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Volumn 30, Issue 26, 2014, Pages 7745-7754

Role of hydrophobicity on self-assembly by peptide amphiphiles via molecular dynamics simulations

Author keywords

[No Author keywords available]

Indexed keywords

HYDROPHOBICITY; MEDICAL APPLICATIONS; MOLECULAR DYNAMICS; NANOSTRUCTURES; SELF ASSEMBLY;

EID: 84903986775     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la5012988     Document Type: Article
Times cited : (54)

References (60)
  • 1
    • 0038387390 scopus 로고    scopus 로고
    • The Dawning Era of Polymer Therapeutics
    • Duncan, R. The Dawning Era of Polymer Therapeutics Nat. Rev. Drug Discovery 2003, 2, 347-360
    • (2003) Nat. Rev. Drug Discovery , vol.2 , pp. 347-360
    • Duncan, R.1
  • 2
    • 33847070591 scopus 로고    scopus 로고
    • Synthesis of Bio-Inspired Hybrid Polymers Using Peptide Synthesis and Protein Engineering
    • Springer-Verlag: Berlin/Heidelberg
    • Löwik, D. W.; Ayres, L.; Smeenk, J. M.; van Hest, J. C. M. Synthesis of Bio-Inspired Hybrid Polymers Using Peptide Synthesis and Protein Engineering. In Advances in Polymer Science; Springer-Verlag: Berlin/Heidelberg, 2006; Vol. 202, pp 19-52.
    • (2006) Advances in Polymer Science , vol.202 , pp. 19-52
    • Löwik, D.W.1    Ayres, L.2    Smeenk, J.M.3    Van Hest, J.C.M.4
  • 4
    • 45249104205 scopus 로고    scopus 로고
    • Cell Encapsulation in Biodegradable Hydrogels for Tissue Engineering Applications
    • Nicodemus, G. D.; Bryant, S. J. Cell Encapsulation in Biodegradable Hydrogels for Tissue Engineering Applications Tissue Eng., Part B: Reviews 2008, 14, 149-165
    • (2008) Tissue Eng., Part B: Reviews , vol.14 , pp. 149-165
    • Nicodemus, G.D.1    Bryant, S.J.2
  • 5
    • 77950342360 scopus 로고    scopus 로고
    • Self-Assembly of Peptide Amphiphiles: From Molecules to Nanostructures to Biomaterials
    • Cui, H.; Webber, M. J.; Stupp, S. I. Self-Assembly of Peptide Amphiphiles: From Molecules to Nanostructures to Biomaterials Biopolymers 2010, 94, 1-18
    • (2010) Biopolymers , vol.94 , pp. 1-18
    • Cui, H.1    Webber, M.J.2    Stupp, S.I.3
  • 8
    • 0036897817 scopus 로고    scopus 로고
    • Design of Nanostructured Biological Materials Through Self-Assembly of Peptides and Proteins
    • Zhang, S.; Marini, D. M.; Hwang, W.; Santoso, S. Design of Nanostructured Biological Materials Through Self-Assembly of Peptides and Proteins Curr. Opin. Chem. Biol. 2002, 6, 865-871
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 865-871
    • Zhang, S.1    Marini, D.M.2    Hwang, W.3    Santoso, S.4
  • 9
    • 0035941074 scopus 로고    scopus 로고
    • Self-Assembly and Mineralization of Peptide-Amphiphile Nanofibers
    • Hartgerink, J. D.; Beniash, E.; Stupp, S. I. Self-Assembly and Mineralization of Peptide-Amphiphile Nanofibers Science 2001, 294, 1684-1688
    • (2001) Science , vol.294 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 10
    • 0037117498 scopus 로고    scopus 로고
    • Peptide-Amphiphile Nanofibers: A Versatile Scaffold for the Preparation of Self-Assembling Materials
    • Hartgerink, J. D.; Beniash, E.; Stupp, S. I. Peptide-Amphiphile Nanofibers: a Versatile Scaffold for the Preparation of Self-Assembling Materials Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 5133-5138
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5133-5138
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 11
    • 11144225434 scopus 로고    scopus 로고
