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Volumn 19, Issue 12, 2013, Pages 737-744

Self-assembly of pH and calcium dual-responsive peptide-amphiphilic hydrogel

Author keywords

calcium response; hydrogel; peptide amphiphile; pH sensitive; self assembly

Indexed keywords

AMPHOPHILE; ASPARTIC ACID; CALCIUM ION; PEPTIDE; SELF ASSEMBLED MONOLAYER;

EID: 84888024731     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.2569     Document Type: Article
Times cited : (29)

References (51)
  • 1
    • 0026433721 scopus 로고
    • Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures
    • Whitesides GM, Mathias JP, Seto CT,. Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures. Science (New York, NY) 1991; 254: 1312-1319.
    • (1991) Science (New York, NY) , vol.254 , pp. 1312-1319
    • Whitesides, G.M.1    Mathias, J.P.2    Seto, C.T.3
  • 3
    • 33744946043 scopus 로고    scopus 로고
    • Self-assembly of peptide-amphiphile nanofibers: The roles of hydrogen bonding and amphiphilic packing
    • Paramonov SE, Jun HW, Hartgerink JD,. Self-assembly of peptide-amphiphile nanofibers: the roles of hydrogen bonding and amphiphilic packing. J. Am. Chem. Soc. 2006; 128: 7291-7298.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7291-7298
    • Paramonov, S.E.1    Jun, H.W.2    Hartgerink, J.D.3
  • 4
    • 33644885444 scopus 로고    scopus 로고
    • Intermolecular forces in the self-assembly of peptide amphiphile nanofibers
    • Stendahl JC, Rao MS, Guler MO, Stupp SI,. Intermolecular forces in the self-assembly of peptide amphiphile nanofibers. Adv. Funct. Mater. 2006; 16: 499-508.
    • (2006) Adv. Funct. Mater. , vol.16 , pp. 499-508
    • Stendahl, J.C.1    Rao, M.S.2    Guler, M.O.3    Stupp, S.I.4
  • 5
    • 0038631832 scopus 로고    scopus 로고
    • Aromatic-aromatic interactions in crystal structures of helical peptide scaffolds containing projecting phenylalanine residues
    • Aravinda S, Shamala N, Das C, Sriranjini A, Karle IL, Balaram P,. Aromatic-aromatic interactions in crystal structures of helical peptide scaffolds containing projecting phenylalanine residues. J. Am. Chem. Soc. 2003; 125: 5308-5315.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5308-5315
    • Aravinda, S.1    Shamala, N.2    Das, C.3    Sriranjini, A.4    Karle, I.L.5    Balaram, P.6
  • 6
    • 0001608018 scopus 로고    scopus 로고
    • Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles
    • Santoso S, Hwang W, Hartman H, Zhang SG,. Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles. Nano Lett. 2002; 2: 687-691.
    • (2002) Nano Lett. , vol.2 , pp. 687-691
    • Santoso, S.1    Hwang, W.2    Hartman, H.3    Zhang, S.G.4
  • 7
    • 41149104937 scopus 로고    scopus 로고
    • Designing peptide based nanomaterials
    • Ulijn RV, Smith AM,. Designing peptide based nanomaterials. Chem. Soc. Rev. 2008; 37: 664-675.
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 664-675
    • Ulijn, R.V.1    Smith, A.M.2
  • 10
    • 0034814485 scopus 로고    scopus 로고
    • Self-assembly and gelation of oxidized glutathione in organic solvents
    • Lyon RP, Atkins WM,. Self-assembly and gelation of oxidized glutathione in organic solvents. J. Am. Chem. Soc. 2001; 123: 4408-4413.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 4408-4413
    • Lyon, R.P.1    Atkins, W.M.2
  • 11
    • 79957985973 scopus 로고    scopus 로고
    • Materials from peptide assembly: Towards the treatment of cancer and transmittable disease
    • Branco MC, Sigano DM, Schneider JP,. Materials from peptide assembly: towards the treatment of cancer and transmittable disease. Curr. Opin. Chem. Biol. 2011; 15: 427-434.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 427-434
    • Branco, M.C.1    Sigano, D.M.2    Schneider, J.P.3
  • 12
    • 84863019040 scopus 로고    scopus 로고
    • Self-assembling peptides as cell-interactive scaffolds
    • Wu EC, Zhang S, Hauser CAE,. Self-assembling peptides as cell-interactive scaffolds. Adv. Funct. Mater. 2012; 22: 456-468.
