메뉴 건너뛰기




Volumn 5, Issue 10, 2015, Pages 1154-1165

Structure-based Design of Peptides with High Affinity and Specificity to HER2 Positive Tumors

Author keywords

breast cancer; HER2 targeted peptide; MD simulation; structure based design

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 2; PEPTIDE 23; PEPTIDE 26; PEPTIDE 27; PEPTIDE 27 24M; PEPTIDE 32; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG; ERBB2 PROTEIN, HUMAN; PEPTIDE; PROTEIN BINDING;

EID: 84945898755     PISSN: None     EISSN: 18387640     Source Type: Journal    
DOI: 10.7150/thno.12398     Document Type: Article
Times cited : (34)

References (56)
  • 3
    • 0037429725 scopus 로고    scopus 로고
    • The ErbB receptors and their role in cancer progression
    • Holbro T, Civenni G, Hynes NE. The ErbB receptors and their role in cancer progression. Exp Cell Res. 2003; 284: 99-110.
    • (2003) Exp Cell Res. , vol.284 , pp. 99-110
    • Holbro, T.1    Civenni, G.2    Hynes, N.E.3
  • 4
    • 0034773992 scopus 로고    scopus 로고
    • The EGFR family and its ligands in human cancer: signalling mechanisms and therapeutic opportunities
    • Yarden Y. The EGFR family and its ligands in human cancer: signalling mechanisms and therapeutic opportunities. Eur J Cancer. 2001; 37 (Suppl 4): S3-S8.
    • (2001) Eur J Cancer. , vol.37 , pp. S3-S8
    • Yarden, Y.1
  • 5
    • 37049183697 scopus 로고
    • Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene
    • Slamon DJ, Clark GM, Wong SG, Levin WJ, Ullrich A, McGuire WL. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science. 1987; 235: 177-82.
    • (1987) Science. , vol.235 , pp. 177-182
    • Slamon, D.J.1    Clark, G.M.2    Wong, S.G.3    Levin, W.J.4    Ullrich, A.5    McGuire, W.L.6
  • 8
    • 34247346051 scopus 로고    scopus 로고
    • Prognostic Significance of Human Epidermal Growth Factor Receptor Positivity for the Development of Brain Metastasis After Newly Diagnosed Breast Cancer
    • Gabos Z, Sinha R, Hanson J, Chauhan N, Hugh J, Mackey JR, et al. Prognostic Significance of Human Epidermal Growth Factor Receptor Positivity for the Development of Brain Metastasis After Newly Diagnosed Breast Cancer. J Clin Oncol. 2006; 24: 5658-63.
    • (2006) J Clin Oncol. , vol.24 , pp. 5658-5663
    • Gabos, Z.1    Sinha, R.2    Hanson, J.3    Chauhan, N.4    Hugh, J.5    Mackey, J.R.6
  • 10
    • 31644439702 scopus 로고    scopus 로고
    • Herceptin: mechanisms of action and resistance
    • Nahta R, Esteva FJ. Herceptin: mechanisms of action and resistance. Cancer Lett. 2006; 232: 123-38.
    • (2006) Cancer Lett. , vol.232 , pp. 123-138
    • Nahta, R.1    Esteva, F.J.2
  • 11
    • 84895074690 scopus 로고    scopus 로고
    • New HER2-positive targeting agents in clinical practice
    • Tolaney S. New HER2-positive targeting agents in clinical practice. Curr Oncol Rep. 2014; 16: 013-0359.
    • (2014) Curr Oncol Rep. , vol.16 , pp. 013-0359
    • Tolaney, S.1
  • 12
    • 84907439121 scopus 로고    scopus 로고
    • Small molecule tyrosine kinase inhibitors of ErbB2/HER2/Neu in the treatment of aggressive breast cancer
    • Schroeder RL, Stevens CL, Sridhar J. Small molecule tyrosine kinase inhibitors of ErbB2/HER2/Neu in the treatment of aggressive breast cancer. Molecules. 2014; 19: 15196-212.