    • Biological-Synthetic Hybrid Block Copolymers: Combining the Best from Two Worlds
    • Klok, H.-A. Biological-Synthetic Hybrid Block Copolymers: Combining the Best From Two Worlds J. Polym. Sci. A: Polym. Chem. 2004, 43, 1-17
    • (2004) J. Polym. Sci. A: Polym. Chem. , vol.43 , pp. 1-17
    • Klok, H.-A.1
  • 12
    • 80053578944 scopus 로고    scopus 로고
    • Structural Properties of Soluble Peptide Amphiphile Micelles
    • Trent, A.; Marullo, R.; Lin, B.; Black, M.; Tirrell, M. Structural Properties of Soluble Peptide Amphiphile Micelles Soft Matter 2011, 7, 9572
    • (2011) Soft Matter , vol.7 , pp. 9572
    • Trent, A.1    Marullo, R.2    Lin, B.3    Black, M.4    Tirrell, M.5
  • 13
    • 84858766244 scopus 로고    scopus 로고
    • Tunable Self-Assembled Peptide Amphiphile Nanostructures
    • Meng, Q.; Kou, Y.; Ma, X.; Liang, Y.; Guo, L.; Ni, C.; Liu, K. Tunable Self-Assembled Peptide Amphiphile Nanostructures Langmuir 2012, 28, 5017-5022
    • (2012) Langmuir , vol.28 , pp. 5017-5022
    • Meng, Q.1    Kou, Y.2    Ma, X.3    Liang, Y.4    Guo, L.5    Ni, C.6    Liu, K.7
  • 14
    • 40549086613 scopus 로고    scopus 로고
    • Molecular Simulation Study of Peptide Amphiphile Self-Assembly
    • Velichko, Y. S.; Stupp, S. I.; de la Cruz, M. O. Molecular Simulation Study of Peptide Amphiphile Self-Assembly J. Phys. Chem. B 2008, 112, 2326-2334
    • (2008) J. Phys. Chem. B , vol.112 , pp. 2326-2334
    • Velichko, Y.S.1    Stupp, S.I.2    De La Cruz, M.O.3
  • 15
    • 3142779302 scopus 로고    scopus 로고
    • Electrostatically-Directed Self-Assembly of Cylindrical Peptide Amphiphile Nanostructures
    • Tsonchev, S.; Schatz, G. C.; Ratner, M. A. Electrostatically-Directed Self-Assembly of Cylindrical Peptide Amphiphile Nanostructures J. Phys. Chem. B 2004, 108, 8817-8822
    • (2004) J. Phys. Chem. B , vol.108 , pp. 8817-8822
    • Tsonchev, S.1    Schatz, G.C.2    Ratner, M.A.3
  • 16
    • 80052301140 scopus 로고    scopus 로고
    • Design Properties of Hydrogel Tissue-Engineering Scaffolds
    • Zhu, J.; Marchant, R. E. Design Properties of Hydrogel Tissue-Engineering Scaffolds Expert Rev. Med. Devices 2011, 8, 607-626
    • (2011) Expert Rev. Med. Devices , vol.8 , pp. 607-626
    • Zhu, J.1    Marchant, R.E.2
  • 17
    • 77951218278 scopus 로고    scopus 로고
    • Engineering Hydrogels as Extracellular Matrix Mimics
    • Geckil, H.; Xu, F.; Zhang, X.; Moon, S.; Demirci, U. Engineering Hydrogels as Extracellular Matrix Mimics Nanomedicine 2010, 5, 469-484
    • (2010) Nanomedicine , vol.5 , pp. 469-484
    • Geckil, H.1    Xu, F.2    Zhang, X.3    Moon, S.4    Demirci, U.5
  • 18
    • 77956012920 scopus 로고    scopus 로고
    • Self-Assembly Behavior of Peptide Amphiphiles (PAs) with Different Length of Hydrophobic Alkyl Tails
    • Xu, X.-D.; Jin, Y.; Liu, Y.; Zhang, X.-Z.; Zhuo, R.-X. Self-Assembly Behavior of Peptide Amphiphiles (PAs) with Different Length of Hydrophobic Alkyl Tails Colloids Surf., B 2010, 81, 329-335
    • (2010) Colloids Surf., B , vol.81 , pp. 329-335
    • Xu, X.-D.1    Jin, Y.2    Liu, Y.3    Zhang, X.-Z.4    Zhuo, R.-X.5
  • 19
    • 77951682263 scopus 로고    scopus 로고
    • Tuning Supramolecular Rigidity of Peptide Fibers Through Molecular Structure
    • Pashuck, E. T.; Cui, H.; Stupp, S. I. Tuning Supramolecular Rigidity of Peptide Fibers Through Molecular Structure J. Am. Chem. Soc. 2010, 132, 6041-6046
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6041-6046
