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Volumn 26, Issue 8, 2010, Pages 5637-5644

Investigating the effect of pH on the aggregation of two surfactant-like octapeptides

Author keywords

[No Author keywords available]

Indexed keywords

AFM IMAGE; AQUEOUS SOLUTIONS; CD SPECTRA; CIRCULAR DICHROISM; EFFECT OF PH; FT-IR SPECTRUM; HYDROGEN BONDINGS; OCTAPEPTIDES; PH VALUE; RANDOM COIL; STRUCTURAL TRANSITIONS; TWISTED RIBBON; VARIOUS PH;

EID: 77950960656     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la904528p     Document Type: Article
Times cited : (12)

References (42)
  • 1
    • 35148865232 scopus 로고    scopus 로고
    • On the structural definition of amyloid fibrils and other polypeptide aggregates
    • DOI 10.1007/s00018-007-7110-2
    • Fandrich, M. On the structural definition of amyloid fibrils and other polypeptide aggregates. Cell. Mol. Life Sci. 2007, 64, 2066-2078. (Pubitemid 350092423)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.16 , pp. 2066-2078
    • Fandrich, M.1
  • 3
    • 0036890278 scopus 로고    scopus 로고
    • Emerging biological materials through molecular self-assembly
    • DOI 10.1016/S0734-9750(02)00026-5, PII S0734975002000265
    • Zhang, S. Emerging biological materials through molecular self-assembly. Biotechnol. Adv. 2002, 20, 321-339. (Pubitemid 35348279)
    • (2002) Biotechnology Advances , vol.20 , Issue.5-6 , pp. 321-339
    • Zhang, S.1
  • 4
    • 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
    • Hong, Y., Legge, R. L., Zhang, S., and Chen, P. Effect of amino acid sequence and pH on nanofiber formation of self-assembling peptides EAK16-II and EAK16-IV. Biomacromolecules 2003, 4, 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
  • 5
    • 4344576758 scopus 로고    scopus 로고
    • Fabrication of molecular materials using peptide construction motifs
    • DOI 10.1016/j.tibtech.2004.07.011, PII S0167779904002045
    • Zhao, X. and Zhang, S. Fabrication of molecular materials using peptide construction motifs. Trends Biotechnol. 2004, 22 (9), 470-476. (Pubitemid 39141161)
    • (2004) Trends in Biotechnology , vol.22 , Issue.9 , pp. 470-476
    • Zhao, X.1    Zhang, S.2
  • 6
    • 33745165393 scopus 로고    scopus 로고
    • Molecular self-assembly of peptide nanostructures: Mechanism associaton and potential uses
    • DOI 10.2174/157341306776875802
    • Reches, M. and Gazit, E. Molecular self-assembly of peptide nanostructures: mechanism of association and potential uses. Curr. Nanosci. 2006, 2, 105-111. (Pubitemid 44083008)
    • (2006) Current Nanoscience , vol.2 , Issue.2 , pp. 105-111
    • Reches, M.1    Gazit, E.2
  • 8
    • 1842781842 scopus 로고    scopus 로고
    • Stimuli-responsive polypeptide vesicles by conformation-specific assembly
    • Bellomo, E. G., Wyrsta, M. D., Pakstis, L., Pochan, D. J., and Deming, T. J. Stimuli-responsive polypeptide vesicles by conformation-specific assembly. Nat. Mater. 2004, 3, 244-248.
    • (2004) Nat. Mater. , vol.3 , pp. 244-248
    • Bellomo, E.G.1    Wyrsta, M.D.2    Pakstis, L.3    Pochan, D.J.4    Deming, T.J.5
  • 9
    • 32044472480 scopus 로고    scopus 로고
    • Controlled self-assembly of amphiphilic oligopeptides into shape-specific nanoarchitectures
    • DOI 10.1002/chem.200500611
    • Koga, T., Higuchi, M., Kinoshita, T., and Higashi, N., Controlled self-assembly of amphiphilic oligopeptides into shape-specific nanoarchitectures. Eur. J. Chem. 2006, 12, 1360-1367. (Pubitemid 43200387)
    • (2006) Chemistry - A European Journal , vol.12 , Issue.5 , pp. 1360-1367
    • Koga, T.1    Higuchi, M.2    Kinoshita, T.3    Higashi, N.4
  • 10
    • 23044431605 scopus 로고    scopus 로고
    • Peptides as novel smart materials
    • DOI 10.1016/j.sbi.2005.07.005, PII S0959440X05001272, Membranes/Engineering and Desing