    • (2014) Molecules. , vol.19 , pp. 15196-15212
    • Schroeder, R.L.1    Stevens, C.L.2    Sridhar, J.3
  • 14
    • 52449108735 scopus 로고    scopus 로고
    • Affibody molecules for in vivo characterization of HER2-positive tumors by near-infrared imaging
    • Lee SB, Hassan M, Fisher R, Chertov O, Chernomordik V, Kramer-Marek G, et al. Affibody molecules for in vivo characterization of HER2-positive tumors by near-infrared imaging. Clin Cancer Res. 2008; 14: 3840-9.
    • (2008) Clin Cancer Res. , vol.14 , pp. 3840-3849
    • Lee, S.B.1    Hassan, M.2    Fisher, R.3    Chertov, O.4    Chernomordik, V.5    Kramer-Marek, G.6
  • 15
    • 33947672248 scopus 로고    scopus 로고
    • Radionuclide therapy of HER2-positive microxenografts using a 177Lu-labeled HER2-specific Affibody molecule
    • Tolmachev V, Orlova A, Pehrson R, Galli J, Baastrup B, Andersson K, et al. Radionuclide therapy of HER2-positive microxenografts using a 177Lu-labeled HER2-specific Affibody molecule. Cancer Res. 2007; 67: 2773-82.
    • (2007) Cancer Res. , vol.67 , pp. 2773-2782
    • Tolmachev, V.1    Orlova, A.2    Pehrson, R.3    Galli, J.4    Baastrup, B.5    Andersson, K.6
  • 17
    • 0037434791 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
    • Cho HS, Mason K, Ramyar KX, Stanley AM, Gabelli SB, Denney DW, Jr., et al. Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature. 2003; 421: 756-60.
    • (2003) Nature. , vol.421 , pp. 756-760
    • Cho, H.S.1    Mason, K.2    Ramyar, K.X.3    Stanley, A.M.4    Gabelli, S.B.5    Denney, D.W.6
  • 20
    • 77953927395 scopus 로고    scopus 로고
    • Molecular imaging of HER2-expressing malignant tumors in breast cancer patients using synthetic 111In- or 68Ga-labeled affibody molecules
    • Baum RP, Prasad V, Muller D, Schuchardt C, Orlova A, Wennborg A, et al. Molecular imaging of HER2-expressing malignant tumors in breast cancer patients using synthetic 111In- or 68Ga-labeled affibody molecules. J Nucl Med. 2010; 51: 892-7.
    • (2010) J Nucl Med. , vol.51 , pp. 892-897
    • Baum, R.P.1    Prasad, V.2    Muller, D.3    Schuchardt, C.4    Orlova, A.5    Wennborg, A.6
  • 24
    • 33748637571 scopus 로고    scopus 로고
    • Recent Advances in Free Energy Calculations with a Combination of Molecular Mechanics and Continuum Models
    • Wang J, Hou T, Xu X. Recent Advances in Free Energy Calculations with a Combination of Molecular Mechanics and Continuum Models. Curr Comput Aided Drug Des. 2006; 2: 287-306.
    • (2006) Curr Comput Aided Drug Des. , vol.2 , pp. 287-306
    • Wang, J.1    Hou, T.2    Xu, X.3
  • 25
    • 0034521981 scopus 로고    scopus 로고
    • Calculating Structures and Free Energies of Complex Molecules: Combining Molecular Mechanics and Continuum Models
    • Kollman PA, Massova I, Reyes C, Kuhn B, Huo S, Chong L, et al. Calculating Structures and Free Energies of Complex Molecules: Combining Molecular Mechanics and Continuum Models. Acc Chem Res. 2000; 33: 889-97.
    • (2000) Acc Chem Res. , vol.33 , pp. 889-897
    • Kollman, P.A.1    Massova, I.2    Reyes, C.3    Kuhn, B.4    Huo, S.5    Chong, L.6
  • 26
    • 84857282935 scopus 로고    scopus 로고
    • Free Energy Calculations by the Molecular Mechanics Poisson-Boltzmann Surface Area Method
    • Homeyer N, Gohlke H. Free Energy Calculations by the Molecular Mechanics Poisson-Boltzmann Surface Area Method. Mol Inf. 2012; 31: 114-22.