    • Pashuck, E.T.1    Cui, H.2    Stupp, S.I.3
  • 20
    • 79958110760 scopus 로고    scopus 로고
    • Effect of the Peptide Secondary Structure on the Peptide Amphiphile Supramolecular Structure and Interactions
    • Missirlis, D.; Chworos, A.; Fu, C. J.; Khant, H. A.; Krogstad, D. V.; Tirrell, M. Effect of the Peptide Secondary Structure on the Peptide Amphiphile Supramolecular Structure and Interactions Langmuir 2011, 27, 6163-6170
    • (2011) Langmuir , vol.27 , pp. 6163-6170
    • Missirlis, D.1    Chworos, A.2    Fu, C.J.3    Khant, H.A.4    Krogstad, D.V.5    Tirrell, M.6
  • 21
    • 80555144149 scopus 로고    scopus 로고
    • Self-Assembly of Short Peptide Amphiphiles: The Cooperative Effect of Hydrophobic Interaction and Hydrogen Bonding
    • Han, S.; Cao, S.; Wang, Y.; Wang, J.; Xia, D.; Xu, H.; Zhao, X.; Lu, J. R. Self-Assembly of Short Peptide Amphiphiles: the Cooperative Effect of Hydrophobic Interaction and Hydrogen Bonding Chem.-Eur. J. 2011, 17, 13095-13102
    • (2011) Chem.-Eur. J. , vol.17 , pp. 13095-13102
    • Han, S.1    Cao, S.2    Wang, Y.3    Wang, J.4    Xia, D.5    Xu, H.6    Zhao, X.7    Lu, J.R.8
  • 23
    • 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
    • Fu, I. W.; Markegard, C. B.; Chu, B. K.; Nguyen, H. D. 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, 1388-1400
    • (2013) Adv. Healthcare Mater. , vol.2 , pp. 1388-1400
    • Fu, I.W.1    Markegard, C.B.2    Chu, B.K.3    Nguyen, H.D.4
  • 24
    • 7244253280 scopus 로고    scopus 로고
    • Solvent Effects on the Conformational Transition of a Model Polyalanine Peptide
    • Nguyen, H. D.; Marchut, A. J.; Hall, C. K. Solvent Effects on the Conformational Transition of a Model Polyalanine Peptide Protein Sci. 2004, 13, 2909-2924
    • (2004) Protein Sci. , vol.13 , pp. 2909-2924
    • Nguyen, H.D.1    Marchut, A.J.2    Hall, C.K.3
  • 26
    • 84866315633 scopus 로고    scopus 로고
    • Modeling the Self-Assembly of Peptide Amphiphiles into Fibers Using Coarse-Grained Molecular Dynamics
    • Lee, O.-S.; Cho, V.; Schatz, G. C. Modeling the Self-Assembly of Peptide Amphiphiles Into Fibers Using Coarse-Grained Molecular Dynamics Nano Lett. 2012, 12, 4907-4913
    • (2012) Nano Lett. , vol.12 , pp. 4907-4913
    • Lee, O.-S.1    Cho, V.2    Schatz, G.C.3
  • 27
    • 79551681262 scopus 로고    scopus 로고
    • Electrostatic Effects on Nanofiber Formation of Self-Assembling Peptide Amphiphiles
    • Toksoz, S.; Mammadov, R.; Tekinay, A. B.; Guler, M. O. Electrostatic Effects on Nanofiber Formation of Self-Assembling Peptide Amphiphiles J. Colloid Interface Sci. 2011, 356, 131-137
    • (2011) J. Colloid Interface Sci. , vol.356 , pp. 131-137
    • Toksoz, S.1    Mammadov, R.2    Tekinay, A.B.3    Guler, M.O.4
  • 29
    • 79952585497 scopus 로고    scopus 로고
    • Atomistic Molecular Dynamics Simulations of Peptide Amphiphile Self-Assembly into Cylindrical Nanofibers
    • Lee, O.-S.; Stupp, S. I.; Schatz, G. C. Atomistic Molecular Dynamics Simulations of Peptide Amphiphile Self-Assembly Into Cylindrical Nanofibers J. Am. Chem. Soc. 2011, 133, 3677-3683
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 3677-3683
    • Lee, O.-S.1    Stupp, S.I.2    Schatz, G.C.3
  • 30
    • 0027080909 scopus 로고
    • Atomic Solvation Parameters Applied to Molecular Dynamics of Proteins in Solution
    • Wesson, L.; Eisenberg, D. Atomic Solvation Parameters Applied to Molecular Dynamics of Proteins in Solution Protein Sci. 1992, 1, 227-235
