메뉴 건너뛰기




Volumn 6, Issue 106, 2016, Pages 104201-104214

Effects of temperature, pH and counterions on the stability of peptide amphiphile nanofiber structures

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPHILES; HYDROGEN BONDS; IONS; MOLECULAR DYNAMICS; MOLECULES; NANOFIBERS; NANOSTRUCTURES; PH EFFECTS; PHASE EQUILIBRIA; POLYPEPTIDES; SELF ASSEMBLY; STABILITY; TEMPERATURE; THERMODYNAMIC STABILITY;

EID: 84994441873     PISSN: None     EISSN: 20462069     Source Type: Journal    
DOI: 10.1039/c6ra21261a     Document Type: Article
Times cited : (40)

References (55)
  • 2
    • 33645504776 scopus 로고    scopus 로고
    • Nano neuro knitting: Peptide nanofiber scaffold for brain repair and axon regeneration with functional return of vision
    • R. Ellis-Behnke Y. Liang S. You D. Tay S. Zhang K. So G. Schneider Nano neuro knitting: peptide nanofiber scaffold for brain repair and axon regeneration with functional return of vision Proc. Natl. Acad. Sci. U. S. A. 2006 103 19 7530
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , Issue.19 , pp. 7530
    • Ellis-Behnke, R.1    Liang, Y.2    You, S.3    Tay, D.4    Zhang, S.5    So, K.6    Schneider, G.7
  • 3
    • 1442281238 scopus 로고    scopus 로고
    • Selective differentiation of neural progenitor cells by high-epitope density nanofibers
    • G. Silva C. Czeisler K. Niece E. Beniash D. Harrington J. Kessler S. Stupp Selective differentiation of neural progenitor cells by high-epitope density nanofibers Science 2004 303 5662 1352 1355
    • (2004) Science , vol.303 , Issue.5662 , pp. 1352-1355
    • Silva, G.1    Czeisler, C.2    Niece, K.3    Beniash, E.4    Harrington, D.5    Kessler, J.6    Stupp, S.7
  • 5
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • J. Hartgerink E. Beniash S. Stupp Self-assembly and mineralization of peptide-amphiphile nanofibers Science 2001 294 5547 1684 1688
    • (2001) Science , vol.294 , Issue.5547 , pp. 1684-1688
    • Hartgerink, J.1    Beniash, E.2    Stupp, S.3
  • 6
    • 0037117498 scopus 로고    scopus 로고
    • Peptide-amphiphile nanofibers: A versatile scaffold for the preparation of self-assembling materials
    • J. Hartgerink E. Beniash S. Stupp Peptide-amphiphile nanofibers: a versatile scaffold for the preparation of self-assembling materials Proc. Natl. Acad. Sci. U. S. A. 2002 99 8 5133 5138
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.8 , pp. 5133-5138
    • Hartgerink, J.1    Beniash, E.2    Stupp, S.3
  • 8
    • 84994440466 scopus 로고    scopus 로고
    • Tuning secondary structure and self-assembly of amphiphilic peptides
    • D. Lowik T. Meijer J. van Hest Tuning secondary structure and self-assembly of amphiphilic peptides Biopolymers 2005 80 4 597
    • (2005) Biopolymers , vol.80 , Issue.4 , pp. 597
    • Lowik, D.1    Meijer, T.2    Van Hest, J.3
  • 10
    • 84891802873 scopus 로고    scopus 로고
    • PH- and thermo-induced morphological changes of an amphiphilic peptide-grafted copolymer in solution
    • M. Yu T. Tang A. Takasu M. Higuchi pH- and thermo-induced morphological changes of an amphiphilic peptide-grafted copolymer in solution Polym. J. 2014 46 1 52 58
    • (2014) Polym. J. , vol.46 , Issue.1 , pp. 52-58
    • Yu, M.1    Tang, T.2    Takasu, A.3    Higuchi, M.4
  • 11
    • 84908376899 scopus 로고    scopus 로고
    • PH and Amphiphilic Structure Direct Supramolecular Behavior in Biofunctional Assemblies
