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Volumn 163-164, Issue , 2012, Pages 1-10

Structure and hydrogel formation studies on homologs of a lactoglobulin-derived peptide

Author keywords

sheet; Circular dichroism; Hydrogel formation; Lactoglobulin peptide; Milk peptide; Secondary structure; Self assembly

Indexed keywords

LACTOGLOBULIN; NANOMATERIAL; OCTAPEPTIDE;

EID: 84859217899     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2011.12.005     Document Type: Article
Times cited : (14)

References (39)
  • 4
    • 78650148591 scopus 로고    scopus 로고
    • Self-assembly and biomaterials
    • S.I. Stupp Self-assembly and biomaterials Nanoletters 10 2010 4783 4786
    • (2010) Nanoletters , vol.10 , pp. 4783-4786
    • Stupp, S.I.1
  • 9
    • 15244355116 scopus 로고    scopus 로고
    • Cytocompatibility of self-assembled β-hairpin peptide hydrogel surfaces
    • DOI 10.1016/j.biomaterials.2005.01.029, PII S0142961205000281
    • J. Kretsinger, L.A. Haines, B. Ozbas, D.J. Pochan, and J.P. Schneider Cytocompatibility of self-assembled β-hairpin peptide hydrogel surfaces Biomaterials 26 2005 5177 5186 (Pubitemid 40387840)
    • (2005) Biomaterials , vol.26 , Issue.25 , pp. 5177-5186
    • Kretsinger, J.K.1    Haines, L.A.2    Ozbas, B.3    Pochan, D.J.4    Schneider, J.P.5
  • 10
    • 77951613692 scopus 로고    scopus 로고
    • Towards functional bionanomaterials based on self-assembling cyclic peptide nanotubes
    • R.J. Brea, C. Reiriz, and J.R. Granja Towards functional bionanomaterials based on self-assembling cyclic peptide nanotubes Chemical Society Reviews 39 2010 1448 1456
    • (2010) Chemical Society Reviews , vol.39 , pp. 1448-1456
    • Brea, R.J.1    Reiriz, C.2    Granja, J.R.3
  • 12
    • 77950342360 scopus 로고    scopus 로고
    • Self-assembly of peptide amphiphiles: From molecules to nanostructures to biomaterials
    • H. Cui, M.J. Webber, and S.I. Stupp Self-assembly of peptide amphiphiles: from molecules to nanostructures to biomaterials Biopolymers: Peptide Science 94 2010 1 18
    • (2010) Biopolymers: Peptide Science , vol.94 , pp. 1-18
    • Cui, H.1    Webber, M.J.2    Stupp, S.I.3
  • 13
  • 16
    • 29944436353 scopus 로고    scopus 로고
    • Probing the importance of lateral hydrophobic association in self-assembling peptide hydrogelators
    • DOI 10.1007/s00249-005-0017-7
    • K. Rajagopal, B. Ozbas, D.J. Pochan, and J.P. Schneider Probing the importance of lateral hydrophobic association in self-assembling peptide hydrogelators European Biophysics Journal 35 2006 162 169 (Pubitemid 43042775)
    • (2006) European Biophysics Journal , vol.35 , Issue.2 , pp. 162-169
    • Rajagopal, K.1    Ozbas, B.2    Pochan, D.J.3    Schneider, J.P.4
  • 19
    • 34248182400 scopus 로고    scopus 로고
    • One-dimensional self-assembly of a rational designed β-structure peptide
    • DOI 10.1002/bip.20681
    • C. Wang, L. Huang, L. Wang, Y. Hong, and Y. Sha One-dimensional self-assembly of a rational designed β-structure peptide Biopolymers 86 2007 23 31 (Pubitemid 46716693)
    • (2007) Biopolymers , vol.86 , Issue.1 , pp. 23-31
    • Wang, C.1    Huang, L.2    Wang, L.3    Hong, Y.4    Sha, Y.5
  • 20
    • 33745165393 scopus 로고    scopus 로고
    • Molecular self-assembly of peptide nanostructures: Mechanism associaton and potential uses
    • DOI 10.2174/157341306776875802
    • M. Reches, and E. Gazit Molecular self-assembly of peptide nanostructures: mechanism of association and potential uses Current Nanoscience 2 2006 105 111 (Pubitemid 44083008)
    • (2006) Current Nanoscience , vol.2 , Issue.2 , pp. 105-111
    • Reches, M.1    Gazit, E.2
  • 22
    • 0030934379 scopus 로고    scopus 로고
    • Responsive gels formed by the spontaneous self-assembly of peptides into polymeric β-sheet tapes
    • DOI 10.1038/386259a0
    • A. Aggeli, M. Bell, N. Boden, J.N. Keen, P.F. Knowles, T.C. McLeish, M. Pitkeathly, and S.E. Radford Responsive gels formed by the spontaneous self-assembly of peptides into polymeric β-sheet tapes Nature 386 1997 259 262 (Pubitemid 27142507)
    • (1997) Nature , vol.386 , Issue.6622 , pp. 259-262
    • Aggeli, A.1    Bell, M.2    Boden, N.3    Keen, J.N.4    Knowles, P.F.5    McLeish, T.C.B.6    Pitkeathly, M.7    Radford, S.E.8
  • 23
    • 23044431605 scopus 로고    scopus 로고
    • Peptides as novel smart materials
    • DOI 10.1016/j.sbi.2005.07.005, PII S0959440X05001272, Membranes/Engineering and Desing