    • Fairman, R. and Akerfeldt, K. S. Peptides as novel smart materials. Curr. Opin. Struct. Biol. 2005, 15, 453-463. (Pubitemid 41073838)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.4 , pp. 453-463
    • Fairman, R.1    Akerfeldt, K.S.2
  • 11
    • 4143141192 scopus 로고    scopus 로고
    • Self-assembling peptides and proteins for nanotechnological applications
    • DOI 10.1016/j.sbi.2004.06.006, PII S0959440X04001046
    • Rajagopal, K. and Schneider, J. P. Self-assembling peptides and proteins for nanotechnological applications. Curr. Opin. Struct. Biol. 2004, 14, 480-486. (Pubitemid 39099286)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.4 , pp. 480-486
    • Rajagopal, K.1    Schneider, J.P.2
  • 12
    • 24644466541 scopus 로고    scopus 로고
    • Peptide-based nanotubes and their applications in bionanotechnology
    • DOI 10.1002/adma.200401849
    • Gao, X. and Matsui, H. Peptide-based nanotubes and their applications in bionanotechnology. Adv. Mater. 2005, 17, 2037-2050. (Pubitemid 41284788)
    • (2005) Advanced Materials , vol.17 , Issue.17 , pp. 2037-2050
    • Gao, X.1    Matsui, H.2
  • 13
    • 0036890278 scopus 로고    scopus 로고
    • Emerging biological materials through molecular self-assembly
    • Zhang, S. G. Emerging biological materials through molecular self-assembly. Biotechnol. Adv. 2002, 20 (5?6), 321-339.
    • (2002) Biotechnol. Adv. , vol.20 , Issue.5-6 , pp. 321-339
    • Zhang, S.G.1
  • 14
    • 0029064713 scopus 로고
    • Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides
    • Xiong, H., Buckwalter, B. L., Shieh, H.-M., and Hecht, M. H. Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 6349-6353.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 6349-6353
    • Xiong, H.1    Buckwalter, B.L.2    Shieh, H.-M.3    Hecht, M.H.4
  • 16
    • 0033937682 scopus 로고    scopus 로고
    • Conformational behavior of ionic self-complementary peptides
    • Altman, M., Lee, P., Rich, A., and Zhang, S. Conformational behaviour of ionic self-complementary peptides. Protein Sci. 2000, 9, 1095-1105. (Pubitemid 30419145)
    • (2000) Protein Science , vol.9 , Issue.6 , pp. 1095-1105
    • Altman, M.1    Lee, P.2    Rich, A.3    Zhang, S.4
  • 17
    • 33750079259 scopus 로고    scopus 로고
    • Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids
    • Dames, S. A., Aregger, R., Vajpai, N., Bernado, P., Blackledge, M., and Grzesiek, S. Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids. J. Am. Chem. Soc. 2006, 128, 13508-13514.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 13508-13514
    • Dames, S.A.1    Aregger, R.2    Vajpai, N.3    Bernado, P.4    Blackledge, M.5    Grzesiek, S.6
  • 18
    • 28944434118 scopus 로고    scopus 로고
    • Effect of NaCl and peptide concentration on the self-assembly of an ionic-complementary peptide EAK16-II
    • Hong, Y., Pritzker, M. D., Legge, R. L., and Chen, P. Effect of NaCl and peptide concentration on the self-assembly of an ionic-complementary peptide EAK16-II. Colloids Surf., B: Biointerf. 2005, 46, 152-161.
    • (2005) Colloids Surf., B: Biointerf. , vol.46 , pp. 152-161
    • Hong, Y.1    Pritzker, M.D.2    Legge, R.L.3    Chen, P.4
  • 19
    • 19344363958 scopus 로고    scopus 로고
    • Self-assembly of ionic-complementary peptides: A physicochemical viewpoint
    • Chen, P. Self-assembly of ionic-complementary peptides: a physicochemical viewpoint. Colloids Surf., A 2005, 261, 3-24.
    • (2005) Colloids Surf., A , vol.261 , pp. 3-24
    • Chen, P.1
  • 20
    • 0037259922 scopus 로고    scopus 로고
    • Supramolecular structure of helical ribbons self-assembled from a β-sheet peptide
    • Hwang, W., Marini, D. M., Kamm, R. D., and Zhang, S. Supramolecular structure of helical ribbons self-assembled from a β-sheet peptide. J. Chem. Phys. 2003, 118 (1), 389-397.
    • (2003) J. Chem. Phys. , vol.118 , Issue.1 , pp. 389-397
    • Hwang, W.1    Marini, D.M.2    Kamm, R.D.3    Zhang, S.4
  • 21
    • 0035834113 scopus 로고    scopus 로고
