메뉴 건너뛰기




Volumn 43, Issue 4-5, 2014, Pages 143-155

All-atom molecular dynamics study of EAK16 peptide: The effect of pH on single-chain conformation, dimerization and self-assembly behavior

Author keywords

Amphiphilic peptides; Ionic complementary peptides; pH effect on self assembly; Self assembly

Indexed keywords

AMINO ACID; CARBON; EAK16 PEPTIDE; GLUTAMIC ACID; HYDROGEN; LYSINE; NITROGEN; OXYGEN; PEPTIDE; UNCLASSIFIED DRUG; OLIGOPEPTIDE;

EID: 84901050612     PISSN: 01757571     EISSN: 14321017     Source Type: Journal    
DOI: 10.1007/s00249-014-0949-x     Document Type: Article
Times cited : (8)

References (49)
  • 1
    • 67651215773 scopus 로고    scopus 로고
    • Molecular dynamics simulation of semiflexible polyampholyte brushes-the effect of charged monomers sequence
    • 10.1140/epje/i2009-10458-x 19466471 10.1140/epje/i2009-10458-x
    • Baratlo M, Fazli H (2009) Molecular dynamics simulation of semiflexible polyampholyte brushes-the effect of charged monomers sequence. Eur Phys J E 29:131-138. doi: 10.1140/epje/i2009-10458-x
    • (2009) Eur Phys J e , vol.29 , pp. 131-138
    • Baratlo, M.1    Fazli, H.2
  • 2
    • 75349086185 scopus 로고    scopus 로고
    • Brushes of flexible, semiflexible, and rodlike diblock polyampholytes: Molecular dynamics simulation and scaling analysis
    • 10.1103/PhysRevE.81.011801 10.1103/PhysRevE.81.011801
    • Baratlo M, Fazli H (2010) Brushes of flexible, semiflexible, and rodlike diblock polyampholytes: molecular dynamics simulation and scaling analysis. Phys Rev E 81:011801. doi: 10.1103/PhysRevE.81.011801
    • (2010) Phys Rev e , vol.81 , pp. 011801
    • Baratlo, M.1    Fazli, H.2
  • 3
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • 10.1007/978-94-015-7658-1-21 10.1007/978-94-015-7658-1-21
    • Berendsen HJC, Postma JPM, van Gunsteren WF, Hermans J (1981) Interaction models for water in relation to protein hydration. Intermol Forces 14:331-342. doi: 10.1007/978-94-015-7658-1-21
    • (1981) Intermol Forces , vol.14 , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 5
    • 0032425463 scopus 로고    scopus 로고
    • Conformational changes and disease - Serpins, prions and Alzheimer's
    • 10.1016/S0959-440X(98)80101-2 9914261 10.1016/S0959-440X(98)80101-2
    • Carrell RW, Gooptut B (1998) Conformational changes and disease - serpins, prions and Alzheimer's. Curr Opin Struct Biol 8:799-809. doi: 10.1016/S0959-440X(98)80101-2
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 799-809
    • Carrell, R.W.1    Gooptut, B.2
  • 6
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems
    • 10.1063/1.464397 10.1063/1.464397
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald: an N·log(N) method for Ewald sums in large systems. J Chem Phys 98:10089-10092. doi: 10.1063/1.464397
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 8
    • 84901039111 scopus 로고    scopus 로고
    • PH-dependent self-assembly of EAK16 peptides in the presence of a hydrophobic surface: Coarse-grained molecular dynamics simulation
    • (to be published)
    • Emamyari S, Fazli H (2014) pH-dependent self-assembly of EAK16 peptides in the presence of a hydrophobic surface: coarse-grained molecular dynamics simulation. Soft Matter (to be published)
    • (2014) Soft Matter
    • Emamyari, S.1    Fazli, H.2
  • 10
    • 1942435239 scopus 로고    scopus 로고
    • Amphipathic peptides and drug delivery
