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Volumn 17, Issue 11, 2011, Pages 735-743

Structural requirements essential for elastin coacervation: Favorable spatial arrangements of valine ridges on the three-dimensional structure of elastin-derived polypeptide (VPGVG)n

Author keywords

Coacervation; Elastin; Repeat structure; Self association; Spiral structure

Indexed keywords

ELASTIN; GLYCINE; VALINE;

EID: 80055006040     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1394     Document Type: Article
Times cited : (28)

References (40)
  • 1
    • 0014409143 scopus 로고
    • Cardiovascular studies on copper deficient swine. XII. Partial purification of a soluble protein resembling elastin
    • Smith DW, Weissman N, Carnes WH. Cardiovascular studies on copper deficient swine. XII. Partial purification of a soluble protein resembling elastin. Biochem. Biophys. Res. Commun. 1968; 31: 309-315.
    • (1968) Biochem. Biophys. Res. Commun. , vol.31 , pp. 309-315
    • Smith, D.W.1    Weissman, N.2    Carnes, W.H.3
  • 2
    • 0032533711 scopus 로고    scopus 로고
    • Biochemistry of tropoelastin. Biochemistry of tropoelastin
    • Vrhovski B, Weiss AS. Biochemistry of tropoelastin. Biochemistry of tropoelastin. Eur. J. Biochem. 1998; 258: 1-18.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 1-18
    • Vrhovski, B.1    Weiss, A.S.2
  • 3
    • 0023888219 scopus 로고
    • Entropic elastic processes in protein mechanisms. II. Simple (passive) and coupled (active) development of elastic forces
    • Urry DW. Entropic elastic processes in protein mechanisms. II. Simple (passive) and coupled (active) development of elastic forces. J. Protein Chem. 1988; 7: 81-114.
    • (1988) J. Protein Chem. , vol.7 , pp. 81-114
    • Urry, D.W.1
  • 6
    • 0023664380 scopus 로고
    • Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones
    • Raju K, Anwar RA. Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones. J. Biol. Chem. 1987; 262: 5755-5762.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5755-5762
    • Raju, K.1    Anwar, R.A.2
  • 7
    • 0023663346 scopus 로고
    • Repeating structure of chick tropoelastin revealed by complementary DNA cloning
    • Bressan GM, Argos P, Stanley KK. Repeating structure of chick tropoelastin revealed by complementary DNA cloning. Biochemistry 1987; 26: 1497-1503.
    • (1987) Biochemistry , vol.26 , pp. 1497-1503
    • Bressan, G.M.1    Argos, P.2    Stanley, K.K.3
  • 8
    • 0025130777 scopus 로고
    • Heterogeneity of rat tropoelastin mRNA revealed by cDNA cloning
    • Pierce RA, Deak SB, Stolle CA, Boyd CD. Heterogeneity of rat tropoelastin mRNA revealed by cDNA cloning. Biochemistry 1990; 29: 9677-9683.
    • (1990) Biochemistry , vol.29 , pp. 9677-9683
    • Pierce, R.A.1    Deak, S.B.2    Stolle, C.A.3    Boyd, C.D.4
  • 10
    • 0017090360 scopus 로고
    • Synthetic, cross-linked polypentapeptide fo tropoelastin: an anisotropic, fibrillar elastomer
    • Urry DW, Okamoto K, Harris RD, Hendrix CF, Long MM. Synthetic, cross-linked polypentapeptide fo tropoelastin: an anisotropic, fibrillar elastomer. Biochemistry 1976; 15: 4083-4089.
    • (1976) Biochemistry , vol.15 , pp. 4083-4089
    • Urry, D.W.1    Okamoto, K.2    Harris, R.D.3    Hendrix, C.F.4    Long, M.M.5
  • 11
    • 0022263575 scopus 로고
    • Polypentapeptide of elastin: temperature dependence of ellipticity and correlation with elastomeric force
    • Urry DW, Shaw RG, Prasad KU. Polypentapeptide of elastin: temperature dependence of ellipticity and correlation with elastomeric force. Biochem. Biophys. Res. Commun. 1985; 130: 50-57.
    • (1985) Biochem. Biophys. Res. Commun. , vol.130 , pp. 50-57
    • Urry, D.W.1    Shaw, R.G.2    Prasad, K.U.3
  • 12
    • 0015994757 scopus 로고
