Keywords: Circular Dichroism, Magnetic Resonance Spectroscopy, Peptides Chemistry, Protein Structure, Secondary, β-Propensity, Amyloidosis, Bio-Membrane, Diffusion, Eak16-Ii Analogs, Pfgnmr, Sans, Self-Assembling, Amyloid Beta Protein, Synthetic Peptide, Amino Acid Sequence, Article, Controlled Study, Hydrophobicity, Priority Journal, Protein Aggregation, Protein Assembly, Protein Conformation, Nuclear Magnetic Resonance Spectroscopy, Protein Secondary Structure, ß-Propensity,
Affiliations: *** IBB - CNR ***
Department of Chemistry, University of Naples "Federico II", 80126 Naples, Italy. gabriella.dauria@unina.it
Institute of Biostructures and Bioimaging, CNR, 80134 Naples, Italy
Consorzio per lo Sviluppo dei Sistemi a Grande Interfase (CSGI), Italy
References: Zhang, S., Altman, M., Peptide self-assembly in functional polymer science and engineering (1999) React. Funct. Polym, 41, pp. 91-10
Chiti, F., Dobson, C.M., Protein misfolding, functional amyloid, and human disease (2006) Annu. Rev. Biochem, 75, pp. 333-366
Zhang, S., Fabrication of novel biomaterials trough molecular self-assembly (2003) Nat. Biotechnol, 21, pp. 1171-1178
Holmes, T.C., Novel Peptide-based biomaterial scaffolds for tissue engineering (2002) Trends Biotechnol, 20, pp. 16-21
Zhang, S., Holmes, T., Lockshin, C., Rich, A., Spontaneous assembly of a self-complementary oligopeptide to form as stable macroscopic membrane (1993) Proc. Natl. Acad. Sci. U.S.A, 90, pp. 3334-3338
Chen, P., Self-assembly of ionic-complementary peptides: A physicochemical viewpoint (2005) Colloids Surf, 261, pp. 3-24
Xiong, H., Buckwalter, B.L., Shieh, H.M., Hecht, M.H., Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides (1995) Proc. Natl. Acad. Sci. U.S.A, 92, pp. 6349-6353
Fung, S.Y., Keyes, C., Duhamel, J., Chen, P., Concentration effect on the aggregation of a self-assembling oligopeptide (2003) Biophys. J, 85, pp. 537-548
Gambaretto, R., Tonin, L., Di Bello, C., Dettin, M., Self-assembling peptides: Correlation among sequence, secondary structure in solution and film formation (2008) Biopolymers, 89, pp. 906-915
Tinti, A., Di Foggia, M., Taddei, P., Torreggiani, A., Dettin, M., Fagnano, C., Vibrational study of auto-assembling oligopeptides for biomedical applications (2008) J. Raman Spectrosc, 39, pp. 250-259
Bax, A., Davis, D.G., MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy (1985) J. Magn. Reson, 65, pp. 355-360
Jeener, J., Meier, B.H., Bachmann, P., Ernst, R.R., Investigation of exchange processes by two-dimensional NMR spectroscopy (1979) J. Chem. Phys, 71, pp. 4546-4553
Kumar, A., Wagner, G., Ernst, R.R., Wüthrich, K., Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy:implications for studies of protein conformation (1981) J. Am. Chem. Soc, 103, pp. 3654-3658
Piantini, U., Sørensen, O.W., Ernst, R.R., Multiple quantum filters for elucidating NMR coupling networks (1982) J. Am. Chem. Soc, 104, pp. 6800-6801
Wüthrich, K., (1986) NMR of Proteins and Nucleic Acids, , John Wiley and Sons: New York
Johnson, B.A., Blevins, R.A., NMRView: A computer program for the visualization and analysis of NMR data (1994) J. Biomol. NMR, 4, pp. 603-614
Guntert, P., Mumenthaler, C., Wüthrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA (1997) J. Mol. Biol, 273, pp. 283-298
Wüthrich, K., Billeter, M., Braun, W., Pseudostructures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-protondistance constraints with nuclear magnetic resonance (1983) J. Mol. Biol, 169, pp. 949-961
Karplus, M., Vicinal proton coupling in nuclear magnetic resonance (1963) J. Am. Chem. Soc, 85, pp. 2870-2871
Guntert, P., Wüthrich, K., Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints (1991) J. Biomol. NMR, 1, pp. 447-456
Pearlman DA, Case DA, Caldwell JW, Ross WS, Cheatham TE III, DeBolt S, Ferguson D, Seibel G, Kollman P. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to stimulate the structural and energetic properties of molecules. Comput. Phys. Commun. 1995
91: 1-41Koradi, R., Billeter, M., Wüthrich, K., MOLMOL: A program for display and analysis of macromolecular structures (1996) J. Mol. Graphics, (14), pp. 51-55. , plates 29-32
Wu, D., Chen, A., Johnson Jr., C.S., An improved diffusion-ordered spectroscopy experiment incorporating bipolar-gradient pulses (1995) J. Magn. Reson., Ser. A, 115, pp. 260-264
Danielsson, J., Jarvet, J., Damberg, P., Graslund, A., Translational diffusion measured by PFG-NMR on full length and fragments of the Alzheimer Aβ(1-40) peptide. Determination of hydrodynamic radii of random coil peptides of varying length (2002) Magn. Reson. Chem, 40, pp. S89-S97