    • (1992) Protein Sci. , vol.1 , pp. 227-235
    • Wesson, L.1    Eisenberg, D.2
  • 31
    • 2442666531 scopus 로고    scopus 로고
    • Solvation Free Energies and Transfer Free Energies for Amino Acids from Hydrophobic Solution to Water Solution from a Very Simple Residue Model
    • Gu, W.; Rahi, S. J.; Helms, V. Solvation Free Energies and Transfer Free Energies for Amino Acids From Hydrophobic Solution to Water Solution From a Very Simple Residue Model J. Phys. Chem. B 2004, 108, 5806-5814
    • (2004) J. Phys. Chem. B , vol.108 , pp. 5806-5814
    • Gu, W.1    Rahi, S.J.2    Helms, V.3
  • 32
    • 77954580346 scopus 로고    scopus 로고
    • Amphiphilic Peptide-Polymer Conjugates Based on the Coiled-Coil Helix Bundle
    • Shu, J. Y.; Huang, Y.-J.; Tan, C.; Presley, A. D.; Chang, J.; Xu, T. Amphiphilic Peptide-Polymer Conjugates Based on the Coiled-Coil Helix Bundle Biomacromolecules 2010, 11, 1443-1452
    • (2010) Biomacromolecules , vol.11 , pp. 1443-1452
    • Shu, J.Y.1    Huang, Y.-J.2    Tan, C.3    Presley, A.D.4    Chang, J.5    Xu, T.6
  • 33
    • 79960217005 scopus 로고    scopus 로고
    • Helix Stabilization of Poly(Ethylene Glycol)-Peptide Conjugates
    • Jain, A.; Ashbaugh, H. S. Helix Stabilization of Poly(Ethylene Glycol)-Peptide Conjugates Biomacromolecules 2011, 12, 2729-2734
    • (2011) Biomacromolecules , vol.12 , pp. 2729-2734
    • Jain, A.1    Ashbaugh, H.S.2
  • 35
    • 0348244547 scopus 로고    scopus 로고
    • All-Atom Empirical Force Field for Nucleic Acids: I. Parameter Optimization Based on Small Molecule and Condensed Phase Macromolecular Target Data
    • Foloppe, N.; MacKerell, A. D., Jr. All-Atom Empirical Force Field for Nucleic Acids: I. Parameter Optimization Based on Small Molecule and Condensed Phase Macromolecular Target Data J. Comput. Chem. 2000, 21, 19
    • (2000) J. Comput. Chem. , vol.21 , pp. 19
    • Foloppe, N.1    Mackerell, Jr.A.D.2
  • 36
    • 0000214231 scopus 로고    scopus 로고
    • All-Atom Empirical Force Field for Nucleic Acids: II. Application to Molecular Dynamics Simulations of DNA and RNA in Solution
    • MacKerell, A. D., Jr; Banavali, N. K. All-Atom Empirical Force Field for Nucleic Acids: II. Application to Molecular Dynamics Simulations of DNA and RNA in Solution J. Comput. Chem. 2000, 21, 16
    • (2000) J. Comput. Chem. , vol.21 , pp. 16
    • Mackerell, Jr.A.D.1    Banavali, N.K.2
  • 38
    • 0024359551 scopus 로고
    • Thermal Stabilities of Globular Proteins
    • Dill, K. A.; Alonso, D. O. V.; Hutchinson, K. Thermal Stabilities of Globular Proteins Biochemistry 1989, 28, 5439-5449
    • (1989) Biochemistry , vol.28 , pp. 5439-5449
    • Dill, K.A.1    Alonso, D.O.V.2    Hutchinson, K.3
  • 39
    • 0034272188 scopus 로고    scopus 로고
    • Temperature Dependence of Hydrophobic Interactions: A Mean Force Perspective, Effects of Water Density, and Nonadditivity of Thermodynamic Signatures
    • Shimizu, S.; Chan, H. S. Temperature Dependence of Hydrophobic Interactions: a Mean Force Perspective, Effects of Water Density, and Nonadditivity of Thermodynamic Signatures J. Chem. Phys. 2000, 113, 4683-4700
    • (2000) J. Chem. Phys. , vol.113 , pp. 4683-4700
    • Shimizu, S.1    Chan, H.S.2
  • 40
    • 0028347939 scopus 로고
    • A Simplified Amino Acid Potential for Use in Structure Predictions of Proteins
    • Wallqvist, A.; Ullner, M. A Simplified Amino Acid Potential for Use in Structure Predictions of Proteins Proteins 1994, 18, 267-280
