메뉴 건너뛰기




Volumn 22, Issue 1 E, 2010, Pages

Investigating by circular dichroism some amyloidogenic elastin-derived polypeptides

Author keywords

amyloid like; Cotton effect; elastin; peptide; secondary structure

Indexed keywords

AMYLOID; ELASTIN; POLYPEPTIDE; THIOFLAVINE; TROPOELASTIN;

EID: 78349260062     PISSN: 08990042     EISSN: 1520636X     Source Type: Journal    
DOI: 10.1002/chir.20869     Document Type: Conference Paper
Times cited : (15)

References (57)
  • 1
    • 0033006918 scopus 로고    scopus 로고
    • Elastin: Molecular description and function
    • Debelle L, Tamburro AM,. Elastin: molecular description and function. Int J Biochem Cell Biol 1999; 31: 261 272.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 261-272
    • Debelle, L.1    Tamburro, A.M.2
  • 2
    • 0032533711 scopus 로고    scopus 로고
    • Biochemistry of tropoelastin
    • Vrhovski B, Weiss AS,. 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
    • 0242499494 scopus 로고    scopus 로고
    • Dissection of human tropoelastin: Exon-by-exon chemical synthesis and related conformational studies
    • Tamburro AM, Bochicchio B, Pepe A,. Dissection of human tropoelastin: exon-by-exon chemical synthesis and related conformational studies. Biochemistry 2003; 42: 13347 13362.
    • (2003) Biochemistry , vol.42 , pp. 13347-13362
    • Tamburro, A.M.1    Bochicchio, B.2    Pepe, A.3
  • 4
    • 22844438705 scopus 로고    scopus 로고
    • The dissection of human tropoelastin: From the molecular structure to the self-assembly to the elasticity mechanism
    • Paris
    • Tamburro AM, Bochicchio B, Pepe A,. The dissection of human tropoelastin: from the molecular structure to the self-assembly to the elasticity mechanism. Pathol Biol (Paris) 2005; 53: 383 389.
    • (2005) Pathol Biol , vol.53 , pp. 383-389
    • Tamburro, A.M.1    Bochicchio, B.2    Pepe, A.3
  • 5
    • 58149242893 scopus 로고    scopus 로고
    • Investigating by CD the molecular mechanism of elasticity of elastomeric proteins
    • Bochicchio B, Pepe A, Tamburro AM,. Investigating by CD the molecular mechanism of elasticity of elastomeric proteins. Chirality 2008; 20: 985 994.
    • (2008) Chirality , vol.20 , pp. 985-994
    • Bochicchio, B.1    Pepe, A.2    Tamburro, A.M.3
  • 7
    • 0030809954 scopus 로고    scopus 로고
    • Coacervation characteristics of recombinant human tropoelastin
    • Vrhovski B, Jensen S, Weiss AS,. Coacervation characteristics of recombinant human tropoelastin. Eur J Biochem 1997; 250: 92 98.
    • (1997) Eur J Biochem , vol.250 , pp. 92-98
    • Vrhovski, B.1    Jensen, S.2    Weiss, A.S.3
  • 8
    • 0015967414 scopus 로고
    • Communication: Coacervation of tropoelastin results in fiber formation
    • Cox BA, Starcher BC, Urry DW,. Communication: coacervation of tropoelastin results in fiber formation. J Biol Chem 1974; 249: 997 998.
    • (1974) J Biol Chem , vol.249 , pp. 997-998
    • Cox, B.A.1    Starcher, B.C.2    Urry, D.W.3
  • 9
    • 0019012422 scopus 로고
    • Spectroscopic and electron micrographic studies on the repeat tetrapeptide of tropoelastin: (Val-Pro-Gly-Gly)n
    • Long MM, Rapaka RS, Volpin D, Pasquali-Ronchetti I, Urry DW,. Spectroscopic and electron micrographic studies on the repeat tetrapeptide of tropoelastin: (Val-Pro-Gly-Gly)n. Arch Biochem Biophys 1980; 201: 445 452.