    • Studies on the conformation and interactions of elastin. Proton magnetic resonance of the repeating pentapeptide
    • Urry DW, Cunningham WD, Ohnishi T. Studies on the conformation and interactions of elastin. Proton magnetic resonance of the repeating pentapeptide. Biochemistry 1974; 13: 609-615.
    • (1974) Biochemistry , vol.13 , pp. 609-615
    • Urry, D.W.1    Cunningham, W.D.2    Ohnishi, T.3
  • 13
    • 0016698904 scopus 로고
    • Proton and carbon magnetic resonance studies of the synthetic polypentapeptide of elastin
    • Urry DW, Mitchell LW, Ohnishi T, Long MM. Proton and carbon magnetic resonance studies of the synthetic polypentapeptide of elastin. J. Mol. Biol. 1975; 96: 101-117.
    • (1975) J. Mol. Biol. , vol.96 , pp. 101-117
    • Urry, D.W.1    Mitchell, L.W.2    Ohnishi, T.3    Long, M.M.4
  • 14
    • 0023203479 scopus 로고
    • Study on coacervation of the repeat pentapeptide model of tropoelastin: effect of cations
    • Kondo M, Nakashima Y, Kodama H, Okamoto K. Study on coacervation of the repeat pentapeptide model of tropoelastin: effect of cations. J. Biochem. 1987; 101: 89-94.
    • (1987) J. Biochem. , vol.101 , pp. 89-94
    • Kondo, M.1    Nakashima, Y.2    Kodama, H.3    Okamoto, K.4
  • 15
    • 0034493728 scopus 로고    scopus 로고
    • Trifluoroethanol may form a solvent matrix for assisted hydrophobic interactions between peptide side chains
    • Reiersen H, Rees AR. Trifluoroethanol may form a solvent matrix for assisted hydrophobic interactions between peptide side chains. Protein Eng. 2000; 13: 739-743.
    • (2000) Protein Eng. , vol.13 , pp. 739-743
    • Reiersen, H.1    Rees, A.R.2
  • 16
    • 0036193711 scopus 로고    scopus 로고
    • Elastin-based biopolymers: chemical synthesis and structural characterization of linear and cross-linked poly(OrnGlyGlyOrnGly)
    • Martino M, Perri T, Tamburro AM. Elastin-based biopolymers: chemical synthesis and structural characterization of linear and cross-linked poly(OrnGlyGlyOrnGly). Biomacromolecules 2002; 3: 297-304.
    • (2002) Biomacromolecules , vol.3 , pp. 297-304
    • Martino, M.1    Perri, T.2    Tamburro, A.M.3
  • 17
    • 0344549704 scopus 로고    scopus 로고
    • Thermal behavior and kinetic analysis of the chain unfolding and refolding and of the concomitant nonpolar solvation and desolvation of two elastin-like polymers
    • Reguera J, Lagarón JM, Alonso M, Reboto V, Calvo B, Rodríguez-Cabello JC. Thermal behavior and kinetic analysis of the chain unfolding and refolding and of the concomitant nonpolar solvation and desolvation of two elastin-like polymers. Macromolecules 2003; 36: 8470-8476.
    • (2003) Macromolecules , vol.36 , pp. 8470-8476
    • Reguera, J.1    Lagarón, J.M.2    Alonso, M.3    Reboto, V.4    Calvo, B.5    Rodríguez-Cabello, J.C.6
  • 18
    • 0000300226 scopus 로고
    • The preparation of peptides using mixed carbonic-carboxylic acid anhydrides
    • Vaugham JR Jr, Osato RL. The preparation of peptides using mixed carbonic-carboxylic acid anhydrides. J. Am. Chem. Soc. 1952; 74: 676-678.
    • (1952) J. Am. Chem. Soc. , vol.74 , pp. 676-678
    • Vaugham Jr., J.R.1    Osato, R.L.2
  • 19
    • 0014704672 scopus 로고
    • A new method for synthesis of peptides: activation of the carboxyl group with dicyclohexylcarbodiimide using 1-hydroxybenzotriazoles as additives
    • König W, Geiger R. A new method for synthesis of peptides: activation of the carboxyl group with dicyclohexylcarbodiimide using 1-hydroxybenzotriazoles as additives. Chem. Ber. 1970; 103: 788-798.
    • (1970) Chem. Ber. , vol.103 , pp. 788-798
    • König, W.1    Geiger, R.2
  • 20
  • 21
    • 0030201469 scopus 로고    scopus 로고
    • 2+ ions with elastin coacervate: ion transport study across coacervate layers of alpha-elastin and elastin model polypeptide, (Val-Pro-Gly-Val-Gly)n