    • (1994) Proteins , vol.18 , pp. 267-280
    • Wallqvist, A.1    Ullner, M.2
  • 41
    • 36849126204 scopus 로고
    • Studies in Molecular Dynamics. I. General Method
    • Alder, B. J.; Wainwright, T. E. Studies in Molecular Dynamics. I. General Method J. Chem. Phys. 1959, 31, 459-466
    • (1959) J. Chem. Phys. , vol.31 , pp. 459-466
    • Alder, B.J.1    Wainwright, T.E.2
  • 42
    • 36749107785 scopus 로고
    • Molecular Dynamics Simulations at Constant Pressure and/or Temperature
    • Andersen, H. Molecular Dynamics Simulations at Constant Pressure and/or Temperature J. Chem. Phys. 1980, 72, 2384-2393
    • (1980) J. Chem. Phys. , vol.72 , pp. 2384-2393
    • Andersen, H.1
  • 43
    • 0029619259 scopus 로고
    • Knowledge-Based Protein Secondary Structure Assignment
    • Frishman, D.; Argos, P. Knowledge-Based Protein Secondary Structure Assignment Proteins 1995, 23, 566-579
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 44
    • 0001616080 scopus 로고    scopus 로고
    • Replica-Exchange Molecular Dynamics Method for Protein Folding
    • Sugita, Y.; Okamoto, Y. Replica-Exchange Molecular Dynamics Method for Protein Folding Chem. Phys. Lett. 1999, 314, 141-151
    • (1999) Chem. Phys. Lett. , vol.314 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 45
    • 0015987426 scopus 로고
    • Prediction of Protein Conformation
    • Chou, P. Y.; Fasman, G. D. Prediction of Protein Conformation Biochemistry 1974, 13, 222-245
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 46
    • 0018093765 scopus 로고
    • Conformational Preferences of Amino-Acids in Globular Proteins
    • Levitt, M. Conformational Preferences of Amino-Acids in Globular Proteins Biochemistry 1978, 17, 4277-4284
    • (1978) Biochemistry , vol.17 , pp. 4277-4284
    • Levitt, M.1
  • 48
    • 0023581602 scopus 로고
    • Applications of Thermally Reversible Polymers and Hydrogels in Therapeutics and Diagnostics
    • Hoffman, A. S. Applications of Thermally Reversible Polymers and Hydrogels in Therapeutics and Diagnostics J. Controlled Release 1987, 6, 297-305
    • (1987) J. Controlled Release , vol.6 , pp. 297-305
    • Hoffman, A.S.1
  • 49
    • 77949898500 scopus 로고    scopus 로고
    • Drug Release Kinetics and Transport Mechanisms of Non-Degradable and Degradable Polymeric Delivery Systems
    • Fu, Y.; Kao, W. J. Drug Release Kinetics and Transport Mechanisms of Non-Degradable and Degradable Polymeric Delivery Systems Expert Opin. Drug Delivery 2010, 7, 429-444
    • (2010) Expert Opin. Drug Delivery , vol.7 , pp. 429-444
    • Fu, Y.1    Kao, W.J.2
  • 50
    • 77954179473 scopus 로고    scopus 로고
    • Design and Evaluation of Peptide Amphiphiles with Different Hydrophobic Blocks for Simultaneous Delivery of Drugs and Genes
    • Wiradharma, N.; Tong, Y. W.; Yang, Y.-Y. Design and Evaluation of Peptide Amphiphiles with Different Hydrophobic Blocks for Simultaneous Delivery of Drugs and Genes Macromol. Rapid Commun. 2010, 31, 1212-1217
    • (2010) Macromol. Rapid Commun. , vol.31 , pp. 1212-1217
    • Wiradharma, N.1    Tong, Y.W.2    Yang, Y.-Y.3
  • 51
    • 0037132592 scopus 로고    scopus 로고
    • Responsive Hydrogels from the Intramolecular Folding and Self-Assembly of a Designed Peptide
    • Schneider, J. P.; Pochan, D. J.; Ozbas, B.; Rajagopal, K.; Pakstis, L.; Kretsinger, J. Responsive Hydrogels From the Intramolecular Folding and Self-Assembly of a Designed Peptide J. Am. Chem. Soc. 2002, 124, 15030-15037
