2007) Surface-assisted assembly of an ionic-complementary peptide: controllable growth of nanofibers. J Am Chem Soc 129: 12200-12210. (Pubitemid 47556856)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.40 , pp. 12200-12210
    • Yang, H.1    Fung, S.-Y.2    Pritzker, M.3    Chen, P.4
  • 28
    • 44449176603 scopus 로고    scopus 로고
    • Modification of hydrophilic and hydrophobic surfaces using an ionic-complementary peptide
    • Yang H, Fung SY, Pritzker M, Chen P (2007) Modification of hydrophilic and hydrophobic surfaces using an ionic-complementary peptide. PLoS One 2:e1325.
    • (2007) PLoS One , vol.2
    • Yang, H.1    Fung, S.Y.2    Pritzker, M.3    Chen, P.4
  • 29
    • 75149191850 scopus 로고    scopus 로고
    • Adsorption of an ionic complementary peptide on the hydrophobic graphite surface
    • Sheng Y, Wang W, Chen P (2010) Adsorption of an ionic complementary peptide on the hydrophobic graphite surface. J Phys Chem C 114:454-459.
    • (2010) J Phys Chem C , vol.114 , pp. 454-459
    • Sheng, Y.1    Wang, W.2    Chen, P.3
  • 30
    • 0029439180 scopus 로고
    • Protein adsorption on low temperature isotropic carbon: V. How is it related to its blood compatibility?
    • Feng L, Andrade JD (1995) Protein adsorption on low temperature isotropic carbon: V. how is it related to its blood compatibility? J Biomater Sci Polym Ed 7:439-452.
    • (1995) J Biomater Sci Polym Ed , vol.7 , pp. 439-452
    • Feng, L.1    Andrade, J.D.2
  • 31
    • 0034984144 scopus 로고    scopus 로고
    • Protein folding theory: From lattice to all-atom models
    • Mirny L, Shakhnovich E (2001) Protein folding theory: From lattice to all-atom models. Annu Rev Biophy Biomol Struct 30:361-369.
    • (2001) Annu Rev Biophy Biomol Struct , vol.30 , pp. 361-369
    • Mirny, L.1    Shakhnovich, E.2
  • 33
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • Daggett V, Fersht AR (2003) The present view of the mechanism of protein folding. Nature Rev Mol Cell Biol 4:497-502.
    • (2003) Nature Rev Mol Cell Biol , vol.4 , pp. 497-502
    • Daggett, V.1    Fersht, A.R.2
  • 34
    • 0027382315 scopus 로고
    • Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysis
    • Jackson SE, elMasry N, Fersht AR (1993) Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis. Biochem 32: 11270-11278.
    • (1993) Biochem , vol.32 , pp. 11270-11278
    • Jackson, S.E.1    ElMasry, N.2    Fersht, A.R.3
  • 35
    • 33644515673 scopus 로고    scopus 로고
    • Comparative all-atomic study of unfolding pathways for proteins CI2 and barnase
    • Sheng Y, Wang W (2006) Comparative all-atomic study of unfolding pathways for proteins CI2 and barnase. Physical Review E 73:021915.
    • (2006) Physical Review E , vol.73 , pp. 021915
    • Sheng, Y.1    Wang, W.2
  • 36
    • 50449108737 scopus 로고    scopus 로고
    • Oriented epitaxial growth of amyloid fibrils of the N27C mutant b25-35 peptide
    • Karsai Á, Murvai Ü, Soós K, Penke B, Kellermayer MSZ (2008) Oriented epitaxial growth of amyloid fibrils of the N27C mutant b25-35 peptide. Eur Biophy J 37: 1133-1137.
    • (2008) Eur Biophy J , vol.37 , pp. 1133-1137
    • Karsai, Á.1    Murvai, Ü.2    Soós, K.3    Penke, B.4    Kellermayer, M.S.Z.5
  • 38
    • 0037093874 scopus 로고    scopus 로고
    • Direct observation of the folding and unfolding of a β-hairpin in explicit water through computer simulation
    • DOI 10.1021/ja0257321
    • Wu X, Wang S, Brooks BR (2002) Direct observation of the folding and unfolding of a β-hairpin in explicit water through computer simulation. J Am Chem Soc 124:5282-5283. (Pubitemid 34506921)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.19 , pp. 5282-5283
    • Wu, X.1    Wang, S.2    Brooks, B.R.3
  • 39
    • 0242509772 scopus 로고    scopus 로고
    • Self-guided Langevin dynamics simulation method
    • Wu X, Brooks BR (2003) Self-guided Langevin dynamics simulation method. Chem Phys Lett 381:512-518.
    • (2003) Chem Phys Lett , vol.381 , pp. 512-518
    • Wu, X.1    Brooks, B.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.