    • R. Fairman, and K.S. Åkerfeldt Peptides as novel smart materials Current Opinion in Structural Biology 15 2005 453 463 (Pubitemid 41073838)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.4 , pp. 453-463
    • Fairman, R.1    Akerfeldt, K.S.2
  • 26
    • 60649106342 scopus 로고    scopus 로고
    • Peptide-directed self-assembly of hydrogels
    • J. Kopeček, and J.Y. Yang Peptide-directed self-assembly of hydrogels Acta Biomaterialia 5 2009 805 816
    • (2009) Acta Biomaterialia , vol.5 , pp. 805-816
    • Kopeček, J.1    Yang, J.Y.2
  • 27
    • 79955866300 scopus 로고    scopus 로고
    • Injectable multidomain peptide nanofiber hydrogel as a delivery agent for stem cell secretome
    • E.L. Bakota, Y. Wang, R. Farhad, R. Danesh, and J.D. Hartgerink Injectable multidomain peptide nanofiber hydrogel as a delivery agent for stem cell secretome Biomacromology 12 2011 1651 1657
    • (2011) Biomacromology , vol.12 , pp. 1651-1657
    • Bakota, E.L.1    Wang, Y.2    Farhad, R.3    Danesh, R.4    Hartgerink, J.D.5
  • 31
    • 0141483558 scopus 로고    scopus 로고
    • Effect of amino acid sequence and pH on nanofiber formation of self-assembling peptides EAK16-II and EAK16-IV
    • DOI 10.1021/bm0341374
    • Y. Hong, R. Legge, S. Zhang, and P. Chen Effect of amino acid sequence and pH on nanofiber formation of self-assembling peptides EAK16-II and EAK16-IV Biomacromology 4 2003 1433 1442 (Pubitemid 37203310)
    • (2003) Biomacromolecules , vol.4 , Issue.5 , pp. 1433-1442
    • Hong, Y.1    Legge, R.L.2    Zhang, S.3    Chen, P.4
  • 32
    • 34250660127 scopus 로고    scopus 로고
    • Effect of ionic strength on the self-assembly, morphology and gelation of pH responsive β-sheet tape-forming peptides
    • DOI 10.1016/j.tet.2007.05.036, PII S0040402007008691, Low Molecular Weight Organic Gelators
    • L.M. Carrick, A. Aggeli, N. Boden, J. Fisher, E. Ingham, and T.A. Waigh Effect of ionic strength on the self-assembly, morphology and gelation of pH responsive β-sheet tape-forming peptides Tetrahedron 63 2007 7457 7467 (Pubitemid 46935277)
    • (2007) Tetrahedron , vol.63 , Issue.31 , pp. 7457-7467
    • Carrick, L.M.1    Aggeli, A.2    Boden, N.3    Fisher, J.4    Ingham, E.5    Waigh, T.A.6
  • 33
    • 35349019738 scopus 로고    scopus 로고
    • Self-assembly of multidomain peptides: Balancing molecular frustration controls conformation and nanostructure
    • DOI 10.1021/ja072536r
    • H. Dong, S.E. Paramonov, L. Aulisa, E.L. Bakota, and J.D. Hartgerink Self-assembly of multidomain peptides: balancing molecular frustration controls conformation and nanostructures Journal of the American Chemical Society 129 2007 12468 12472 (Pubitemid 47598246)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.41 , pp. 12468-12472
    • Dong, H.1    Paramonov, S.E.2    Aulisa, L.3    Bakota, E.L.4    Hartgerink, J.D.5
  • 37
    • 34247245185 scopus 로고    scopus 로고
    • Peptide self-assembly at the nanoscale: A challenging target for computational and experimental biotechnology
    • DOI 10.1016/j.tibtech.2007.03.004, PII S0167779907000753
    • G. Colombo, P. Soto, and E. Gazit Peptide self-assembly at the nanoscale: a challenging target for computational and experimental biotechnology Trends Biotechnology 25 2007 211 218 (Pubitemid 46613816)
    • (2007) Trends in Biotechnology , vol.25 , Issue.5 , pp. 211-218
    • Colombo, G.1    Soto, P.2    Gazit, E.3
  • 38
    • 28444485044 scopus 로고    scopus 로고
    • Laminated morphology of nontwisting β-sheet fibrils constructed via peptide self-assembly
    • DOI 10.1021/ja054721f
    • M.S. Lamm, K. Rajagopal, J.P. Schneider, and D.J. Pochan Laminated morphology of nontwisting β-sheet fribrils constructed via peptide self-assembly Journal of the American Chemical Society 127 2005 16692 16700 (Pubitemid 41740422)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.47 , pp. 16692-16700
    • Lamm, M.S.1    Rajagopal, K.2    Schneider, J.P.3    Pochan, D.J.4
  • 39
    • 44349108852 scopus 로고    scopus 로고
    • Peptide amphiphile nanostructure-heparin interactions and their relationship to bioactivity
    • K. Rajangam, M.S. Arnold, M.A. Rocco, and S.I. Stupp Peptide amphiphile nanostructure-heparin interactions and their relationship to bioactivity Biomaterials 29 2008 3298 3305
    • (2008) Biomaterials , vol.29 , pp. 3298-3305
    • Rajangam, K.1    Arnold, M.S.2    Rocco, M.A.3    Stupp, S.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.