    • (2012) Adv. Funct. Mater. , vol.22 , pp. 456-468
    • Wu, E.C.1    Zhang, S.2    Hauser, C.A.E.3
  • 13
    • 84857506134 scopus 로고    scopus 로고
    • From short peptides to nanofibers to macromolecular assemblies in biomedicine
    • Loo Y, Zhang S, Hauser CAE,. From short peptides to nanofibers to macromolecular assemblies in biomedicine. Biotechnol. Adv. 2012; 30: 593-603.
    • (2012) Biotechnol. Adv. , vol.30 , pp. 593-603
    • Loo, Y.1    Zhang, S.2    Hauser, C.A.E.3
  • 16
    • 79953235459 scopus 로고    scopus 로고
    • Effect of C-terminal modification on the self-assembly and hydrogelation of fluorinated Fmoc-Phe derivatives
    • Ryan DM, Doran TM, Anderson SB, Nilsson BL,. Effect of C-terminal modification on the self-assembly and hydrogelation of fluorinated Fmoc-Phe derivatives. Langmuir 2011; 27: 4029-4039.
    • (2011) Langmuir , vol.27 , pp. 4029-4039
    • Ryan, D.M.1    Doran, T.M.2    Anderson, S.B.3    Nilsson, B.L.4
  • 17
    • 82455172070 scopus 로고    scopus 로고
    • Effect of glycine substitution on fmoc-diphenylalanine self-assembly and gelation properties
    • Tang C, Ulijn RV, Saiani A,. Effect of glycine substitution on fmoc-diphenylalanine self-assembly and gelation properties. Langmuir 2011; 27: 14438-14449.
    • (2011) Langmuir , vol.27 , pp. 14438-14449
    • Tang, C.1    Ulijn, R.V.2    Saiani, A.3
  • 18
    • 0141596163 scopus 로고    scopus 로고
    • Thermally reversible hydrogels via intramolecular folding and consequent self-assembly of a de novo designed peptide
    • Pochan DJ, Schneider JP, Kretsinger J, Ozbas B, Rajagopal K, Haines L,. Thermally reversible hydrogels via intramolecular folding and consequent self-assembly of a de novo designed peptide. J. Am. Chem. Soc. 2003; 125: 11802-11803.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11802-11803
    • Pochan, D.J.1    Schneider, J.P.2    Kretsinger, J.3    Ozbas, B.4    Rajagopal, K.5    Haines, L.6
  • 20
    • 46849093387 scopus 로고    scopus 로고
    • Self-assembled pH-responsive hydrogels composed of the RATEA16 peptide
    • Zhao Y, Yokoi H, Tanaka M, Kinoshita T, Tan T,. Self-assembled pH-responsive hydrogels composed of the RATEA16 peptide. Biomacromolecules 2008; 9: 1511-1518.
    • (2008) Biomacromolecules , vol.9 , pp. 1511-1518
    • Zhao, Y.1    Yokoi, H.2    Tanaka, M.3    Kinoshita, T.4    Tan, T.5
  • 21
    • 70349173315 scopus 로고    scopus 로고
    • Tuning the pH responsiveness of beta-hairpin peptide folding, self-assembly, and hydrogel material formation
    • Rajagopal K, Lamm MS, Haines-Butterick LA, Pochan DJ, Schneider JP,. Tuning the pH responsiveness of beta-hairpin peptide folding, self-assembly, and hydrogel material formation. Biomacromolecules 2009; 10: 2619-2625.
    • (2009) Biomacromolecules , vol.10 , pp. 2619-2625
    • Rajagopal, K.1    Lamm, M.S.2    Haines-Butterick, L.A.3    Pochan, D.J.4    Schneider, J.P.5
  • 22
    • 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 JP, Pochan DJ,. 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
  • 23
    • 77953420989 scopus 로고    scopus 로고
    • Influence of salt on the self-assembly of two model amyloid heptapeptides
    • Castelletto V, Hamley IW, Cenker C, Olsson U,. Influence of salt on the self-assembly of two model amyloid heptapeptides. J. Phys. Chem. B 2010; 114: 8002-8008.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8002-8008
    • Castelletto, V.1    Hamley, I.W.2    Cenker, C.3    Olsson, U.4
  • 24
    • 28844449157 scopus 로고    scopus 로고
    • Light-activated hydrogel formation via the triggered folding and self-assembly of a designed peptide
    • Haines LA, Rajagopal K, Ozbas B, Salick DA, Pochan DJ, Schneider JP,. Light-activated hydrogel formation via the triggered folding and self-assembly of a designed peptide. J. Am. Chem. Soc. 2005; 127: 17025-17029.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17025-17029