    • (2012) Mol Inf. , vol.31 , pp. 114-122
    • Homeyer, N.1    Gohlke, H.2
  • 27
    • 0043245780 scopus 로고    scopus 로고
    • Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes
    • Gohlke H, Kiel C, Case DA. Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. J Mol Biol. 2003; 330: 891-913.
    • (2003) J Mol Biol. , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 28
    • 66149146342 scopus 로고    scopus 로고
    • Characterization of domain-peptide interaction interface: a generic structure-based model to decipher the binding specificity of SH3 domains
    • Hou T, Xu Z, Zhang W, McLaughlin WA, Case DA, Xu Y, et al. Characterization of domain-peptide interaction interface: a generic structure-based model to decipher the binding specificity of SH3 domains. Mol Cell Proteomics. 2009; 8: 639-49.
    • (2009) Mol Cell Proteomics. , vol.8 , pp. 639-649
    • Hou, T.1    Xu, Z.2    Zhang, W.3    McLaughlin, W.A.4    Case, D.A.5    Xu, Y.6
  • 29
    • 39049111013 scopus 로고    scopus 로고
    • Characterization of domain-peptide interaction interface: a case study on the amphiphysin-1 SH3 domain
    • Hou T, Zhang W, Case DA, Wang W. Characterization of domain-peptide interaction interface: a case study on the amphiphysin-1 SH3 domain. J Mol Biol. 2008; 376: 1201-14.
    • (2008) J Mol Biol. , vol.376 , pp. 1201-1214
    • Hou, T.1    Zhang, W.2    Case, D.A.3    Wang, W.4
  • 32
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Duan Y, Wu C, Chowdhury S, Lee MC, Xiong G, Zhang W, et al. A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. J Comput Chem. 2003; 24: 1999-2012.
    • (2003) J Comput Chem. , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5    Zhang, W.6
  • 34
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes
    • Ryckaert J-P, Ciccotti G, Berendsen HJC. Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys. 1977; 23: 327-41.
    • (1977) J Comput Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 35
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N [center-dot] log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. Particle mesh Ewald: An N [center-dot] log(N) method for Ewald sums in large systems. J Chem Phys. 1993; 98: 10089-92.
    • (1993) J Chem Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 36
    • 14244273182 scopus 로고    scopus 로고
    • Theory and applications of the generalized Born solvation model in macromolecular simulations
    • Tsui V, Case DA. Theory and applications of the generalized Born solvation model in macromolecular simulations. Biopolymers. 2000; 56: 275-91.
    • (2000) Biopolymers. , vol.56 , pp. 275-291
    • Tsui, V.1    Case, D.A.2
  • 37
    • 0000408363 scopus 로고    scopus 로고
    • Approximate atomic surfaces from linear combinations of pairwise overlaps (L.C.P.O)
    • Weiser Jr, Shenkin PS, Still WC. Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO). J Comput Chem. 1999: 217-30.
    • (1999) J Comput Chem. , pp. 217-230
    • Weiser, J.R.1    Shenkin, P.S.2    Still, W.C.3
  • 41
    • 84878167933 scopus 로고    scopus 로고
    • Unraveling the allosteric inhibition mechanism of PTP1B by free energy calculation based on umbrella sampling
    • Cui W, Cheng YH, Geng LL, Liang DS, Hou TJ, Ji MJ. Unraveling the allosteric inhibition mechanism of PTP1B by free energy calculation based on umbrella sampling. J Chem Inf Model. 2013; 53: 1157-67.
    • (2013) J Chem Inf Model. , vol.53 , pp. 1157-1167
    • Cui, W.1    Cheng, Y.H.2    Geng, L.L.3    Liang, D.S.4    Hou, T.J.5    Ji, M.J.6
  • 42
    • 33947644064 scopus 로고    scopus 로고
    • Molecular dynamics and free energy studies on the wild-type and double mutant HIV-1 protease complexed with amprenavir and two amprenavir-related inhibitors: mechanism for binding and drug resistance
    • Hou T, Yu R. Molecular dynamics and free energy studies on the wild-type and double mutant HIV-1 protease complexed with amprenavir and two amprenavir-related inhibitors: mechanism for binding and drug resistance. J Med Chem. 2007; 50: 1177-88.
