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Articles

Pressure-induced structural changes of alanine oligopeptides in aqueous solutions

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Pages 202-209 | Received 29 Oct 2018, Accepted 06 Feb 2019, Published online: 01 Mar 2019

References

  • Chakrabartty A, Baldwin RL. Stability of α-helices. Adv Protein Chem. 1995;45:141–176. doi: 10.1016/S0065-3233(08)60334-4
  • Takekiyo T, Shimizu A, Kato M, et al. Pressure-tuning FT-IR spectroscopic study on the helix-coil transition of Ala-rich oligopeptide in aqueous solution. Biochim Biophys Acta. 2005;1750:1–4. doi: 10.1016/j.bbapap.2005.02.014
  • Imamura H, Kato M. Effect of pressure on helix–coil transition of an alanine-based peptide: an FTIR study. Proteins. 2009;75:911–918. doi: 10.1002/prot.22302
  • Cochran AG, Skelton NJ, Starovasnik MA. Tryptophan zippers: stable, monomeric beta-hairpins. Proc Nat Acad Sci USA. 2001;98:5578–5583. doi: 10.1073/pnas.091100898
  • Takekiyo T, Wu L, Yoshimura Y, et al. Relationship between hydrophobic interactions and secondary structure stability for Trpzip β-hairpin peptides. Biochemistry. 2009;48:1543–1552. doi: 10.1021/bi8019838
  • Wu L, McElheny D, Takekiyo T, et al. Geometry and efficacy of Trp/Trp, Trp/Tyr, and Tyr/Tyr aromatic interaction in cross-strand positions of a designed β-hairpin peptide. Biochemistry. 2010;49:4705–4714. doi: 10.1021/bi100491s
  • Shi Z, Woody RW, Kallenbach NR. Is polyproline II a major backbone conformation in unfolded proteins? Adv Protein Chem. 2002;62:163–240. doi: 10.1016/S0065-3233(02)62008-X
  • Bochicchio B, Tamburro AM. Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and function. Chilarity. 2002;14:782–792.
  • Kelly MA, Chellgren BW, Rucker AL, et al. Host-guest study of left-handed polyproline II helix formation. Biochemistry. 2001;40:14376–14383. doi: 10.1021/bi011043a
  • Daly S, Kulesza A, Poussigue F, et al. Conformational changes in amyloid-beta (12-28) alloforms studied using action-FRET, IMS, and molecular dynamics simulations Chem Soc. 2015;6:5040–5047.
  • Schweitzer-Stenner R, Eker F, Griebenow K, et al. The conformation of tetraalanine in water determined by polarized Raman, FT-IR, and VCD spectroscopy. J Am Chem Soc. 2004;126:2768–2776. doi: 10.1021/ja039452c
  • Schweitzer-Stenner R, Eker F, Huang Q, et al. Dihedral angles of trialanine in D2O determined by combining FTIR and polarized visible Raman spectroscopy. J Am Chem Soc. 2001;123:9628–9633. doi: 10.1021/ja016202s
  • Feng Y, Huang J, Kim S, et al. Structure of pentalanine investigated by two-dimensional infrared spectroscopy and molecular dynamics simulation. J Phys Chem B. 2016;120:5325–5339. doi: 10.1021/acs.jpcb.6b02608
  • Eker F, Cao X, Nafie LA, et al. Tripeptides adopt stable structures in water. A combined polarized visible Raman, FTIR, VCD spectroscopy study. J Am Chem Soc. 2002;124:14330–14341. doi: 10.1021/ja027381w
  • Shi Z, Olson CA, Rose GD, et al. Polyproline II structure in a sequence of seven alanine residues. Proc Natl Acd Sci USA. 2002;99:9190–9195. doi: 10.1073/pnas.112193999
  • Graf J, Nguyen PH, Stock G, et al. Structure and dynamics of the homologues series of alanine peptides: A joint molecular dynamics/NMR study. J Am Chem Soc. 2007;129:1179–1189. doi: 10.1021/ja0660406
  • Foguel D, Suarez MC, Ferrão-Gonzales AD, et al. Dissociation of amyloid filbrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water excluded cavities. Proc Natl Acad Sci USA. 2003;100:9831–9836. doi: 10.1073/pnas.1734009100
  • Oliveira AC, Gaspar GD, da Poian AT, et al. Arc repressor will not denature under pressure in the absence of water. J Mol Biol. 1994;240:184–187. doi: 10.1006/jmbi.1994.1433
  • Cordeiro Y, Kraineva J, Gomes NPB, et al. The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation. Biophys J. 2005;89:2667–2676. doi: 10.1529/biophysj.105.067603
  • Somkuti J, Houska M, Smeller L. Pressure and temperature stability of the amin apple allergen Mal d1. Eur Biophys J. 2011;40:143–151. doi: 10.1007/s00249-010-0633-8
  • Jansen R, Grudzielanek S, Dzwolak W, et al. High pressure promotes circularly shaped insulin amyloid. J Mol Biol. 2004;338:203–206. doi: 10.1016/j.jmb.2004.02.056
  • Dzwolack W, Kato M, Taniguchi Y. Fourier transform infrared spectroscopy in high-pressure studies on proteins. Biochim Biophys Acta. 2002;1595:131–144. doi: 10.1016/S0167-4838(01)00340-5
  • Dirix C, Meersman F, MacPhee CE, et al. High hydrostatic pressure dissociates early aggregates of TTR105-115, but not mature amyloid fibrils. J Mol Biol. 2005;347:903–909. doi: 10.1016/j.jmb.2005.01.073
  • Takekiyo T, Yoshimura Y, Okuno A, et al. 2007. Pressure-induced amide I’ frequency shift of model compound of proteins in water. Proceedings of the 4th International Conference on High Pressure Bioscience and Biotechnology, Vol. 1; 2007. p. 47–52.
  • Woutersen S, Pfister R, Hamm P, et al. Peptide conformational heterogeneity revealed nonlinear vibrational spectroscopy and molecular-dynamics simulations. J Chem Phys. 2002;117:6833–6840. doi: 10.1063/1.1506151
  • Talukdar H, Pudra S, Kundu K. Thermodynamics of transfer of glycine, diglycine, and triglycie from water to aqueous solutions of urea, glycerol, and sodium nitrate. Can J Chem. 1988;66:461–468. doi: 10.1139/v88-080

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