    • Haines, L.A.1    Rajagopal, K.2    Ozbas, B.3    Salick, D.A.4    Pochan, D.J.5    Schneider, J.P.6
  • 27
    • 78650154377 scopus 로고    scopus 로고
    • Supramolecular structures of amyloid-related peptides in an ambient water nanofilm
    • Ye M, Zhang Y, Li H, Xie M, Hu J,. Supramolecular structures of amyloid-related peptides in an ambient water nanofilm. J. Phys. Chem. B 2010; 114: 15759-15765.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 15759-15765
    • Ye, M.1    Zhang, Y.2    Li, H.3    Xie, M.4    Hu, J.5
  • 28
    • 70350109508 scopus 로고    scopus 로고
    • Wormlike micelle formation in peptide-lipid conjugates driven by secondary structure transformation of the headgroups
    • Shimada T, Lee S, Bates FS, Hotta A, Tirrell M,. Wormlike micelle formation in peptide-lipid conjugates driven by secondary structure transformation of the headgroups. J. Phys. Chem. B 2009; 113: 13711-13714.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 13711-13714
    • Shimada, T.1    Lee, S.2    Bates, F.S.3    Hotta, A.4    Tirrell, M.5
  • 29
    • 79953837228 scopus 로고    scopus 로고
    • From fibers to micelles using point-mutated amphiphilic peptides
    • Schuster TB, Ouboter DdB, Palivan CG, Meier W,. From fibers to micelles using point-mutated amphiphilic peptides. Langmuir 2011; 27: 4578-4584.
    • (2011) Langmuir , vol.27 , pp. 4578-4584
    • Schuster, T.B.1    Ouboter, D.2    Palivan, C.G.3    Meier, W.4
  • 31
    • 34147200105 scopus 로고    scopus 로고
    • Cell adhesion and growth to peptide-patterned supported lipid membranes
    • Stroumpoulis D, Zhang H, Rubalcava L, Gliem J, Tirrell M,. Cell adhesion and growth to peptide-patterned supported lipid membranes. Langmuir 2007; 23: 3849-3856.
    • (2007) Langmuir , vol.23 , pp. 3849-3856
    • Stroumpoulis, D.1    Zhang, H.2    Rubalcava, L.3    Gliem, J.4    Tirrell, M.5
  • 34
    • 84555220404 scopus 로고    scopus 로고
    • Biphasic peptide amphiphile nanomatrix embedded with hydroxyapatite nanoparticles for stimulated osteoinductive response
    • Anderson JM, Patterson JL, Vines JB, Javed A, Gilbert SR, Jun H-W,. Biphasic peptide amphiphile nanomatrix embedded with hydroxyapatite nanoparticles for stimulated osteoinductive response. Acs Nano. 2011; 5: 9463-9479.
    • (2011) Acs Nano. , vol.5 , pp. 9463-9479
    • Anderson, J.M.1    Patterson, J.L.2    Vines, J.B.3    Javed, A.4    Gilbert, S.R.5    Jun, H.-W.6
  • 35
    • 67649202811 scopus 로고    scopus 로고
    • Self-assembly of peptide-amphiphile C-12-A beta(11-17) into nanofibrils
    • Deng M, Yu D, Hou Y, Wang Y,. Self-assembly of peptide-amphiphile C-12-A beta(11-17) into nanofibrils. J. Phys. Chem. B 2009; 113: 8539-8544.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 8539-8544
    • Deng, M.1    Yu, D.2    Hou, Y.3    Wang, Y.4
  • 36
    • 73249121218 scopus 로고    scopus 로고
    • Modulating the gelation properties of self-assembling peptide amphiphiles
    • Anderson JM, Andukuri A, Lim DJ, Jun H-W,. Modulating the gelation properties of self-assembling peptide amphiphiles. Acs Nano. 2009; 3: 3447-3454.
    • (2009) Acs Nano. , vol.3 , pp. 3447-3454
    • Anderson, J.M.1    Andukuri, A.2    Lim, D.J.3    Jun, H.-W.4
  • 37
    • 0038789021 scopus 로고    scopus 로고
    • Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction
    • Niece KL, Hartgerink JD, Donners J, Stupp SI,. Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction. J. Am. Chem. Soc. 2003; 125: 7146-7147.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7146-7147
    • Niece, K.L.1    Hartgerink, J.D.2    Donners, J.3    Stupp, S.I.4
  • 38
    • 41449095163 scopus 로고    scopus 로고
    • Quadruple helix formation of a photoresponsive peptide amphiphile and its light-triggered dissociation into single fibers
    • Muraoka T, Cui H, Stupp SI,. Quadruple helix formation of a photoresponsive peptide amphiphile and its light-triggered dissociation into single fibers. J. Am. Chem. Soc. 2008; 130: 2946-2947.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2946-2947
