메뉴 건너뛰기




Volumn 290, Issue 14, 2015, Pages 9251-9261

The self-assembly of a mini-fibril with axial periodicity from a designed collagen-mimetic triple helix

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC FORCE MICROSCOPY; BIOMIMETICS; COLLAGEN; ELECTRON MICROSCOPY; ESCHERICHIA COLI; HYDROXYPROLINE; TRANSMISSION ELECTRON MICROSCOPY;

EID: 84926677376     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.542241     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 0023656926 scopus 로고
    • Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process
    • Kadler, K. E., Hojima, Y., and Prockop, D. J. (1987) Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process. J. Biol. Chem. 262, 15696-15701
    • (1987) J. Biol. Chem. , vol.262 , pp. 15696-15701
    • Kadler, K.E.1    Hojima, Y.2    Prockop, D.J.3
  • 2
    • 0033579423 scopus 로고    scopus 로고
    • Does the triple helical domain of type I collagen encode molecular recognition and fiber assembly while telopeptides serve as catalytic domains? Effect of proteolytic cleavage on fibrillogenesis and on collagen-collagen interaction in fibers
    • Kuznetsova, N., and Leikin, S. (1999) Does the triple helical domain of type I collagen encode molecular recognition and fiber assembly while telopeptides serve as catalytic domains? Effect of proteolytic cleavage on fibrillogenesis and on collagen-collagen interaction in fibers. J. Biol. Chem. 274, 36083-36088
    • (1999) J. Biol. Chem. , vol.274 , pp. 36083-36088
    • Kuznetsova, N.1    Leikin, S.2
  • 4
    • 0002097152 scopus 로고
    • The collagen family: Structure, assembly, and organization in the extracellular matrix
    • (Royce, P. M., and Steinmann, B., eds), Wiley-Liss, New York
    • Kielty, C. M., Hopkinson, I., and Grant, M. E. (1993) The collagen family: structure, assembly, and organization in the extracellular matrix. In Connective Tissue and Its Heritable Disorders (Royce, P. M., and Steinmann, B., eds) pp. 103-147, Wiley-Liss, New York
    • (1993) Connective Tissue and Its Heritable Disorders , pp. 103-147
    • Kielty, C.M.1    Hopkinson, I.2    Grant, M.E.3
  • 5
    • 0031692465 scopus 로고    scopus 로고
    • The collagen fibril: The almost crystalline structure
    • Prockop, D. J., and Fertala, A. (1998) The collagen fibril: the almost crystalline structure. J. Struct. Biol. 122, 111-118
    • (1998) J. Struct. Biol. , vol.122 , pp. 111-118
    • Prockop, D.J.1    Fertala, A.2
  • 6
    • 0016370642 scopus 로고
    • The structure of collagen fibrils
    • Piez, K. A., and Miller, A. (1974) The structure of collagen fibrils. J. Supramol. Struct. 2, 121-137
    • (1974) J. Supramol. Struct. , vol.2 , pp. 121-137
    • Piez, K.A.1    Miller, A.2
  • 7
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution
    • Bella, J., Eaton, M., Brodsky, B., and Berman, H. M. (1994) Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution. Science 266, 75-81
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 10
    • 0015892994 scopus 로고
    • Analysis of the primary structure of collagen for the origins of molecular packing
    • Hulmes, D. J., Miller, A., Parry, D. A., Piez, K. A., and Woodhead-Galloway, J. (1973) Analysis of the primary structure of collagen for the origins of molecular packing. J. Mol. Biol. 79, 137-148
    • (1973) J. Mol. Biol. , vol.79 , pp. 137-148
    • Hulmes, D.J.1    Miller, A.2    Parry, D.A.3    Piez, K.A.4    Woodhead-Galloway, J.5
  • 11
    • 0032546947 scopus 로고    scopus 로고
    • Inhibition of the self-assembly of collagen I into fibrils with synthetic peptides. Demonstration that assembly is driven by specific binding sites on the monomers