    • Hierarchical self-assembly of chiral rod-like molecules as a model for peptide β-sheet tapes, ribbons, fibrils, and fibers
    • Aggeli, A., Nyrkova, I. A., Bell, M., Harding, R., Carrick, L., McLeish, T. B. C., Semenov, A. N., and Boden, N. Hierarchical self-assembly of chiral rod-like molecules as a model for peptide β-sheet tapes, ribbons, fibrils, and fibers. Proc. Natl. Acad. Sci. U.S.A. 2001, 98 (21), 11857-11862.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , Issue.21 , pp. 11857-11862
    • Aggeli, A.1    Nyrkova, I.A.2    Bell, M.3    Harding, R.4    Carrick, L.5    McLeish, T.B.C.6    Semenov, A.N.7    Boden, N.8
  • 22
    • 0034315736 scopus 로고    scopus 로고
    • Theoretical studies on the origin of β-sheet twisting
    • Shamovsky, I. L., Ross, G. M., and Roipelle, R. J. Theoretical studies on the origin of β-sheet twisting. J. Phys. Chem. B 2000, 104, 11296-11307.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 11296-11307
    • Shamovsky, I.L.1    Ross, G.M.2    Roipelle, R.J.3
  • 23
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Barth, A. Infrared spectroscopy of proteins. Biochim. Biophys. Acta 2007, 1767.
    • (2007) Biochim. Biophys. Acta , pp. 1767
    • Barth, A.1
  • 24
    • 0035887070 scopus 로고    scopus 로고
    • Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling method and stress factors
    • Weert, M. v. d., Haris, P. I., Hennink, W. E., and Crommelin, D. J. A. Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors. Anal. Biochem. 2001, 297.
    • (2001) Anal. Biochem. , pp. 297
    • Weert, M.V.D.1    Haris, P.I.2    Hennink, W.E.3    Crommelin, D.J.A.4
  • 25
    • 58149476769 scopus 로고    scopus 로고
    • A summary of the measured pK values of the ionizable groups in folded proteins
    • Grimsley, G. R., Scholtz, J. M., and Pace, C. N. A summary of the measured pK values of the ionizable groups in folded proteins. Protein Sci. 2009, 18.
    • (2009) Protein Sci. , pp. 18
    • Grimsley, G.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 26
    • 0036099192 scopus 로고    scopus 로고
    • Experimental pK(a) values of buried residues: Analysis with continuum methods and role of water penetration
    • Fitch, C. A., Karp, D. A., Lee, K. K., Stites, W. E., Lattman, E. E., and Garcia-Moreno, B. Experimental pK(a) values of buried residues: Analysis with continuum methods and role of water penetration. Biophys. J. 2002, 82 (6), 3289-3304.
    • (2002) Biophys. J. , vol.82 , Issue.6 , pp. 3289-3304
    • Fitch, C.A.1    Karp, D.A.2    Lee, K.K.3    Stites, W.E.4    Lattman, E.E.5    Garcia-Moreno, B.6
  • 28
    • 33847029566 scopus 로고    scopus 로고
    • Conformations of alanine-based peptides in water probed by FTIR, raman, vibrational circular dichroism, electronic circular dichroism, and NMR spectroscopy
    • Schweitzer-Stenner, R., Measey, T., Kakalis, L., Jordan, F., Pizzanelli, S., Forte, C., and Griebenow, K. Conformations of alanine-based peptides in water probed by FTIR, raman, vibrational circular dichroism, electronic circular dichroism, and NMR spectroscopy. Biochemistry 2007, 46.
    • (2007) Biochemistry , pp. 46
    • Schweitzer-Stenner, R.1    Measey, T.2    Kakalis, L.3    Jordan, F.4    Pizzanelli, S.5    Forte, C.6    Griebenow, K.7
  • 29
    • 35648936428 scopus 로고    scopus 로고
    • Flanking polyproline sequences inhibit beta-sheet structure in polyglutamine segments by inducing PPII-like helix structure
    • Darnell, G., Orgel, J. P. R. O., Pahl, R., and Meredith, S. C., Flanking polyproline sequences inhibit beta-sheet structure in polyglutamine segments by inducing PPII-like helix structure. J. Mol. Biol. 2007, 374.
    • (2007) J. Mol. Biol. , pp. 374
    • Darnell, G.1    Orgel, J.P.R.O.2    Pahl, R.3    Meredith, S.C.4
  • 30
    • 70449109702 scopus 로고    scopus 로고
    • Mechanism of cis-inhibition of polyQ fibrillation by polyP: PPII oligomers and the hydrophobic effect