    • Muraoka, T.1    Cui, H.2    Stupp, S.I.3
  • 41
    • 84866092398 scopus 로고    scopus 로고
    • Elastin-like peptide amphiphiles form nanofibers with tunable length
    • Aluri S, Pastuszka MK, Moses AS, MacKay JA,. Elastin-like peptide amphiphiles form nanofibers with tunable length. Biomacromolecules 2012; 13: 2645-2654.
    • (2012) Biomacromolecules , vol.13 , pp. 2645-2654
    • Aluri, S.1    Pastuszka, M.K.2    Moses, A.S.3    Mackay, J.A.4
  • 42
    • 0034708415 scopus 로고    scopus 로고
    • Folding of a synthetic parallel beta-roll protein
    • Lilie H, Haehnel W, Rudolph R, Baumann U,. Folding of a synthetic parallel beta-roll protein. FEBS Lett. 2000; 470: 173-177.
    • (2000) FEBS Lett. , vol.470 , pp. 173-177
    • Lilie, H.1    Haehnel, W.2    Rudolph, R.3    Baumann, U.4
  • 43
    • 78649896548 scopus 로고    scopus 로고
    • Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxin
    • Chenal A, Karst JC, Perez ACS, Wozniak AK, Baron B, England P, Ladant D,. Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxin. Biophys. J. 2010; 99: 3744-3753.
    • (2010) Biophys. J. , vol.99 , pp. 3744-3753
    • Chenal, A.1    Karst, J.C.2    Perez, A.C.S.3    Wozniak, A.K.4    Baron, B.5    England, P.6    Ladant, D.7
  • 44
    • 77349122288 scopus 로고    scopus 로고
    • Characterization of the regions involved in the calcium-induced folding of the intrinsically disordered RTX motifs from the bordetella pertussis adenylate cyclase toxin
    • Perez A-CS, Karst JC, Davi M, Guijarro JI, Ladant D, Chenal A,. Characterization of the regions involved in the calcium-induced folding of the intrinsically disordered RTX motifs from the bordetella pertussis adenylate cyclase toxin. J. Mol. Biol. 2010; 397: 534-549.
    • (2010) J. Mol. Biol. , vol.397 , pp. 534-549
    • Perez, A.-C.1    Karst, J.C.2    Davi, M.3    Guijarro, J.I.4    Ladant, D.5    Chenal, A.6
  • 45
    • 77953811286 scopus 로고    scopus 로고
    • Calcium-induced folding of a beta roll motif requires C-terminal entropic stabilization
    • Blenner MA, Shur O, Szilvay GR, Cropek DM, Banta S,. Calcium-induced folding of a beta roll motif requires C-terminal entropic stabilization. J. Mol. Biol. 2010; 400: 244-256.
    • (2010) J. Mol. Biol. , vol.400 , pp. 244-256
    • Blenner, M.A.1    Shur, O.2    Szilvay, G.R.3    Cropek, D.M.4    Banta, S.5
  • 46
    • 77957782184 scopus 로고    scopus 로고
    • De novo design of a shear-thin recoverable peptide-based hydrogel capable of intrafibrillar photopolymerization
    • Rughani RV, Branco MC, Pochan D, Schneider JP,. De novo design of a shear-thin recoverable peptide-based hydrogel capable of intrafibrillar photopolymerization. Macromolecules 2010; 43: 7924-7930.
    • (2010) Macromolecules , vol.43 , pp. 7924-7930
    • Rughani, R.V.1    Branco, M.C.2    Pochan, D.3    Schneider, J.P.4
  • 50
    • 70349165421 scopus 로고    scopus 로고
    • Self-assembly of multidomain peptides: Sequence variation allows control over cross-linking and viscoelasticity
    • Aulisa L, Dong H, Hartgerink JD,. Self-assembly of multidomain peptides: sequence variation allows control over cross-linking and viscoelasticity. Biomacromolecules 2009; 10: 2694-2698.
    • (2009) Biomacromolecules , vol.10 , pp. 2694-2698
    • Aulisa, L.1    Dong, H.2    Hartgerink, J.D.3
  • 51
    • 35349019738 scopus 로고    scopus 로고
    • Self-assembly7 of multidomain peptides: Balancing molecular frustration controls conformation and nanostructure
    • Dong H, Paramonov SE, Aulisa L, Bakota EL, Hartgerink JD,. Self-assembly7 of multidomain peptides: balancing molecular frustration controls conformation and nanostructure. J. Am. Chem. Soc. 2007; 129: 12468-12472.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12468-12472
    • Dong, H.1    Paramonov, S.E.2    Aulisa, L.3    Bakota, E.L.4    Hartgerink, J.D.5


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