    • Prockop, D. J., and Fertala, A. (1998) Inhibition of the self-assembly of collagen I into fibrils with synthetic peptides. Demonstration that assembly is driven by specific binding sites on the monomers. J. Biol. Chem. 273, 15598-15604
    • (1998) J. Biol. Chem. , vol.273 , pp. 15598-15604
    • Prockop, D.J.1    Fertala, A.2
  • 12
    • 0017666765 scopus 로고
    • The mechanism of nucleation for in vitro collagen fibril formation
    • Comper, W. D., and Veis, A. (1977) The mechanism of nucleation for in vitro collagen fibril formation. Biopolymers 16, 2113-2131
    • (1977) Biopolymers , vol.16 , pp. 2113-2131
    • Comper, W.D.1    Veis, A.2
  • 13
    • 33845959679 scopus 로고    scopus 로고
    • Self-association of collagen triple helic peptides into higher order structures
    • Kar, K., Amin, P., Bryan, M. A., Persikov, A. V., Mohs, A., Wang, Y. H., and Brodsky, B. (2006) Self-association of collagen triple helic peptides into higher order structures. J. Biol. Chem. 281, 33283-33290
    • (2006) J. Biol. Chem. , vol.281 , pp. 33283-33290
    • Kar, K.1    Amin, P.2    Bryan, M.A.3    Persikov, A.V.4    Mohs, A.5    Wang, Y.H.6    Brodsky, B.7
  • 14
    • 0035941338 scopus 로고    scopus 로고
    • Unhydroxylated triple helical collagen I produced in transgenic plants provides new clues on the role of hydroxyproline in collagen folding and fibril formation
    • Perret, S., Merle, C., Bernocco, S., Berland, P., Garrone, R., Hulmes, D. J., Theisen, M., and Ruggiero, F. (2001) Unhydroxylated triple helical collagen I produced in transgenic plants provides new clues on the role of hydroxyproline in collagen folding and fibril formation. J. Biol. Chem. 276, 43693-43698
    • (2001) J. Biol. Chem. , vol.276 , pp. 43693-43698
    • Perret, S.1    Merle, C.2    Bernocco, S.3    Berland, P.4    Garrone, R.5    Hulmes, D.J.6    Theisen, M.7    Ruggiero, F.8
  • 15
    • 33644777607 scopus 로고    scopus 로고
    • Self-assembly of synthetic collagen triple helices
    • Kotch, F. W., and Raines, R. T. (2006) Self-assembly of synthetic collagen triple helices. Proc. Natl. Acad. Sci. U.S.A. 103, 3028-3033
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 3028-3033
    • Kotch, F.W.1    Raines, R.T.2
  • 16
    • 33744946043 scopus 로고    scopus 로고
    • Self-assembly of peptide-amphiphile nanofibers: The roles of hydrogen bonding and amphiphilic packing
    • Paramonov, S. E., Jun, H. W., and Hartgerink, J. D. (2006) Self-assembly of peptide-amphiphile nanofibers: the roles of hydrogen bonding and amphiphilic packing. J. Am. Chem. Soc. 128, 7291-7298
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7291-7298
    • Paramonov, S.E.1    Jun, H.W.2    Hartgerink, J.D.3
  • 17
    • 31544469198 scopus 로고    scopus 로고
    • Modulation of peptide-amphiphile nanofibers via phospholipid inclusions
    • Paramonov, S. E., Jun, H. W., and Hartgerink, J. D. (2006) Modulation of peptide-amphiphile nanofibers via phospholipid inclusions. Biomacromolecules 7, 24-26
    • (2006) Biomacromolecules , vol.7 , pp. 24-26
    • Paramonov, S.E.1    Jun, H.W.2    Hartgerink, J.D.3
  • 18
    • 33847654171 scopus 로고    scopus 로고
    • Collagen-related peptides: Self-assembly of short, single strands into a functional biomaterial of micrometer scale
    • Cejas, M. A., Kinney, W. A., Chen, C., Leo, G. C., Tounge, B. A., Vinter, J. G., Joshi, P. P., and Maryanoff, B. E. (2007) Collagen-related peptides: self-assembly of short, single strands into a functional biomaterial of micrometer scale. J. Am. Chem. Soc. 129, 2202-2203
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 2202-2203
    • Cejas, M.A.1    Kinney, W.A.2    Chen, C.3    Leo, G.C.4    Tounge, B.A.5    Vinter, J.G.6    Joshi, P.P.7    Maryanoff, B.E.8