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 15030-15037
    • Schneider, J.P.1    Pochan, D.J.2    Ozbas, B.3    Rajagopal, K.4    Pakstis, L.5    Kretsinger, J.6
  • 52
    • 84869407296 scopus 로고    scopus 로고
    • Effect of Peptide and Guest Charge on the Structural, Mechanical and Release Properties of B-Sheet Forming Peptides
    • Roberts, D.; Rochas, C.; Saiani, A.; Miller, A. F. Effect of Peptide and Guest Charge on the Structural, Mechanical and Release Properties of B-Sheet Forming Peptides Langmuir 2012, 28, 16196-16206
    • (2012) Langmuir , vol.28 , pp. 16196-16206
    • Roberts, D.1    Rochas, C.2    Saiani, A.3    Miller, A.F.4
  • 53
    • 4744350913 scopus 로고    scopus 로고
    • Salt-Triggered Peptide Folding and Consequent Self-Assembly into Hydrogels with Tunable Modulus
    • Ozbas, B.; Kretsinger, J.; Rajagopal, K.; Schneider, J. P.; Pochan, D. J. Salt-Triggered Peptide Folding and Consequent Self-Assembly Into Hydrogels with Tunable Modulus Macromolecules 2004, 37, 7331-7337
    • (2004) Macromolecules , vol.37 , pp. 7331-7337
    • Ozbas, B.1    Kretsinger, J.2    Rajagopal, K.3    Schneider, J.P.4    Pochan, D.J.5
  • 54
    • 79955876659 scopus 로고    scopus 로고
    • Interfiber Interactions Alter the Stiffness of Gels Formed by Supramolecular Self-Assembled Nanofibers
    • Dagdas, Y. S.; Tombuloglu, A.; Tekinay, A. B.; Dana, A.; Guler, M. O. Interfiber Interactions Alter the Stiffness of Gels Formed by Supramolecular Self-Assembled Nanofibers Soft Matter 2011, 7, 3524-3532
    • (2011) Soft Matter , vol.7 , pp. 3524-3532
    • Dagdas, Y.S.1    Tombuloglu, A.2    Tekinay, A.B.3    Dana, A.4    Guler, M.O.5
  • 55
    • 27944497333 scopus 로고    scopus 로고
    • Tissue Cells Feel and Respond to the Stiffness of Their Substrate
    • Discher, D. E. Tissue Cells Feel and Respond to the Stiffness of Their Substrate Science 2005, 310, 1139-1143
    • (2005) Science , vol.310 , pp. 1139-1143
    • Discher, D.E.1
  • 57
    • 84863664833 scopus 로고    scopus 로고
    • Molecular Dynamics Simulation of B-Sheet Formation in Self-Assembled Peptide Amphiphile Fibers
    • Lee, O.-S.; Liu, Y.; Schatz, G. C. Molecular Dynamics Simulation of B-Sheet Formation in Self-Assembled Peptide Amphiphile Fibers J. Nanopart. Res. 2012, 14, 936
    • (2012) J. Nanopart. Res. , vol.14 , pp. 936
    • Lee, O.-S.1    Liu, Y.2    Schatz, G.C.3
  • 58
    • 84859104555 scopus 로고    scopus 로고
    • Self-Assembling Glucagon-Like Peptide 1-Mimetic Peptide Amphiphiles for Enhanced Activity and Proliferation of Insulin-Secreting Cells
    • Khan, S.; Sur, S.; Newcomb, C. J.; Appelt, E. A.; Stupp, S. I. Self-Assembling Glucagon-Like Peptide 1-Mimetic Peptide Amphiphiles for Enhanced Activity and Proliferation of Insulin-Secreting Cells Acta Biomater. 2012, 8, 1685-1692
    • (2012) Acta Biomater. , vol.8 , pp. 1685-1692
    • Khan, S.1    Sur, S.2    Newcomb, C.J.3    Appelt, E.A.4    Stupp, S.I.5
  • 59
  • 60
    • 9244260521 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of Spontaneous Fibril Formation by Random-Coil Peptides
    • Nguyen, H. D.; Hall, C. K. Molecular Dynamics Simulations of Spontaneous Fibril Formation by Random-Coil Peptides Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 16180-16185
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16180-16185
    • Nguyen, H.D.1    Hall, C.K.2


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