    • Darnell, G. D., Derryberry, J., Kurutz, J. W., and Meredith, S. C. Mechanism of cis-inhibition of polyQ fibrillation by polyP: PPII oligomers and the hydrophobic effect. Biophys. J. 2009, 97.
    • (2009) Biophys. J. , pp. 97
    • Darnell, G.D.1    Derryberry, J.2    Kurutz, J.W.3    Meredith, S.C.4
  • 31
    • 0014143492 scopus 로고
    • Aggregation-induced red shift of the Cotton effect of mitochondrial structural protein
    • Steim, J. M. and Fleischer, S. Aggregation-induced red shift of the Cotton effect of mitochondrial structural protein. Proc. Natl. Acad. Sci. U.S.A. 1967, 58, 1292-1298.
    • (1967) Proc. Natl. Acad. Sci. U.S.A. , vol.58 , pp. 1292-1298
    • Steim, J.M.1    Fleischer, S.2
  • 32
    • 0037144424 scopus 로고    scopus 로고
    • Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin
    • Reches, M., Porat, Y., and Gazit, E. Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin. J. Biol. Chem. 2002, 277 (38), 35475-35480.
    • (2002) J. Biol. Chem. , vol.277 , Issue.38 , pp. 35475-35480
    • Reches, M.1    Porat, Y.2    Gazit, E.3
  • 33
    • 0345550440 scopus 로고    scopus 로고
    • Structures of helical β-tapes and twisted ribbons: The role of side-chain interactions on twist and bend behaviour
    • Fishwick, C. W. G., Beevers, A. J., Carrick, L. M., Whitehouse, C. D., Aggeli, A., and Boden, N. Structures of helical β-tapes and twisted ribbons: the role of side-chain interactions on twist and bend behaviour. Nano Lett. 2003, 3 (11), 1475-1479.
    • (2003) Nano Lett. , vol.3 , Issue.11 , pp. 1475-1479
    • Fishwick, C.W.G.1    Beevers, A.J.2    Carrick, L.M.3    Whitehouse, C.D.4    Aggeli, A.5    Boden, N.6
  • 34
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • Pelton, J. T. and McLean, L. R. Spectroscopic methods for analysis of protein secondary structure. Anal. Biochem. 2000, 277, 167-176.
    • (2000) Anal. Biochem. , vol.277 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 36
    • 0034076545 scopus 로고    scopus 로고
    • Do parallel beta-helix proteins have a unique fourier transform infrared spectrum?
    • Khurana, R. and Fink, A. L. Do parallel beta-helix proteins have a unique fourier transform infrared spectrum? Biophys. J. 2000, 78.
    • (2000) Biophys. J. , pp. 78
    • Khurana, R.1    Fink, A.L.2
  • 37
    • 43449118401 scopus 로고    scopus 로고
    • Time-resolved infrared spectroscopy of ph-indiced aggregation of the alzheimer abeta1?28 peptide
    • Peralvarez-Marin, A., Barth, A., and Graslund, A. Time-resolved infrared spectroscopy of ph-indiced aggregation of the alzheimer abeta1?28 peptide. J. Mol. Biol. 2008, 379.
    • (2008) J. Mol. Biol. , pp. 379
    • Peralvarez-Marin, A.1    Barth, A.2    Graslund, A.3
  • 39
    • 68949142908 scopus 로고    scopus 로고
    • Amyloid fibril-like structure underlies the aggregate structure across the pH range for beta-lactoglobulin
    • Krebs, M. R. H., Devlin, G. L., and Donald, A. M. Amyloid fibril-like structure underlies the aggregate structure across the pH range for beta-lactoglobulin. Biophys. J. 2009, 96.
    • (2009) Biophys. J. , pp. 96
    • Krebs, M.R.H.1    Devlin, G.L.2    Donald, A.M.3
  • 42
    • 0037931536 scopus 로고    scopus 로고
    • Differential degradation of amyloid beta genetic varients associated with hereditary dementia or stroke by insulin-degrading enzyme
    • Morelli, L., Llovera, R., Gonzalez, S. A., Affranchino, J. L., Prelli, F., Frangione, B., Ghiso, J., and Castano, E. M. Differential degradation of amyloid beta genetic varients associated with hereditary dementia or stroke by insulin-degrading enzyme. J. Biol. Chem. 2003, 278.
    • (2003) J. Biol. Chem. , pp. 278
    • Morelli, L.1    Llovera, R.2    Gonzalez, S.A.3    Affranchino, J.L.4    Prelli, F.5    Frangione, B.6    Ghiso, J.7    Castano, E.M.8


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