    • (2007) J Med Chem. , vol.50 , pp. 1177-1188
    • Hou, T.1    Yu, R.2
  • 43
    • 84876292595 scopus 로고    scopus 로고
    • Computational insights into the selectivity mechanism of APP-IP over matrix metalloproteinases
    • Geng L, Gao J, Cui W, Tang Y, Ji M, Chen B. Computational insights into the selectivity mechanism of APP-IP over matrix metalloproteinases. J Comput Aided Mol Des. 2012; 26: 1327-42.
    • (2012) J Comput Aided Mol Des. , vol.26 , pp. 1327-1342
    • Geng, L.1    Gao, J.2    Cui, W.3    Tang, Y.4    Ji, M.5    Chen, B.6
  • 44
    • 0043245780 scopus 로고    scopus 로고
    • Insights into Protein-Protein Binding by Binding Free Energy Calculation and Free Energy Decomposition for the Ras-Raf and Ras-RalGDS Complexes
    • Gohlke H, Kiel C, Case DA. Insights into Protein-Protein Binding by Binding Free Energy Calculation and Free Energy Decomposition for the Ras-Raf and Ras-RalGDS Complexes. J Mol Biol. 2003; 330: 891-913.
    • (2003) J Mol Biol. , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 45
    • 1842479952 scopus 로고    scopus 로고
    • Exploring protein native states and large-scale conformational changes with a modified generalized born model
    • Onufriev A, Bashford D, Case DA. Exploring protein native states and large-scale conformational changes with a modified generalized born model. Proteins. 2004; 55: 383-94.
    • (2004) Proteins. , vol.55 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 46
    • 33845209913 scopus 로고    scopus 로고
    • A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes
    • Neve RM, Chin K, Fridlyand J, Yeh J, Baehner FL, Fevr T, et al. A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes. Cancer Cell. 2006; 10: 515-27.
    • (2006) Cancer Cell. , vol.10 , pp. 515-527
    • Neve, R.M.1    Chin, K.2    Fridlyand, J.3    Yeh, J.4    Baehner, F.L.5    Fevr, T.6
  • 47
    • 77953408213 scopus 로고    scopus 로고
    • The Expression Patterns of ER, PR, HER2, CK5/6, EGFR, Ki-67 and AR by Immunohistochemical Analysis in Breast Cancer Cell Lines
    • Subik K, Lee JF, Baxter L, Strzepek T, Costello D, Crowley P, et al. The Expression Patterns of ER, PR, HER2, CK5/6, EGFR, Ki-67 and AR by Immunohistochemical Analysis in Breast Cancer Cell Lines. Breast Cancer. 2010; 4: 35-41.
    • (2010) Breast Cancer. , vol.4 , pp. 35-41
    • Subik, K.1    Lee, J.F.2    Baxter, L.3    Strzepek, T.4    Costello, D.5    Crowley, P.6
  • 48
    • 1642493921 scopus 로고    scopus 로고
    • Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data
    • Zheng D, Aramini JM, Montelione GT. Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data. Protein Sci. 2004; 13: 549-54.
    • (2004) Protein Sci. , vol.13 , pp. 549-554
    • Zheng, D.1    Aramini, J.M.2    Montelione, G.T.3
  • 49
    • 84866494853 scopus 로고    scopus 로고
    • The PyM.O.L Molecular Graphics System.
    • Version 1.3r1
    • Schrodinger LLC. The PyMOL Molecular Graphics System, Version 1.3r1. 2010.
    • (2010)
    • Schrodinger, L.L.C.1
  • 50
    • 84906881070 scopus 로고    scopus 로고
    • Label-free quantitative detection of tumor-derived exosomes through surface plasmon resonance imaging
    • Zhu L, Wang K, Cui J, Liu H, Bu X, Ma H, et al. Label-free quantitative detection of tumor-derived exosomes through surface plasmon resonance imaging. Anal Chem. 2014; 86: 8857-64.