    • 2+ ions with elastin coacervate: ion transport study across coacervate layers of alpha-elastin and elastin model polypeptide, (Val-Pro-Gly-Val-Gly)n. Biopolymers 1996; 39: 189-198.
    • (1996) Biopolymers , vol.39 , pp. 189-198
    • Kaibara, K.1    Akinari, Y.2    Okamoto, K.3    Uemura, Y.4    Yamamoto, S.5    Kodama, H.6    Kondo, M.7
  • 22
    • 0014772602 scopus 로고
    • Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides
    • Kaiser E, Colescott RL, Bossinger CD, Cook PI. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal. Biochem. 1970; 34: 595-598.
    • (1970) Anal. Biochem. , vol.34 , pp. 595-598
    • Kaiser, E.1    Colescott, R.L.2    Bossinger, C.D.3    Cook, P.I.4
  • 23
    • 0021115861 scopus 로고
    • Protein structure by Fourier transform infrared spectroscopy: second derivative spectra
    • Susi H, Byler DM. Protein structure by Fourier transform infrared spectroscopy: second derivative spectra. Biochem. Biophys. Res. Commun. 1983; 115: 391-397.
    • (1983) Biochem. Biophys. Res. Commun. , vol.115 , pp. 391-397
    • Susi, H.1    Byler, D.M.2
  • 24
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler DM, Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 1986; 25: 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 25
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • Susi H, Byler DM. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol. 1986; 130: 290-311.
    • (1986) Methods Enzymol. , vol.130 , pp. 290-311
    • Susi, H.1    Byler, D.M.2
  • 26
    • 0022024822 scopus 로고
    • Protein conformation by infrared spectroscopy: resolution enhancement by Fourier self-deconvolution
    • Yang WJ, Griffiths PR, Byler DM, Susi H. Protein conformation by infrared spectroscopy: resolution enhancement by Fourier self-deconvolution. Appl. Spectrosc. 1985; 39: 282-287.
    • (1985) Appl. Spectrosc. , vol.39 , pp. 282-287
    • Yang, W.J.1    Griffiths, P.R.2    Byler, D.M.3    Susi, H.4
  • 27
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong A, Huang P, Caughey WS. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 1990; 29: 3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 28
    • 0041413204 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic studies of peptides: potentials and pitfalls. In: Infrared analysis of peptides and proteins 3
    • Haris PI. Fourier transform infrared spectroscopic studies of peptides: potentials and pitfalls. In: Infrared analysis of peptides and proteins 3. Am. Chem. Soc. Symp. 2000; 750:pp 54-95.
    • (2000) Am. Chem. Soc. Symp. , vol.750 , pp. 54-95
    • Haris, P.I.1
  • 29
    • 0346966848 scopus 로고    scopus 로고
    • An Alternative structure model for the polypentapeptide in elastin
    • Groß PC, Possart W, Zeppezauer M. An Alternative structure model for the polypentapeptide in elastin. Z. Naturforsch. 2003; 58c: 873-878.
    • (2003) Z. Naturforsch. , vol.58 C , pp. 873-878
    • Groß, P.C.1    Possart, W.2    Zeppezauer, M.3
  • 30
    • 0016966143 scopus 로고
    • Conformations of the repeat peptides of elastin in solution: an application of proton and carbon-13 magnetic resonance to the determination of polypeptide secondary structure
    • Urry DW, Long MM. Conformations of the repeat peptides of elastin in solution: an application of proton and carbon-13 magnetic resonance to the determination of polypeptide secondary structure. CRC Crit. Rev. Biochem. 1976; 4: 1-45.
    • (1976) CRC Crit. Rev. Biochem. , vol.4 , pp. 1-45
    • Urry, D.W.1    Long, M.M.2
  • 31
    • 0017444462 scopus 로고
    • On the conformation, coacervation and function of polymeric models of elastin; in Elastin and elastic tissue