    • 10.1002/bip.10585 10.1002/bip.10585
    • Fernández-Carneado J, Kogan MJ, Pujals S, Giralt E (2004) Amphipathic peptides and drug delivery. Pept Sci 76:196-203. doi: 10.1002/bip.10585
    • (2004) Pept Sci , vol.76 , pp. 196-203
    • Fernández-Carneado, J.1    Kogan, M.J.2    Pujals, S.3    Giralt, E.4
  • 11
    • 0035827364 scopus 로고    scopus 로고
    • Protein dynamics, folding and misfolding: From basic physical chemistry to human conformational diseases
    • 10.1016/S0014-5793(01)02491-7 11412843 10.1016/S0014-5793(01)02491-7
    • Ferreira ST, De Felice FG (2001) Protein dynamics, folding and misfolding: from basic physical chemistry to human conformational diseases. FEBS Lett 498:129-134. doi: 10.1016/S0014-5793(01)02491-7
    • (2001) FEBS Lett , vol.498 , pp. 129-134
    • Ferreira, S.T.1    De Felice, F.G.2
  • 12
    • 0037699014 scopus 로고    scopus 로고
    • Concentration effect on the aggregation of a self-assembling oligopeptide
    • 10.1016/S0006-3495(03)74498-1 1303109 12829508 10.1016/S0006-3495(03) 74498-1
    • Fung SY, Keyes C, Duhamel J, Chen P (2003) Concentration effect on the aggregation of a self-assembling oligopeptide. Biophys J 85:537-548. doi: 10.1016/S0006-3495(03)74498-1
    • (2003) Biophys J , vol.85 , pp. 537-548
    • Fung, S.Y.1    Keyes, C.2    Duhamel, J.3    Chen, P.4
  • 13
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • 10.1002/(SICI)1096-987X(199709)18:12<1463: AID-JCC4>3.0.CO;2-H 10.1002/(SICI)1096-987X(199709)18:12<1463: AID-JCC4>3.0.CO;2-H
    • Hess B, Bekker H, Berendsen HJC, Fraaije JGEM (1997) LINCS: a linear constraint solver for molecular simulations. J Comp Chem 18:1463-1472. doi:10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H
    • (1997) J Comp Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.4
  • 14
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • 10.1021/ct700301q 10.1021/ct700301q
    • Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4:435-447. doi: 10.1021/ct700301q
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 15
    • 0034612266 scopus 로고    scopus 로고
    • Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds
    • doi: 10.1073/pnas.97.12.6728
    • Holmes TC, de Lacalle S, Su X, Liu G, Rich A, Zhang S (2000) Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds. Proc Natl Acad Sci USA 97:6728-6733. doi: 10.1073/pnas.97.12.6728
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6728-6733
    • Holmes, T.C.1    De Lacalle, S.2    Su, X.3    Liu, G.4    Rich, A.5    Zhang, S.6
  • 16
    • 0141483558 scopus 로고    scopus 로고
    • Effect of amino acid sequence and pH on nanofiber formation of self-assembling peptides EAK16-II and EAK16-IV
    • 10.1021/bm0341374 12959616 10.1021/bm0341374
    • Hong Y, Legge RL, Zhang S, Chen P (2003) Effect of amino acid sequence and pH on nanofiber formation of self-assembling peptides EAK16-II and EAK16-IV. Biomacromolecules 4:1433-1442. doi: 10.1021/bm0341374
    • (2003) Biomacromolecules , vol.4 , pp. 1433-1442
    • Hong, Y.1    Legge, R.L.2    Zhang, S.3    Chen, P.4
  • 17
    • 8644285594 scopus 로고    scopus 로고
    • Critical self-assembly concentration of an ionic-complementary peptide EAK16-I
    • 10.1080/00218460490508616 10.1080/00218460490508616
    • Hong Y, Lau LS, Legge RL, Chen P (2004) Critical self-assembly concentration of an ionic-complementary peptide EAK16-I. J Adhesion 80:913-931. doi: 10.1080/00218460490508616