    • (1980) Arch Biochem Biophys , vol.201 , pp. 445-452
    • Long, M.M.1    Rapaka, R.S.2    Volpin, D.3    Pasquali-Ronchetti, I.4    Urry, D.W.5
  • 10
    • 0015880008 scopus 로고
    • Coacervation of alpha-elastin results in fiber formation
    • Cox BA, Starcher BC, Urry DW,. Coacervation of alpha-elastin results in fiber formation. Biochim Biophys Acta 1973; 317: 209 213.
    • (1973) Biochim Biophys Acta , vol.317 , pp. 209-213
    • Cox, B.A.1    Starcher, B.C.2    Urry, D.W.3
  • 12
    • 34249829242 scopus 로고    scopus 로고
    • Supramolecular Organization of elastin and elastin-related nanostructured biopolymers
    • Pepe A, Bochicchio B, Tamburro AM,. Supramolecular Organization of elastin and elastin-related nanostructured biopolymers. Nanomedicine 2007; 2: 203 218.
    • (2007) Nanomedicine , vol.2 , pp. 203-218
    • Pepe, A.1    Bochicchio, B.2    Tamburro, A.M.3
  • 13
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • Tycko R,. Progress towards a molecular-level structural understanding of amyloid fibrils. Curr Opin Struct Biol 2004; 14: 96 103.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 96-103
    • Tycko, R.1
  • 14
    • 45049083085 scopus 로고    scopus 로고
    • Mapping of macrophage elastase cleavage sites in insoluble human skin elastin
    • Taddese S, Weiss AS, Neubert RH, Schmelzer CE,. Mapping of macrophage elastase cleavage sites in insoluble human skin elastin. Matrix Biol 2008; 27: 420 428.
    • (2008) Matrix Biol , vol.27 , pp. 420-428
    • Taddese, S.1    Weiss, A.S.2    Neubert, R.H.3    Schmelzer, C.E.4
  • 15
    • 54049087842 scopus 로고    scopus 로고
    • Amyloid deposits in senile vertebral arteries, immunohistological and ultrastructural findings
    • Doostkam S, Bohl JR, Sahraian A, Mahjoor AA,. Amyloid deposits in senile vertebral arteries, immunohistological and ultrastructural findings. Pak J Biol Sci 2008; 11: 1852 1855.
    • (2008) Pak J Biol Sci , vol.11 , pp. 1852-1855
    • Doostkam, S.1    Bohl, J.R.2    Sahraian, A.3    Mahjoor, A.A.4
  • 16
    • 60249089077 scopus 로고    scopus 로고
    • On enhancers and inhibitors of elastin-derived amyloidogenesis
    • Bochicchio B, Lorusso M, Pepe A, Tamburro AM,. On enhancers and inhibitors of elastin-derived amyloidogenesis. Nanomedicine 2009; 4: 31 46.
    • (2009) Nanomedicine , vol.4 , pp. 31-46
    • Bochicchio, B.1    Lorusso, M.2    Pepe, A.3    Tamburro, A.M.4
  • 17
    • 34648822550 scopus 로고    scopus 로고
    • Elastic fibers and amyloid deposition in vascular tissue
    • Bochicchio B, Pepe A, Tamburro AM,. Elastic fibers and amyloid deposition in vascular tissue. Future Neurol 2007; 2: 523 536.
    • (2007) Future Neurol , vol.2 , pp. 523-536
    • Bochicchio, B.1    Pepe, A.2    Tamburro, A.M.3
  • 18
    • 13244275209 scopus 로고    scopus 로고
    • Supramolecular amyloid-like assembly of the polypeptide sequence coded by exon 30 of human tropoelastin
    • Tamburro AM, Pepe A, Bochicchio B, Quaglino D, Ronchetti IP,. Supramolecular amyloid-like assembly of the polypeptide sequence coded by exon 30 of human tropoelastin. J Biol Chem 2005; 280: 2682 2690.