    • Urry DW, Long MM. On the conformation, coacervation and function of polymeric models of elastin; in Elastin and elastic tissue. Adv. Exp. Med. Biol. 1977; 79: 685-714.
    • (1977) Adv. Exp. Med. Biol. , vol.79 , pp. 685-714
    • Urry, D.W.1    Long, M.M.2
  • 32
    • 0001756543 scopus 로고
    • Development of a linear helical conformation from its cyclic correlate. β-Spiral model of the elastin poly(pentapeptide) (VPGVG)n
    • Venkatachalam CM, Urry DW. Development of a linear helical conformation from its cyclic correlate. β-Spiral model of the elastin poly(pentapeptide) (VPGVG)n. Macromolecules 1981; 14: 1225-1229.
    • (1981) Macromolecules , vol.14 , pp. 1225-1229
    • Venkatachalam, C.M.1    Urry, D.W.2
  • 33
    • 0023021294 scopus 로고
    • Polytetrapeptide of elastin. Temperature-correlated elastomeric force and structure development
    • Urry DW, Harris RD, Long MM, Prasad KU. Polytetrapeptide of elastin. Temperature-correlated elastomeric force and structure development. Int. J. Pept. Protein Res. 1986; 28: 649-660.
    • (1986) Int. J. Pept. Protein Res. , vol.28 , pp. 649-660
    • Urry, D.W.1    Harris, R.D.2    Long, M.M.3    Prasad, K.U.4
  • 34
    • 0020554865 scopus 로고
    • What is elastin; what is not'
    • Urry DW. What is elastin; what is not'. Ultrastruct. Pathol. 1983; 4: 227-251.
    • (1983) Ultrastruct. Pathol. , vol.4 , pp. 227-251
    • Urry, D.W.1
  • 36
    • 46149138361 scopus 로고
    • Evidence of order in (Val-Pro-Gly)n, a repeating sequence of chick elastin
    • Tamburro AM, Guantieri V. Evidence of order in (Val-Pro-Gly)n, a repeating sequence of chick elastin. Int. J. Biol. Macromol. 1986; 8: 62-63.
    • (1986) Int. J. Biol. Macromol. , vol.8 , pp. 62-63
    • Tamburro, A.M.1    Guantieri, V.2
  • 37
    • 0017758491 scopus 로고
    • Nuclear Overhauser enhancement evidence for inverse temperature dependence of hydrophobic side chain proximity in the polytetrapeptide of tropoelastin
    • Urry DW, Khaled MA, Rapaka RS, Okamoto K. Nuclear Overhauser enhancement evidence for inverse temperature dependence of hydrophobic side chain proximity in the polytetrapeptide of tropoelastin. Biochem. Biophys. Res. Commun. 1977; 79: 700-706.
    • (1977) Biochem. Biophys. Res. Commun. , vol.79 , pp. 700-706
    • Urry, D.W.1    Khaled, M.A.2    Rapaka, R.S.3    Okamoto, K.4
  • 38
    • 0035814373 scopus 로고    scopus 로고
    • Hydrophobic hydration is an important source of elasticity in elastin-based biopolymers
    • Li B, Alonso DOV, Bennion BJ, Daggett V. Hydrophobic hydration is an important source of elasticity in elastin-based biopolymers. J. Am. Chem. Soc. 2001; 123: 11991-11998.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11991-11998
    • Li, B.1    Alonso, D.O.V.2    Bennion, B.J.3    Daggett, V.4
  • 39
    • 0038245213 scopus 로고    scopus 로고
    • Mechanics of elastin: molecular mechanism of biological elasticity and its relationship to contraction
    • Urry DW, Parker TM. Mechanics of elastin: molecular mechanism of biological elasticity and its relationship to contraction. J. Muscle Res. Cell Motility 2002; 23: 543-559.
    • (2002) J. Muscle Res. Cell Motility , vol.23 , pp. 543-559
    • Urry, D.W.1    Parker, T.M.2
  • 40
    • 33847253510 scopus 로고    scopus 로고
    • Effect of NaCl on the exothermic and endothermic components of the inverse temperature transition of a model elastin-like polymer
    • Reguera J, Urry DW, Parker TM, McPherson DT, Rodriguez-Cabello JC. Effect of NaCl on the exothermic and endothermic components of the inverse temperature transition of a model elastin-like polymer. Biomacromolecules 2007; 8: 354-358.
    • (2007) Biomacromolecules , vol.8 , pp. 354-358
    • Reguera, J.1    Urry, D.W.2    Parker, T.M.3    McPherson, D.T.4    Rodriguez-Cabello, J.C.5


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