    • (2004) J Adhesion , vol.80 , pp. 913-931
    • Hong, Y.1    Lau, L.S.2    Legge, R.L.3    Chen, P.4
  • 18
    • 28944434118 scopus 로고    scopus 로고
    • Effect of NaCl and peptide concentration on the self-assembly of an ionic-complementary peptide EAK16-II
    • 10.1016/j.colsurfb.2005.11.004 10.1016/j.colsurfb.2005.11.004
    • Hong Y, Pritzker MD, Legge RL, Chen P (2005) Effect of NaCl and peptide concentration on the self-assembly of an ionic-complementary peptide EAK16-II. Colloids Surf B 46:152-161. doi: 10.1016/j.colsurfb.2005.11.004
    • (2005) Colloids Surf B , vol.46 , pp. 152-161
    • Hong, Y.1    Pritzker, M.D.2    Legge, R.L.3    Chen, P.4
  • 19
    • 0036629182 scopus 로고    scopus 로고
    • Towards quantitative assays with peptide chips: A surface engineering approach
    • 10.1016/S0167-7799(02)01984-4 12062966 10.1016/S0167-7799(02)01984-4
    • Houseman BT, Mrksich M (2002) Towards quantitative assays with peptide chips: a surface engineering approach. Trends Biotechnol 20:279-281. doi: 10.1016/S0167-7799(02)01984-4
    • (2002) Trends Biotechnol , vol.20 , pp. 279-281
    • Houseman, B.T.1    Mrksich, M.2
  • 20
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • 10.1016/0263-7855(96)00018-5 8744570 10.1016/0263-7855(96)00018-5
    • Humphrey W, Dalkeand A, Schulten K (1996) VMD: visual molecular dynamics. J Mol Graph 14:33-38. doi: 10.1016/0263-7855(96)00018-5
    • (1996) J Mol Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalkeand, A.2    Schulten, K.3
  • 21
    • 84901039112 scopus 로고    scopus 로고
    • HyperChem(TM), Hypercube, Inc., 1115 NW 4th Street, Gainesville, Florida 32601, USA
    • HyperChem(TM), Hypercube, Inc., 1115 NW 4th Street, Gainesville, Florida 32601, USA
  • 22
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins. Energy minimizations for crystals of cyclic peptides and crambin
    • 10.1021/ja00214a001 10.1021/ja00214a001
    • Jorgensen WL, Tirado-Rives J (1988) The OPLS potential functions for proteins. Energy minimizations for crystals of cyclic peptides and crambin. J Am Chem Soc 110:1657-1666. doi: 10.1021/ja00214a001
    • (1988) J Am Chem Soc , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 23
    • 4143071284 scopus 로고    scopus 로고
    • Self-assembly of the ionic peptide EAK16: The effect of charge distributions on self-assembly
    • 10.1529/biophysj.103.038166 1304463 15298927 10.1529/biophysj.103.038166
    • Jun S, Hong Y, Imamura H, Ha B-Y, Bechhoefer J, Chen P (2004) Self-assembly of the ionic peptide EAK16: the effect of charge distributions on self-assembly. Biophys J 87:1249-1259. doi: 10.1529/biophysj.103.038166
    • (2004) Biophys J , vol.87 , pp. 1249-1259
    • Jun, S.1    Hong, Y.2    Imamura, H.3    Ha, B.-Y.4    Bechhoefer, J.5    Chen, P.6
  • 24
    • 0037162463 scopus 로고    scopus 로고
    • Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: Implications for cartilage tissue repair
    • 10.1073/pnas.142309999 126613 12119393 10.1073/pnas.142309999
    • Kisiday J, Jin M, Kurz B, Hung H, Semino C, Zhang S, Grodzinsky AJ (2002) Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: implications for cartilage tissue repair. Proc Natl Acad Sci USA 99:9996-10001. doi: 10.1073/pnas.142309999
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9996-10001
    • Kisiday, J.1    Jin, M.2    Kurz, B.3    Hung, H.4    Semino, C.5    Zhang, S.6    Grodzinsky, A.J.7
  • 25