    • (2005) J Biol Chem , vol.280 , pp. 2682-2690
    • Tamburro, A.M.1    Pepe, A.2    Bochicchio, B.3    Quaglino, D.4    Ronchetti, I.P.5
  • 19
    • 36649020438 scopus 로고    scopus 로고
    • Investigating the amyloidogenic nanostructured sequences of elastin: Sequence encoded by exon 28 of human tropoelastin gene
    • Bochicchio B, Pepe A, Flamia R, Lorusso M, Tamburro AM,. Investigating the amyloidogenic nanostructured sequences of elastin: sequence encoded by exon 28 of human tropoelastin gene. Biomacromolecules 2007; 8: 3478 3486.
    • (2007) Biomacromolecules , vol.8 , pp. 3478-3486
    • Bochicchio, B.1    Pepe, A.2    Flamia, R.3    Lorusso, M.4    Tamburro, A.M.5
  • 20
    • 34648850062 scopus 로고    scopus 로고
    • Molecular and supramolecular structural studies on human tropoelastin sequences
    • Ostuni A, Bochicchio B, Armentano MF, Bisaccia F, Tamburro AM,. Molecular and supramolecular structural studies on human tropoelastin sequences. Biophys J 2007; 93: 3640 3651.
    • (2007) Biophys J , vol.93 , pp. 3640-3651
    • Ostuni, A.1    Bochicchio, B.2    Armentano, M.F.3    Bisaccia, F.4    Tamburro, A.M.5
  • 21
    • 0027068138 scopus 로고
    • Synthesis and structural studies of a pentapeptide sequence of elastin. Poly (Val-Gly-Gly-Leu-Gly)
    • Tamburro AM, Guantieri V, Gordini DD,. Synthesis and structural studies of a pentapeptide sequence of elastin. Poly (Val-Gly-Gly-Leu-Gly). J Biomol Struct Dyn 1992; 10: 441 454.
    • (1992) J Biomol Struct Dyn , vol.10 , pp. 441-454
    • Tamburro, A.M.1    Guantieri, V.2    Gordini, D.D.3
  • 22
    • 0033963010 scopus 로고    scopus 로고
    • Synthesis and structural characterization of poly(LGGVG), an elastin-like polypeptide
    • Martino M, Coviello A, Tamburro AM,. Synthesis and structural characterization of poly(LGGVG), an elastin-like polypeptide. Int J Biol Macromol 2000; 27: 59 64.
    • (2000) Int J Biol Macromol , vol.27 , pp. 59-64
    • Martino, M.1    Coviello, A.2    Tamburro, A.M.3
  • 24
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson MR,. Techniques to study amyloid fibril formation in vitro. Methods 2004; 34: 151 160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 25
    • 0036444474 scopus 로고    scopus 로고
    • In vitro fibrillogenesis of the amyloid beta 142 peptide: Cholesterol potentiation and aspirin inhibition
    • Harris JR,. In vitro fibrillogenesis of the amyloid beta 142 peptide: cholesterol potentiation and aspirin inhibition. Micron 2002; 33: 609 626.
    • (2002) Micron , vol.33 , pp. 609-626
    • Harris, J.R.1
  • 26
    • 24044518189 scopus 로고    scopus 로고
    • Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism
    • Carrotta R, Manno M, Bulone D, Martorana V, San Biagio PL,. Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism. J Biol Chem 2005; 280: 30001 30008.
    • (2005) J Biol Chem , vol.280 , pp. 30001-30008
    • Carrotta, R.1    Manno, M.2    Bulone, D.3    Martorana, V.4    San Biagio, P.L.5
  • 28
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • LeVine H III,. Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol 1999; 309: 274 284.