  • 19
    • 69049114117 scopus 로고    scopus 로고
    • Aromatic interactions promote self-association of collagen triple-helical peptides to higher-order structures
    • Kar, K., Ibrar, S., Nanda, V., Getz, T. M., Kunapuli, S. P., and Brodsky, B. (2009) Aromatic interactions promote self-association of collagen triple-helical peptides to higher-order structures. Biochemistry 48, 7959-7968
    • (2009) Biochemistry , vol.48 , pp. 7959-7968
    • Kar, K.1    Ibrar, S.2    Nanda, V.3    Getz, T.M.4    Kunapuli, S.P.5    Brodsky, B.6
  • 21
    • 57749112119 scopus 로고    scopus 로고
    • Recombinant collagen studies link the severe conformational changes induced by osteogenesis imperfecta mutations to the disruption of a set of interchain salt bridges
    • Xu, K., Nowak, I., Kirchner, M., and Xu, Y. (2008) Recombinant collagen studies link the severe conformational changes induced by osteogenesis imperfecta mutations to the disruption of a set of interchain salt bridges. J. Biol. Chem. 283, 34337-34344
    • (2008) J. Biol. Chem. , vol.283 , pp. 34337-34344
    • Xu, K.1    Nowak, I.2    Kirchner, M.3    Xu, Y.4
  • 25
    • 0018959643 scopus 로고
    • Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen
    • Bächinger, H. P., Bruckner, P., Timpl, R., Prockop, D. J., and Engel, J. (1980) Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Eur. J. Biochem. 106, 619-632
    • (1980) Eur. J. Biochem. , vol.106 , pp. 619-632
    • Bächinger, H.P.1    Bruckner, P.2    Timpl, R.3    Prockop, D.J.4    Engel, J.5
  • 26
    • 0036290657 scopus 로고    scopus 로고
    • Nucleation and propagation of the collagen triple helix in single-chain and trimerized peptides: Transition from third to first order kinetics
    • Boudko, S., Frank, S., Kammerer, R. A., Stetefeld, J., Schulthess, T., Landwehr, R., Lustig, A., Bächinger, H. P., and Engel, J. (2002) Nucleation and propagation of the collagen triple helix in single-chain and trimerized peptides: transition from third to first order kinetics. J. Mol. Biol. 317, 459-470
    • (2002) J. Mol. Biol. , vol.317 , pp. 459-470
    • Boudko, S.1    Frank, S.2    Kammerer, R.A.3    Stetefeld, J.4    Schulthess, T.5    Landwehr, R.6    Lustig, A.7    Bächinger, H.P.8    Engel, J.9
  • 27
    • 21444453832 scopus 로고    scopus 로고
    • Prediction of collagen stability from amino acid sequence
    • Persikov, A. V., Ramshaw, J. A., and Brodsky, B. (2005) Prediction of collagen stability from amino acid sequence. J. Biol. Chem. 280, 19343-19349
    • (2005) J. Biol. Chem. , vol.280 , pp. 19343-19349
    • Persikov, A.V.1    Ramshaw, J.A.2    Brodsky, B.3
  • 28
    • 0040358808 scopus 로고    scopus 로고
    • The collagen-like peptide (GER)15GPCCG forms pH-dependent covalently linked triple helical trimers
    • Mechling, D. E., and Bachinger, H. P. (2000) The collagen-like peptide (GER)15GPCCG forms pH-dependent covalently linked triple helical trimers. J. Biol. Chem. 275, 14532-14536
    • (2000) J. Biol. Chem. , vol.275 , pp. 14532-14536
    • Mechling, D.E.1    Bachinger, H.P.2
  • 29
    • 0029837626 scopus 로고    scopus 로고
    • Acetyl-terminated and template-assembled collagen-based polypeptides composed of Gly-Pro-Hyp sequences: 2. Synthesis and conformational analysis by circular dichroism, ultraviolet absorbance and optical rotation
    • Feng, Y., Melacini, G., Taulane, J. P., and Goodman, M. (1996) Acetyl-terminated and template-assembled collagen-based polypeptides composed of Gly-Pro-Hyp sequences: 2. synthesis and conformational analysis by circular dichroism, ultraviolet absorbance and optical rotation. J. Am. Chem. Soc. 118, 10351-10358