    • 33751022571 scopus 로고    scopus 로고
    • Photoreversibly switchable superhydrophobic surface with erasable and rewritable pattern
    • 10.1021/ja0655901 17090019 10.1021/ja0655901
    • Lim HS, Han JT, Kwak D, Jin M, Cho K (2006) Photoreversibly switchable superhydrophobic surface with erasable and rewritable pattern. J Am Chem Soc 128:14458-14459. doi: 10.1021/ja0655901
    • (2006) J Am Chem Soc , vol.128 , pp. 14458-14459
    • Lim, H.S.1    Han, J.T.2    Kwak, D.3    Jin, M.4    Cho, K.5
  • 26
    • 48449091156 scopus 로고    scopus 로고
    • Structural dynamic of a self-assembling peptide d-EAK16 made of only d-amino acids
    • 10.1371/journal.pone.0002364 2387071 18509542 10.1371/journal.pone. 0002364
    • Luo Z, Zhao X, Zhang S (2008) Structural dynamic of a self-assembling peptide d-EAK16 made of only d-amino acids. PLoS ONE 3(5):e2364. doi: 10.1371/journal.pone.0002364
    • (2008) PLoS ONE , vol.3 , Issue.5 , pp. 2364
    • Luo, Z.1    Zhao, X.2    Zhang, S.3
  • 27
    • 84986440341 scopus 로고
    • Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • 10.1002/jcc.540130805 10.1002/jcc.540130805
    • Miyamoto S, Kollman PA (1992) Settle: an analytical version of the SHAKE and RATTLE algorithm for rigid water models. J Comp Chem 13:952-962. doi: 10.1002/jcc.540130805
    • (1992) J Comp Chem , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 28
    • 77956380613 scopus 로고    scopus 로고
    • Interaction of an ionic complementary peptide with a hydrophobic graphite surface
    • 10.1002/pro.444 2975128 20572020 10.1002/pro.444
    • Sheng Y, Wang Y, Chen P (2010) Interaction of an ionic complementary peptide with a hydrophobic graphite surface. Protein Sci 19:1639-1648. doi: 10.1002/pro.444
    • (2010) Protein Sci , vol.19 , pp. 1639-1648
    • Sheng, Y.1    Wang, Y.2    Chen, P.3
  • 29
    • 0035090680 scopus 로고    scopus 로고
    • Prions: Disease propagation and disease therapy by conformational transmission
    • 10.1016/S1471-4914(01)01931-1 11286781 10.1016/S1471-4914(01)01931-1
    • Soto C, Saborio GP (2001) Prions: disease propagation and disease therapy by conformational transmission. TRENDS Mol Med 7:109-114. doi: 10.1016/S1471-4914(01)01931-1
    • (2001) TRENDS Mol Med , vol.7 , pp. 109-114
    • Soto, C.1    Saborio, G.P.2
  • 32
    • 84943200457 scopus 로고
    • A Leap-frog algorithm for stochastic dynamics
    • 10.1080/08927028808080941 10.1080/08927028808080941
    • van Gunsteren WF, Berendsen HJC (1988) A Leap-frog algorithm for stochastic dynamics. Mol Sim 1:173-185. doi: 10.1080/08927028808080941
    • (1988) Mol Sim , vol.1 , pp. 173-185
    • Van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 33
    • 77953156726 scopus 로고    scopus 로고
    • The amphiphilic self-assembling peptide EAK16-I as a potential hydrophobic drug carrier
    • doi: 10.1155/2008/516286
    • Wang J, Tang F, Li F, Lin J, Zhang Y, Du L, Zhao X (2008a) The amphiphilic self-assembling peptide EAK16-I as a potential hydrophobic drug carrier. J Nanomater 2008:516286-516294. doi: 10.1155/2008/516286
    • (2008) J Nanomater , pp. 516286-516294
    • Wang, J.1    Tang, F.2    Li, F.3    Lin, J.4    Zhang, Y.5    Du, L.6    Zhao, X.7
  • 34
    • 56049106833 scopus 로고    scopus 로고
    • Designer functionalized self-assembling peptide nanofiber scaffolds for growth, migration, and tubulogenesis of human umbilical vein endothelial cells