    • T. Moyer J. Finbloom F. Chen D. Toft V. Cryns S. Stupp pH and Amphiphilic Structure Direct Supramolecular Behavior in Biofunctional Assemblies J. Am. Chem. Soc. 2014 136 42 14746 14752
    • (2014) J. Am. Chem. Soc. , vol.136 , Issue.42 , pp. 14746-14752
    • Moyer, T.1    Finbloom, J.2    Chen, F.3    Toft, D.4    Cryns, V.5    Stupp, S.6
  • 12
    • 70549093059 scopus 로고    scopus 로고
    • Self-assembled peptidic nanostructures
    • S. Toksoz M. Guler Self-assembled peptidic nanostructures Nano Today 2009 4 6 458 469
    • (2009) Nano Today , vol.4 , Issue.6 , pp. 458-469
    • Toksoz, S.1    Guler, M.2
  • 14
    • 84970022034 scopus 로고    scopus 로고
    • Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres
    • R. da Silva D. van der Zwaag L. Albertazzi S. Lee E. Meijer S. Stupp Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres Nat. Commun. 2016 7 11561
    • (2016) Nat. Commun. , vol.7 , pp. 11561
    • Da Silva, R.1    Van Der Zwaag, D.2    Albertazzi, L.3    Lee, S.4    Meijer, E.5    Stupp, S.6
  • 17
    • 0038789021 scopus 로고    scopus 로고
    • Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction
    • K. Niece J. Hartgerink J. Donners S. Stupp Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction J. Am. Chem. Soc. 2003 125 24 7146 7147
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.24 , pp. 7146-7147
    • Niece, K.1    Hartgerink, J.2    Donners, J.3    Stupp, S.4
  • 18
    • 79551681262 scopus 로고    scopus 로고
    • Electrostatic effects on nanofiber formation of self-assembling peptide amphiphiles
    • S. Toksoz R. Mammadov A. Tekinay M. Guler Electrostatic effects on nanofiber formation of self-assembling peptide amphiphiles J. Colloid Interface Sci. 2011 356 1 131 137
    • (2011) J. Colloid Interface Sci. , vol.356 , Issue.1 , pp. 131-137
    • Toksoz, S.1    Mammadov, R.2    Tekinay, A.3    Guler, M.4
  • 19
    • 84928684000 scopus 로고    scopus 로고
    • PH-Controlled Hierarchical Self-Assembly of Peptide Amphiphile
    • Y. Chen H. Gan Y. Tong pH-Controlled Hierarchical Self-Assembly of Peptide Amphiphile Macromolecules 2015 48 8 2647 2653
    • (2015) Macromolecules , vol.48 , Issue.8 , pp. 2647-2653
    • Chen, Y.1    Gan, H.2    Tong, Y.3
  • 21
    • 84881084547 scopus 로고    scopus 로고
    • The effect of pH on the self-assembly of a collagen derived peptide amphiphile
    • A. Dehsorkhi V. Castelletto I. Hamley J. Adamcik R. Mezzenga The effect of pH on the self-assembly of a collagen derived peptide amphiphile Soft Matter 2013 9 26 6033 6036
    • (2013) Soft Matter , vol.9 , Issue.26 , pp. 6033-6036
    • Dehsorkhi, A.1    Castelletto, V.2    Hamley, I.3    Adamcik, J.4    Mezzenga, R.5
  • 22
    • 67649202811 scopus 로고    scopus 로고
    • Self-assembly of Peptide-Amphiphile C-12-A beta (11-17) into Nanofibrils
    • M. Deng D. Yu Y. Hou Y. Wang Self-assembly of Peptide-Amphiphile C-12-A beta (11-17) into Nanofibrils J. Phys. Chem. B 2009 113 25 8539 8544
    • (2009) J. Phys. Chem. B , vol.113 , Issue.25 , pp. 8539-8544
    • Deng, M.1    Yu, D.2    Hou, Y.3    Wang, Y.4
  • 23
    • 84881562356 scopus 로고    scopus 로고
    • The Robust Hydrogel Hierarchically Assembled from a pH Sensitive Peptide Amphiphile Based on Silk Fibroin
    • H. Guo J. Zhang T. Xu Z. Zhang J. Yao Z. Shao The Robust Hydrogel Hierarchically Assembled from a pH Sensitive Peptide Amphiphile Based on Silk Fibroin Biomacromolecules 2013 14 8 2733 2738