    • (1999) Methods Enzymol , vol.309 , pp. 274-284
    • Levine Iii, H.1
  • 31
    • 0031570763 scopus 로고    scopus 로고
    • Stopped-flow kinetics reveal multiple phases of thioflavin T binding to Alzheimer b(140) amyloid fibrils
    • LeVine H,. Stopped-flow kinetics reveal multiple phases of thioflavin T binding to Alzheimer b(140) amyloid fibrils. Arch Biochem Biophys 1997; 342: 306 316.
    • (1997) Arch Biochem Biophys , vol.342 , pp. 306-316
    • Levine, H.1
  • 32
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
    • Naiki H, Higuchi K, Hosokawa M, Takeda T,. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal Biochem 1989; 177: 244 249.
    • (1989) Anal Biochem , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 33
    • 0002815020 scopus 로고    scopus 로고
    • Early detection of inflammation associated amyloid in murine spleen using thioflavin T fluorescence of spleen homogenates: Implications for amyloidogenesis
    • Graether SP, Kisilevsky R, Young ID,. Early detection of inflammation associated amyloid in murine spleen using thioflavin T fluorescence of spleen homogenates: implications for amyloidogenesis. Amyloid Int J Exp Clin Invest 1996; 3: 20 27.
    • (1996) Amyloid Int J Exp Clin Invest , vol.3 , pp. 20-27
    • Graether, S.P.1    Kisilevsky, R.2    Young, I.D.3
  • 34
    • 0001781312 scopus 로고
    • Double refringence of amyloid Congo red complex in histological section
    • Ladewig P,. Double refringence of amyloid Congo red complex in histological section. Nature 1945; 156: 81.
    • (1945) Nature , vol.156 , pp. 81
    • Ladewig, P.1
  • 35
    • 0000880131 scopus 로고
    • On the binding of Congo red by amyloid
    • Puchtler H,. On the binding of Congo red by amyloid. J Histochem Cytochem 1962; 10: 355.
    • (1962) J Histochem Cytochem , vol.10 , pp. 355
    • Puchtler, H.1
  • 36
    • 0015408029 scopus 로고
    • The relation of the properties of Congo red-stained amyloid fibrils to the -conformation
    • Glenner GG, Eanes ED, Page DL,. The relation of the properties of Congo red-stained amyloid fibrils to the -conformation. J Histochem Cytochem 1972; 20: 821 826.
    • (1972) J Histochem Cytochem , vol.20 , pp. 821-826
    • Glenner, G.G.1    Eanes, E.D.2    Page, D.L.3
  • 37
    • 0016287131 scopus 로고
    • Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods
    • Cooper JH,. Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods. Lab Invest 1974; 31: 232 238.
    • (1974) Lab Invest , vol.31 , pp. 232-238
    • Cooper, J.H.1
  • 38
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by congo red spectral shift assay
    • Klunk WE, Jacob RF, Mason RP,. Quantifying amyloid by congo red spectral shift assay. Methods Enzymol 1999; 309: 285 305.
    • (1999) Methods Enzymol , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 40
    • 0000930795 scopus 로고
    • Etude histochimique des plaques seniles
    • Divry P,. Etude histochimique des plaques seniles. J Belge Neurol Psychiatr 1927; 27: 643 657.
    • (1927) J Belge Neurol Psychiatr , vol.27 , pp. 643-657
    • Divry, P.1
  • 41
    • 0024066499 scopus 로고
    • Reassessment of the electronic circular dichroism criteria for random coil conformations of poly(L-lysine) and the implications for protein folding and denaturation studies
    • Drake AF, Siligardi G, Gibbons WA,. Reassessment of the electronic circular dichroism criteria for random coil conformations of poly(L-lysine) and the implications for protein folding and denaturation studies. Biophys Chem 1988; 31: 143 146.