    • 10.1039/B807155A 10.1039/b807155a
    • Wang X, Horii A, Zhang S (2008b) Designer functionalized self-assembling peptide nanofiber scaffolds for growth, migration, and tubulogenesis of human umbilical vein endothelial cells. Soft Matter 4:2388-2395. doi: 10.1039/B807155A
    • (2008) Soft Matter , vol.4 , pp. 2388-2395
    • Wang, X.1    Horii, A.2    Zhang, S.3
  • 35
    • 33750067974 scopus 로고    scopus 로고
    • Dipolar control of monolayer morphology: Spontaneous SAM patterning
    • 10.1021/ja065338t 17031941 10.1021/ja065338t
    • Wei Y, Tong W, Wise C, Wei X, Armbrust K, Zimmt M (2006) Dipolar control of monolayer morphology: spontaneous SAM patterning. J Am Chem Soc 128:13362-13363. doi: 10.1021/ja065338t
    • (2006) J Am Chem Soc , vol.128 , pp. 13362-13363
    • Wei, Y.1    Tong, W.2    Wise, C.3    Wei, X.4    Armbrust, K.5    Zimmt, M.6
  • 36
    • 0037117591 scopus 로고    scopus 로고
    • Beyond molecules: Self-assembly of mesoscopic and macroscopic components
    • 10.1073/pnas.082065899 122665 11959929 10.1073/pnas.082065899
    • Whitesides GM, Boncheva M (2002) Beyond molecules: self-assembly of mesoscopic and macroscopic components. Proc Natl Acad Sci USA 99:4769-4774. doi: 10.1073/pnas.082065899
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4769-4774
    • Whitesides, G.M.1    Boncheva, M.2
  • 37
    • 0037192505 scopus 로고    scopus 로고
    • Self-assembly at all scales
    • 10.1126/science.1070821 11923529 10.1126/science.1070821
    • Whitesides GM, Grzybowski B (2002) Self-assembly at all scales. Science 295:2418-2421. doi: 10.1126/science.1070821
    • (2002) Science , vol.295 , pp. 2418-2421
    • Whitesides, G.M.1    Grzybowski, B.2
  • 38
    • 0026433721 scopus 로고
    • Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures
    • 10.1126/science.1962191 1962191 10.1126/science.1962191
    • Whitesides GM, Mathias JP, Seto C (1991) Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures. Science 254:1312-1319. doi: 10.1126/science.1962191
    • (1991) Science , vol.254 , pp. 1312-1319
    • Whitesides, G.M.1    Mathias, J.P.2    Seto, C.3
  • 39
    • 4544357583 scopus 로고    scopus 로고
    • Nanolithography and nanochemistry: Probe-related patterning techniques and chemical modification for nanometer-sized devices
    • 10.1002/anie.200300609 10.1002/anie.200300609
    • Wouters D, Schubert US (2004) Nanolithography and nanochemistry: probe-related patterning techniques and chemical modification for nanometer-sized devices. Angew Chem Int Ed 43:2480-2495. doi: 10.1002/anie.200300609
    • (2004) Angew Chem Int Ed , vol.43 , pp. 2480-2495
    • Wouters, D.1    Schubert, U.S.2
  • 40
    • 44949188455 scopus 로고    scopus 로고
    • Folding and dimerization of the ionic peptide EAK16-IV
    • 10.1002/prot.21903 18214962 10.1002/prot.21903
    • Yan Z, Wang J, Wang W (2008) Folding and dimerization of the ionic peptide EAK16-IV. Proteins 72:150-162. doi: 10.1002/prot.21903
    • (2008) Proteins , vol.72 , pp. 150-162
    • Yan, Z.1    Wang, J.2    Wang, W.3
  • 41
    • 35048825244 scopus 로고    scopus 로고
    • Surface-assisted assembly of an ionic-complementary peptide: Controllable growth of nanofibers
    • 10.1021/ja073168u
    • Yang H, Fung S-Yu, Pritzker M, Chen P (2007a) Surface-assisted assembly of an ionic-complementary peptide: controllable growth of nanofibers. J Am Chem Soc 129(12200):12210. doi: 10.1021/ja073168u