    • (2013) Biomacromolecules , vol.14 , Issue.8 , pp. 2733-2738
    • Guo, H.1    Zhang, J.2    Xu, T.3    Zhang, Z.4    Yao, J.5    Shao, Z.6
  • 24
    • 79955876659 scopus 로고    scopus 로고
    • Interfiber interactions alter the stiffness of gels formed by supramolecular self-assembled nanofibers
    • Y. Dagdas A. Tombuloglu A. Tekinay A. Dana M. Guler Interfiber interactions alter the stiffness of gels formed by supramolecular self-assembled nanofibers Soft Matter 2011 7 7 3524 3532
    • (2011) Soft Matter , vol.7 , Issue.7 , pp. 3524-3532
    • Dagdas, Y.1    Tombuloglu, A.2    Tekinay, A.3    Dana, A.4    Guler, M.5
  • 25
    • 84904994538 scopus 로고    scopus 로고
    • Mechanism of the pH-Controlled Self-Assembly of Nanofibers from Peptide Amphiphiles
    • Y. Cote I. Fu E. Dobson J. Goldberger H. Nguyen J. Shen Mechanism of the pH-Controlled Self-Assembly of Nanofibers from Peptide Amphiphiles J. Phys. Chem. C 2014 118 29 16272 16278
    • (2014) J. Phys. Chem. C , vol.118 , Issue.29 , pp. 16272-16278
    • Cote, Y.1    Fu, I.2    Dobson, E.3    Goldberger, J.4    Nguyen, H.5    Shen, J.6
  • 26
    • 84903986775 scopus 로고    scopus 로고
    • Role of Hydrophobicity on Self-Assembly by Peptide Amphiphiles via Molecular Dynamics Simulations
    • I. Fu C. Markegard B. Chu H. Nguyen Role of Hydrophobicity on Self-Assembly by Peptide Amphiphiles via Molecular Dynamics Simulations Langmuir 2014 30 26 7745 7754
    • (2014) Langmuir , vol.30 , Issue.26 , pp. 7745-7754
    • Fu, I.1    Markegard, C.2    Chu, B.3    Nguyen, H.4
  • 27
    • 84884930249 scopus 로고    scopus 로고
    • The Role of Electrostatics and Temperature on Morphological Transitions of Hydrogel Nanostructures Self-Assembled by Peptide Amphiphiles Via Molecular Dynamics Simulations
    • I. Fu C. Markegard B. Chu H. Nguyen The Role of Electrostatics and Temperature on Morphological Transitions of Hydrogel Nanostructures Self-Assembled by Peptide Amphiphiles Via Molecular Dynamics Simulations Adv. Healthcare Mater. 2013 2 10 1388 1400
    • (2013) Adv. Healthcare Mater. , vol.2 , Issue.10 , pp. 1388-1400
    • Fu, I.1    Markegard, C.2    Chu, B.3    Nguyen, H.4
  • 28
    • 84938912056 scopus 로고    scopus 로고
    • Molecular dynamics simulations of self-assembled peptide amphiphile based cylindrical nanofibers
    • E. Tekin Molecular dynamics simulations of self-assembled peptide amphiphile based cylindrical nanofibers RSC Adv. 2015 5 82 66582 66590
    • (2015) RSC Adv. , vol.5 , Issue.82 , pp. 66582-66590
    • Tekin, E.1
  • 29
    • 84907611160 scopus 로고    scopus 로고
    • Odd-even effect in the potential energy of the self-assembled peptide amphiphiles
    • E. Tekin Odd-even effect in the potential energy of the self-assembled peptide amphiphiles Chem. Phys. Lett. 2014 614 204 206
    • (2014) Chem. Phys. Lett. , vol.614 , pp. 204-206
    • Tekin, E.1
  • 30
    • 77951682263 scopus 로고    scopus 로고
    • Tuning Supramolecular Rigidity of Peptide Fibers through Molecular Structure
    • E. Pashuck H. Cui S. Stupp Tuning Supramolecular Rigidity of Peptide Fibers through Molecular Structure J. Am. Chem. Soc. 2010 132 17 6041 6046
    • (2010) J. Am. Chem. Soc. , vol.132 , Issue.17 , pp. 6041-6046
    • Pashuck, E.1    Cui, H.2    Stupp, S.3
  • 31
    • 0001305589 scopus 로고
    • The viscosity of SPC and SPC/E water at 277-K and 300-K