    • (2014) Anal Chem. , vol.86 , pp. 8857-8864
    • Zhu, L.1    Wang, K.2    Cui, J.3    Liu, H.4    Bu, X.5    Ma, H.6
  • 51
    • 84904266092 scopus 로고    scopus 로고
    • Cathepsin D serum and urine concentration in superficial and invasive transitional bladder cancer as determined by surface plasmon resonance imaging
    • Gorodkiewicz E, Guszcz T, Roszkowska-Jakimiec W, Kozlowski R. Cathepsin D serum and urine concentration in superficial and invasive transitional bladder cancer as determined by surface plasmon resonance imaging. Oncol Lett. 2014; 8: 1323-7.
    • (2014) Oncol Lett. , vol.8 , pp. 1323-1327
    • Gorodkiewicz, E.1    Guszcz, T.2    Roszkowska-Jakimiec, W.3    Kozlowski, R.4
  • 52
    • 84925240123 scopus 로고    scopus 로고
    • Protein-peptide arrays for detection of specific anti-hepatitis D virus (HDV) genotype 1, 6, and 8 antibodies among HDV-infected patients by surface plasmon resonance imaging
    • Villiers MB, Cortay JC, Cortes S, Bloquel B, Brichler S, Brakha C, et al. Protein-peptide arrays for detection of specific anti-hepatitis D virus (HDV) genotype 1, 6, and 8 antibodies among HDV-infected patients by surface plasmon resonance imaging. J Clin Microbiol. 2015; 53: 1164-71.
    • (2015) J Clin Microbiol. , vol.53 , pp. 1164-1171
    • Villiers, M.B.1    Cortay, J.C.2    Cortes, S.3    Bloquel, B.4    Brichler, S.5    Brakha, C.6
  • 53
    • 84921625704 scopus 로고    scopus 로고
    • Label-free detection microarray for novel peptide ligands screening base on MS-SPRi combination
    • Wang W, Zhang D, Wei Z, Wang Z, Bu X, Yang S, et al. Label-free detection microarray for novel peptide ligands screening base on MS-SPRi combination. Talanta. 2015; 134: 705-11.
    • (2015) Talanta. , vol.134 , pp. 705-711
    • Wang, W.1    Zhang, D.2    Wei, Z.3    Wang, Z.4    Bu, X.5    Yang, S.6
  • 54
    • 84915748441 scopus 로고    scopus 로고
    • Rapid screening of peptide probes through in situ single-bead sequencing microarray
    • Wang W, Wei Z, Zhang D, Ma H, Wang Z, Bu X, et al. Rapid screening of peptide probes through in situ single-bead sequencing microarray. Anal Chem. 2014; 86: 11854-9.
    • (2014) Anal Chem. , vol.86 , pp. 11854-11859
    • Wang, W.1    Wei, Z.2    Zhang, D.3    Ma, H.4    Wang, Z.5    Bu, X.6
  • 55
    • 22344445345 scopus 로고    scopus 로고
    • In vitro characterization of a bivalent anti-HER-2 affibody with potential for radionuclide-based diagnostics
    • Steffen AC, Wikman M, Tolmachev V, Adams GP, Nilsson FY, Stahl S, et al. In vitro characterization of a bivalent anti-HER-2 affibody with potential for radionuclide-based diagnostics. Cancer Biother Radiopharm. 2005; 20: 239-48.
    • (2005) Cancer Biother Radiopharm. , vol.20 , pp. 239-248
    • Steffen, A.C.1    Wikman, M.2    Tolmachev, V.3    Adams, G.P.4    Nilsson, F.Y.5    Stahl, S.6
  • 56
    • 84893510899 scopus 로고    scopus 로고
    • Distribution and accumulation of Cy5.5-labeled thermally cross-linked superparamagnetic iron oxide nanoparticles in the tissues of ICR mice
    • Hue JJ, Lee HJ, Jon S, Nam SY, Yun YW, Kim JS, et al. Distribution and accumulation of Cy5.5-labeled thermally cross-linked superparamagnetic iron oxide nanoparticles in the tissues of ICR mice. J Vet Sci. 2013; 14: 473-9.
    • (2013) J Vet Sci. , vol.14 , pp. 473-479
    • Hue, J.J.1    Lee, H.J.2    Jon, S.3    Nam, S.Y.4    Yun, Y.W.5    Kim, J.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.