    • (2007) J Am Chem Soc , vol.129 , Issue.1220 , pp. 12210
    • Yang, H.1    Fung, S.-Y.2    Pritzker, M.3    Chen, P.4
  • 42
    • 44449176603 scopus 로고    scopus 로고
    • Modification of hydrophilic and hydrophobic surfaces using an ionic-complementary peptide
    • 10.1371/journal.pone.0001325 2117347 18091996 10.1371/journal.pone. 0001325
    • Yang H, Fung S-Yu, Pritzker M, Chen P (2007b) Modification of hydrophilic and hydrophobic surfaces using an ionic-complementary peptide. PLoS ONE 2:e1325. doi: 10.1371/journal.pone.0001325
    • (2007) PLoS ONE , vol.2 , pp. 1325
    • Yang, H.1    Fung, S.-Y.2    Pritzker, M.3    Chen, P.4
  • 43
    • 0036377156 scopus 로고    scopus 로고
    • Amyloid-fibril formation: Proposed mechanisms and relevance to conformational disease
    • 10.1046/j.1432-1033.2002.03024.x 12135474 10.1046/j.1432-1033.2002.03024. x
    • Zerovnik E (2002) Amyloid-fibril formation: proposed mechanisms and relevance to conformational disease. Eur J Biochem 269:3362-3371. doi: 10.1046/j.1432-1033.2002.03024.x
    • (2002) Eur J Biochem , vol.269 , pp. 3362-3371
    • Zerovnik, E.1
  • 44
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • 10.1038/nbt874 14520402 10.1038/nbt874
    • Zhang S (2003) Fabrication of novel biomaterials through molecular self-assembly. Nat Biotechnol 21:1171-1178. doi: 10.1038/nbt874
    • (2003) Nat Biotechnol , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 45
    • 0026758377 scopus 로고
    • Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae
    • 556839 1396572
    • Zhang S, Lockshin C, Herbert A, Winter E, Rich A (1992) Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae. EMBO J 11:3787-3796
    • (1992) EMBO J , vol.11 , pp. 3787-3796
    • Zhang, S.1    Lockshin, C.2    Herbert, A.3    Winter, E.4    Rich, A.5
  • 46
    • 0027416047 scopus 로고
    • Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane
    • 10.1073/pnas.90.8.3334 46294 7682699 10.1073/pnas.90.8.3334
    • Zhang S, Holmes T, Lockshin C, Rich A (1993) Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane. Proc Natl Acad Sci USA 90:3334-3338. doi: 10.1073/pnas.90.8.3334
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3334-3338
    • Zhang, S.1    Holmes, T.2    Lockshin, C.3    Rich, A.4
  • 47
    • 0029411957 scopus 로고
    • Self-complementary oligopeptide matrices support mammalian cell attachment
    • 10.1016/0142-9612(95)96874-Y 8590765 10.1016/0142-9612(95)96874-Y
    • Zhang S, Holmes TC, Michael DiPersio C, Hynes RO, Su X, Rich A (1995) Self-complementary oligopeptide matrices support mammalian cell attachment. Biomaterials 16:1385-1393. doi: 10.1016/0142-9612(95)96874-Y
    • (1995) Biomaterials , vol.16 , pp. 1385-1393
    • Zhang, S.1    Holmes, T.C.2    Michael Dipersio, C.3    Hynes, R.O.4    Su, X.5    Rich, A.6
  • 49
    • 0036897817 scopus 로고    scopus 로고
    • Design of nanostructured biological materials through self-assembly of peptides and proteins
    • 10.1016/s1367-5931(02)00391-5 12470743 10.1016/S1367-5931(02)00391-5
    • Zhang S, Marini DM, Hwang W, Santoso S (2002) Design of nanostructured biological materials through self-assembly of peptides and proteins. Curr Opin Chem Biol 6:865-871. doi: 10.1016/s1367-5931(02)00391-5
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 865-871
    • Zhang, S.1    Marini, D.M.2    Hwang, W.3    Santoso, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.