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10351-10358
    • Feng, Y.1    Melacini, G.2    Taulane, J.P.3    Goodman, M.4
  • 31
    • 0020248260 scopus 로고
    • Synthesis and investigation of collagen model peptides
    • Heidemann, E., and Roth, W. (1982) Synthesis and investigation of collagen model peptides. Adv. Polymer Sci. 43, 143-203
    • (1982) Adv. Polymer Sci. , vol.43 , pp. 143-203
    • Heidemann, E.1    Roth, W.2
  • 32
    • 1642385074 scopus 로고    scopus 로고
    • Characterization of heterogeneity of self-associating systems using equilibrium sedimentation techniques
    • Xu, Y. (2004) Characterization of heterogeneity of self-associating systems using equilibrium sedimentation techniques. Biophys. Chem. 108, 141-163
    • (2004) Biophys. Chem. , vol.108 , pp. 141-163
    • Xu, Y.1
  • 34
    • 0002459842 scopus 로고
    • The function of hydroxyproline in collanges
    • Gustavson, K. H. (1955) The function of hydroxyproline in collanges. Nature 175, 70-74
    • (1955) Nature , vol.175 , pp. 70-74
    • Gustavson, K.H.1
  • 36
    • 0014690899 scopus 로고
    • Effect of polymer size on the inhibition of protocollagen proline hydroxylase by polyproline II
    • Prockop, D. J., and Kivirikko, K. I. (1969) Effect of polymer size on the inhibition of protocollagen proline hydroxylase by polyproline II. J. Biol. Chem. 244, 4838-4842
    • (1969) J. Biol. Chem. , vol.244 , pp. 4838-4842
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 37
    • 0019888241 scopus 로고
    • Collagen self-assembly in vitro: Differentiating specific telopeptide-dependent interactions using selective enzyme modification and the addition of free amino telopeptide
    • Helseth, D. L., Jr., and Veis, A. (1981) Collagen self-assembly in vitro: differentiating specific telopeptide-dependent interactions using selective enzyme modification and the addition of free amino telopeptide. J. Biol. Chem. 256, 7118-7128
    • (1981) J. Biol. Chem. , vol.256 , pp. 7118-7128
    • Helseth, D.L.1    Veis, A.2
  • 38
    • 0016804150 scopus 로고
    • Oblique banding pattern in collagen fibrils reconstituted in vitro after trypsin treatment
    • Ghosh, S. K., and Mitra, H. P. (1975) Oblique banding pattern in collagen fibrils reconstituted in vitro after trypsin treatment. Biochim. Biophys. Acta 405, 340-346
    • (1975) Biochim. Biophys. Acta , vol.405 , pp. 340-346
    • Ghosh, S.K.1    Mitra, H.P.2
  • 39
    • 0013863815 scopus 로고
    • Action of proteolytic enzymes on tropocollagen and insoluble collagen
    • Drake, M. P., Davison, P. F., Bump, S., and Schmitt, F. O. (1966) Action of proteolytic enzymes on tropocollagen and insoluble collagen. Biochemistry 5, 301-312
    • (1966) Biochemistry , vol.5 , pp. 301-312
    • Drake, M.P.1    Davison, P.F.2    Bump, S.3    Schmitt, F.O.4
  • 40
    • 0014967257 scopus 로고
    • Electron microscope studies of the effects of endo- and exopeptidase digestion on tropocollagen. A novel concept of the role of terminal regions in fibrillogenesis
    • Leibovich, S. J., and Weiss, J. B. (1970) Electron microscope studies of the effects of endo- and exopeptidase digestion on tropocollagen. A novel concept of the role of terminal regions in fibrillogenesis. Biochim. Biophys. Acta 214, 445-454
    • (1970) Biochim. Biophys. Acta , vol.214 , pp. 445-454
    • Leibovich, S.J.1    Weiss, J.B.2
  • 41
    • 0030963588 scopus 로고    scopus 로고
    • The collagen triple helix structure
    • Brodsky, B., and Ramshaw, J. A. (1997) The collagen triple helix structure. Matrix Biol. 15, 545-554
    • (1997) Matrix Biol. , vol.15 , pp. 545-554
    • Brodsky, B.1    Ramshaw, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.