    • (1988) Biophys Chem , vol.31 , pp. 143-146
    • Drake, A.F.1    Siligardi, G.2    Gibbons, W.A.3
  • 42
    • 0002251831 scopus 로고
    • Circular dichroism and conformation of unordered polypeptides
    • Woody RW,. Circular dichroism and conformation of unordered polypeptides. Adv Biophys Chem 1992; 2: 37 79.
    • (1992) Adv Biophys Chem , vol.2 , pp. 37-79
    • Woody, R.W.1
  • 43
    • 0036400325 scopus 로고    scopus 로고
    • Is polyproline II a major backbone conformation in unfolded proteins?
    • Shi Z, Woody RW, Kallenbach NR,. Is polyproline II a major backbone conformation in unfolded proteins? Adv Protein Chem 2002; 62: 163 240.
    • (2002) Adv Protein Chem , vol.62 , pp. 163-240
    • Shi, Z.1    Woody, R.W.2    Kallenbach, N.R.3
  • 45
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions
    • Bochicchio B, Tamburro AM,. Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and functions. Chirality 2002; 14: 782 792.
    • (2002) Chirality , vol.14 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 46
    • 0029058133 scopus 로고
    • The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides
    • Siligardi G, Drake AF,. The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides. Biopolymers 1995; 37: 281 292.
    • (1995) Biopolymers , vol.37 , pp. 281-292
    • Siligardi, G.1    Drake, A.F.2
  • 47
    • 0014378447 scopus 로고
    • Circular dichroism of poly-L-proline in an unordered conformation
    • Tiffany ML, Krimm S,. Circular dichroism of poly-L-proline in an unordered conformation. Biopolymers 1968; 6: 1767 1770.
    • (1968) Biopolymers , vol.6 , pp. 1767-1770
    • Tiffany, M.L.1    Krimm, S.2
  • 49
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield N, Fasman GD,. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 1969; 8: 4108 4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 50
    • 0028981219 scopus 로고
    • Structure-activity analyses of beta-amyloid peptides: Contributions of the beta 2535 region to aggregation and neurotoxicity
    • Pike CJ, Walencewicz-Wasserman AJ, Kosmoski J, Cribbs DH, Glabe CG, Cotman CW,. Structure-activity analyses of beta-amyloid peptides: contributions of the beta 2535 region to aggregation and neurotoxicity. J Neurochem 1995; 64: 253 265.
    • (1995) J Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 51
    • 27944455577 scopus 로고    scopus 로고
    • Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: An induced circular dichroism/DFT study
    • Dzwolak W, Pecul M,. Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: an induced circular dichroism/DFT study. FEBS Lett 2005; 579: 6601 6603.
    • (2005) FEBS Lett , vol.579 , pp. 6601-6603
    • Dzwolak, W.1    Pecul, M.2
  • 54
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes ED, Glenner GG,. X-ray diffraction studies on amyloid filaments. J Histochem Cytochem 1968; 16: 673 677.
    • (1968) J Histochem Cytochem , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 55
    • 57849137449 scopus 로고    scopus 로고
    • Formation of nanostructures by self-assembly of an elastin peptide
    • Pepe A, Armenante MR, Bochicchio B, Tamburro AM,. Formation of nanostructures by self-assembly of an elastin peptide. Soft Matter 2009; 5: 104 113.
    • (2009) Soft Matter , vol.5 , pp. 104-113
    • Pepe, A.1    Armenante, M.R.2    Bochicchio, B.3    Tamburro, A.M.4
  • 56
    • 2642567722 scopus 로고    scopus 로고
    • Abeta(128) fragment of the amyloid peptide predominantly adopts a polyproline II conformation in an acidic solution
    • Eker F, Griebenow K, Schweitzer-Stenner R,. Abeta(128) fragment of the amyloid peptide predominantly adopts a polyproline II conformation in an acidic solution. Biochemistry 2004; 43: 6893 6898.
    • (2004) Biochemistry , vol.43 , pp. 6893-6898
    • Eker, F.1    Griebenow, K.2    Schweitzer-Stenner, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.