    • P. Smith W. Vangunsteren The viscosity of SPC and SPC/E water at 277-K and 300-K Chem. Phys. Lett. 1993 215 4 315 318
    • (1993) Chem. Phys. Lett. , vol.215 , Issue.4 , pp. 315-318
    • Smith, P.1    Vangunsteren, W.2
  • 32
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess C. Kutzner D. van der Spoel E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 2008 4 3 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 33
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • C. Oostenbrink A. Villa A. Mark W. Van Gunsteren A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6 J. Comput. Chem. 2004 25 13 1656 1676
    • (2004) J. Comput. Chem. , vol.25 , Issue.13 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.3    Van Gunsteren, W.4
  • 34
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • O. Berger O. Edholm F. Jahnig Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature Biophys. J. 1997 72 5 2002 2013
    • (1997) Biophys. J. , vol.72 , Issue.5 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 35
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • B. Hess H. Bekker H. Berendsen J. Fraaije LINCS: a linear constraint solver for molecular simulations J. Comput. Chem. 1997 18 12 1463 1472
    • (1997) J. Comput. Chem. , vol.18 , Issue.12 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.3    Fraaije, J.4
  • 36
    • 33846823909 scopus 로고
    • Particle mesh Ewald-an n log(n) method for Ewald sums in large systems
    • T. Darden D. York L. Pedersen Particle mesh Ewald-an n log(n) method for Ewald sums in large systems J. Chem. Phys. 1993 98 12 10089 10092
    • (1993) J. Chem. Phys. , vol.98 , Issue.12 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 37
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • G. Bussi D. Donadio M. Parrinello Canonical sampling through velocity rescaling J. Chem. Phys. 2007 126 1 014101 014107
    • (2007) J. Chem. Phys. , vol.126 , Issue.1 , pp. 014101-014107
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 38
    • 0019707626 scopus 로고
    • Polymorphic transitions in single-crystals-a new molecular-dynamics method
    • M. Parrinello A. Rahman Polymorphic transitions in single-crystals-a new molecular-dynamics method J. Appl. Phys. 1981 52 12 7182 7190
    • (1981) J. Appl. Phys. , vol.52 , Issue.12 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 40
    • 84879107554 scopus 로고    scopus 로고
    • Rational Design of Particle Mesh Ewald Compatible Lennard-Jones Parameters for +2 Metal Cations in Explicit Solvent
    • P. Li B. P. Roberts D. K. Chakravorty K. M. Merz Rational Design of Particle Mesh Ewald Compatible Lennard-Jones Parameters for +2 Metal Cations in Explicit Solvent J. Chem. Theory Comput. 2013 9 6 2733 2748
    • (2013) J. Chem. Theory Comput. , vol.9 , Issue.6 , pp. 2733-2748
    • Li, P.1    Roberts, B.P.2    Chakravorty, D.K.3    Merz, K.M.4
  • 41
    • 84892597525 scopus 로고    scopus 로고
    • Taking into Account the Ion-induced Dipole Interaction in the Nonbonded Model of Ions
    • P. Li K. M. Merz Taking into Account the Ion-induced Dipole Interaction in the Nonbonded Model of Ions J. Chem. Theory Comput. 2014 10 1 289 297
    • (2014) J. Chem. Theory Comput. , vol.10 , Issue.1 , pp. 289-297
    • Li, P.1    Merz, K.M.2
  • 42
    • 84872697347 scopus 로고    scopus 로고
    • Force fields for divalent cations based on single-ion and ion-pair properties