Wignall, G.D., Bates, F.S., Absolute calibration of small-angle neutron scattering data (1987) J. Appl. Crystallogr, 20, pp. 28-40
Russell, T.P., Lin, J.S., Spooner, S., Wignall, G.D., Intercalibration of small-angle x-ray and neutron scattering data (1988) J. Appl. Crystallogr, 21, pp. 629-638
Wishart, D.S., Sykes, B.D., Richards, F.M., Relationship between nuclear magnetic resonance chemical shift and protein secondary structure (1991) J. Mol. Biol, 222, pp. 311-333
Radulescu, A., Mathers, R.T., Coates, G.W., Richter, D., Fetters, L.J., A SANS study of the Self-assembly in solution of syndiotactic polypropylene homopolymers, syndiotactic polypropylene-block-poly(ethyleneco-propylene) diblock copolymers, and an alternating alternating atactic-isotactic multisegment polypropylene (2004) Macromolecules, 37, pp. 6962-6971
Mutter, M., Hersperger, R., Peptides as conformational switch: Medium-induced conformational transitions of designed peptides (1990) Angew. Chem., Int. Ed. Engl, 29, pp. 185-186
Mutter, M., Gassmann, R., Buttkus, U., Altmann, K.H., Switch peptides: PH-induced α-helix to β-sheet transitions of bis-amphiphilic oligopeptides (1991) Angew. Chem., Int. Ed. Engl, 30, pp. 1514-1516
Holmes, T. C., Novel Peptide-based biomaterial scaffolds for tissue engineering (2002) Trends Biotechnol, 20, pp. 16-21
Fung, S. Y., Keyes, C., Duhamel, J., Chen, P., Concentration effect on the aggregation of a self-assembling oligopeptide (2003) Biophys. J, 85, pp. 537-548
Bax, A., Davis, D. G., MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy (1985) J. Magn. Reson, 65, pp. 355-360
Piantini, U., S rensen, O. W., Ernst, R. R., Multiple quantum filters for elucidating NMR coupling networks (1982) J. Am. Chem. Soc, 104, pp. 6800-6801
W thrich, K., (1986) NMR of Proteins and Nucleic Acids, , John Wiley and Sons: New York
Johnson, B. A., Blevins, R. A., NMRView: A computer program for the visualization and analysis of NMR data (1994) J. Biomol. NMR, 4, pp. 603-614
W thrich, K., Billeter, M., Braun, W., Pseudostructures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-protondistance constraints with nuclear magnetic resonance (1983) J. Mol. Biol, 169, pp. 949-961
Guntert, P., W thrich, K., Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints (1991) J. Biomol. NMR, 1, pp. 447-456
Wignall, G. D., Bates, F. S., Absolute calibration of small-angle neutron scattering data (1987) J. Appl. Crystallogr, 20, pp. 28-40
Russell, T. P., Lin, J. S., Spooner, S., Wignall, G. D., Intercalibration of small-angle x-ray and neutron scattering data (1988) J. Appl. Crystallogr, 21, pp. 629-638
Wishart, D. S., Sykes, B. D., Richards, F. M., Relationship between nuclear magnetic resonance chemical shift and protein secondary structure (1991) J. Mol. Biol, 222, pp. 311-333
Self-assembling properties of ionic-complementary peptides
Self-complementary synthetic peptides, composed by 8 and 16 residues, were analyzed by CD, NMR and small angle neutron scattering (SANS) techniques in order to investigate the relevance of charge and hydrophobic interactions in determining their self-assembling properties. All the sequences are potentially able to form fibrils and membranes as they share, with the prototype EAK16, a strictly alternating arrangement of polar and nonpolar residues. We find that 16-mer peptides show higher self-assembling propensities than the 8-mer analogs and that the aggregation processes are favored by salts and neutral pH. Peptide hydrophobic character appears as the most relevant factor in determining self-assembling. Solution conformational analysis, diffusion and SANS measurements all together show that the sequences with a higher self-assemble propensity are distributed, in mild conditions, between light and heavy forms. For some of the systems, the light form is mostly constituted by monomers in a random conformation, while the heavy one is constituted by beta-aggregates. In our study we also verified that sequences designed to adopt extended conformation, when dissolved in alcohol-water mixtures, can easily fold in helix structures. In that media, the prototype of the series appears distributed between helical monomers and beta-aggregates. It is worth noticing that the structural conversion from helical monomer to beta-aggregates, mimics beta-amyloid peptide aggregation mechanisms. Copyright (C) 2008 European Peptide Society and John Wiley & Sons, Ltd.
Self-assembling properties of ionic-complementary peptides