    • S. Mamatkulov M. Fyta R. Netz Force fields for divalent cations based on single-ion and ion-pair properties J. Chem. Phys. 2013 138 2 024505
    • (2013) J. Chem. Phys. , vol.138 , Issue.2 , pp. 024505
    • Mamatkulov, S.1    Fyta, M.2    Netz, R.3
  • 43
    • 84978818147 scopus 로고    scopus 로고
    • Divalent Ion Dependent Conformational Changes in an RNA Stem-Loop Observed by Molecular Dynamics
    • C. Bergonzo K. B. Hall T. E. Cheatham Divalent Ion Dependent Conformational Changes in an RNA Stem-Loop Observed by Molecular Dynamics J. Chem. Theory Comput. 2016 12 7 3382 3389
    • (2016) J. Chem. Theory Comput. , vol.12 , Issue.7 , pp. 3382-3389
    • Bergonzo, C.1    Hall, K.B.2    Cheatham, T.E.3
  • 44
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure-pattern-recognition of hydrogen-bonded and geometrical features
    • W. Kabsch C. Sander Dictionary of protein secondary structure-pattern-recognition of hydrogen-bonded and geometrical features Biopolymers 1983 22 12 2577 2637
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 45
    • 0025179832 scopus 로고
    • Protein folding
    • T. Creighton Protein folding Biochem. J. 1990 270 1 1 16
    • (1990) Biochem. J. , vol.270 , Issue.1 , pp. 1-16
    • Creighton, T.1
  • 46
    • 84887956341 scopus 로고    scopus 로고
    • Free-Energy Landscape for Peptide Amphiphile Self-Assembly: Stepwise versus Continuous Assembly Mechanisms
    • T. Yu G. Schatz Free-Energy Landscape for Peptide Amphiphile Self-Assembly: Stepwise versus Continuous Assembly Mechanisms J. Phys. Chem. B 2013 117 45 14059 14064
    • (2013) J. Phys. Chem. B , vol.117 , Issue.45 , pp. 14059-14064
    • Yu, T.1    Schatz, G.2
  • 47
    • 84937789196 scopus 로고    scopus 로고
    • Supramolecular chirality in self-assembled peptide amphiphile nanostructures
    • R. Garifullin M. Guler Supramolecular chirality in self-assembled peptide amphiphile nanostructures Chem. Commun. 2015 51 62 12470 12473
    • (2015) Chem. Commun. , vol.51 , Issue.62 , pp. 12470-12473
    • Garifullin, R.1    Guler, M.2
  • 48
    • 4143141192 scopus 로고    scopus 로고
    • Self-assembling peptides and proteins for nanotechnological applications
    • K. Rajagopal J. Schneider Self-assembling peptides and proteins for nanotechnological applications Curr. Opin. Struct. Biol. 2004 14 4 480 486
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , Issue.4 , pp. 480-486
    • Rajagopal, K.1    Schneider, J.2
  • 52
    • 14644438367 scopus 로고    scopus 로고
    • Presentation and recognition of biotin on nanofibers formed by branched peptide amphiphiles
    • M. Guler S. Soukasene J. Hulvat S. Stupp Presentation and recognition of biotin on nanofibers formed by branched peptide amphiphiles Nano Lett. 2005 5 2 249 252
    • (2005) Nano Lett. , vol.5 , Issue.2 , pp. 249-252
    • Guler, M.1    Soukasene, S.2    Hulvat, J.3    Stupp, S.4
  • 54
    • 84929171965 scopus 로고    scopus 로고
    • Oligonucleotide Delivery with Cell Surface Binding and Cell Penetrating Peptide Amphiphile Nanospheres
    • D. Mumcuoglu M. Sardan T. Tekinay M. Guler A. Tekinay Oligonucleotide Delivery with Cell Surface Binding and Cell Penetrating Peptide Amphiphile Nanospheres Mol. Pharm. 2015 12 5 1584 1591
    • (2015) Mol. Pharm. , vol.12 , Issue.5 , pp. 1584-1591
    • Mumcuoglu, D.1    Sardan, M.2    Tekinay, T.3    Guler, M.4    Tekinay, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.