메뉴 건너뛰기




Volumn 45, Issue 12, 2012, Pages 2142-2150

Lipid-like self-assembling peptides

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DODECYL SULFATE SODIUM; LIPID; MEMBRANE PROTEIN; NANOTUBE; PEPTIDE; PREBIOTIC AGENT; RNA;

EID: 84871301136     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar300034v     Document Type: Article
Times cited : (108)

References (44)
  • 1
    • 0017620007 scopus 로고
    • Synthesis of phospholipids and membranes in prebiotic conditions
    • Hargreaves, W. R.; Mulvihill, S. J.; Deamer, D. W. Synthesis of phospholipids and membranes in prebiotic conditions Nature 1977, 266, 78-80
    • (1977) Nature , vol.266 , pp. 78-80
    • Hargreaves, W.R.1    Mulvihill, S.J.2    Deamer, D.W.3
  • 2
    • 0004155427 scopus 로고
    • 1 st ed. Freeman & Co. San Francisco, CA.
    • Stryer, L. Biochemistry, 1 st ed.; Freeman & Co.: San Francisco, CA, 1978.
    • (1978) Biochemistry
    • Stryer, L.1
  • 3
    • 0000444955 scopus 로고
    • Thermal copolymerization of amino acids to a product resembling protein
    • Fox, S. W.; Harada, K. Thermal copolymerization of amino acids to a product resembling protein Science 1958, 128, 1214
    • (1958) Science , vol.128 , pp. 1214
    • Fox, S.W.1    Harada, K.2
  • 4
    • 0016715114 scopus 로고
    • Beta structures of alternating polypeptides and their possible prebiotic significance
    • Brack, A.; Orgel, L. E. Beta structures of alternating polypeptides and their possible prebiotic significance Nature 1975, 256, 383-387
    • (1975) Nature , vol.256 , pp. 383-387
    • Brack, A.1    Orgel, L.E.2
  • 5
    • 0019546705 scopus 로고
    • Enantiomer enrichment in early peptides
    • Brack, A.; Spach, G. Enantiomer enrichment in early peptides Origins Life 1981, 11, 135-142
    • (1981) Origins Life , vol.11 , pp. 135-142
    • Brack, A.1    Spach, G.2
  • 6
    • 0024231451 scopus 로고
    • Construction of protocellular structures under simulated primitive earth conditions
    • Yanagawa, H.; Ogawa, Y.; Kojima, K.; Ito, M. Construction of protocellular structures under simulated primitive earth conditions Origins Life Evol. Biospheres 1988, 18, 179-207
    • (1988) Origins Life Evol. Biospheres , vol.18 , pp. 179-207
    • Yanagawa, H.1    Ogawa, Y.2    Kojima, K.3    Ito, M.4
  • 7
    • 37049243502 scopus 로고
    • A production of amino acids under possible primitive earth conditions
    • Miller, S. L. A production of amino acids under possible primitive earth conditions Science 1953, 117, 528-529
    • (1953) Science , vol.117 , pp. 528-529
    • Miller, S.L.1
  • 8
    • 33748637711 scopus 로고
    • Organic compound synthesis on the primitive earth
    • Miller, S. L.; Urey, H. C. Organic compound synthesis on the primitive earth Science 1959, 130, 245-251
    • (1959) Science , vol.130 , pp. 245-251
    • Miller, S.L.1    Urey, H.C.2
  • 9
    • 36949085702 scopus 로고
    • Amino-acid synthesis from hydrogen cyanide under possible primitive earth conditions
    • Oro, J.; Kamat, S. S. Amino-acid synthesis from hydrogen cyanide under possible primitive earth conditions Nature 1961, 190, 442-443
    • (1961) Nature , vol.190 , pp. 442-443
    • Oro, J.1    Kamat, S.S.2
  • 10
    • 0028036289 scopus 로고
    • Impact melting of frozen oceans on the early Earth: Implications for the origin of life
    • Bada, J. L.; Bigham, C.; Miller, S. L. Impact melting of frozen oceans on the early Earth: Implications for the origin of life Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 1248-1250
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1248-1250
    • Bada, J.L.1    Bigham, C.2    Miller, S.L.3
  • 12
    • 0018795087 scopus 로고
    • Inadequacy of prebiotic synthesis as origin of proteinous amino acids
    • Wong, J. T.-F.; Bronskill, P. M. Inadequacy of prebiotic synthesis as origin of proteinous amino acids J. Mol. Evol. 1979, 13, 115-125
    • (1979) J. Mol. Evol. , vol.13 , pp. 115-125
    • Wong, J.T.-F.1    Bronskill, P.M.2
  • 13
    • 0024972533 scopus 로고
    • Pre-biotic organic matter from comets and asteroids
    • Anders, E. Pre-biotic organic matter from comets and asteroids Nature 1989, 342, 255-257
    • (1989) Nature , vol.342 , pp. 255-257
    • Anders, E.1
  • 14
    • 0026513112 scopus 로고
    • Endogenous production, exogenous delivery and impact-shock synthesis of organic molecules: An inventory for the origins of life
    • Chyba, C.; Sagan, C. Endogenous production, exogenous delivery and impact-shock synthesis of organic molecules: an inventory for the origins of life Nature 1992, 355, 125-132
    • (1992) Nature , vol.355 , pp. 125-132
    • Chyba, C.1    Sagan, C.2
  • 15
    • 0035956925 scopus 로고    scopus 로고
    • Extraterrestrial amino acids in Orgueil and Ivuna: Tracing the parent body of CI type carbonaceous chondrites
    • Ehrenfreund, P.; Glavin, D. P.; Botta, O.; Cooper, G.; Bada, J. L. Extraterrestrial amino acids in Orgueil and Ivuna: tracing the parent body of CI type carbonaceous chondrites Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 2138-2142
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2138-2142
    • Ehrenfreund, P.1    Glavin, D.P.2    Botta, O.3    Cooper, G.4    Bada, J.L.5
  • 16
    • 0038843223 scopus 로고
    • Direct synthesis of polypeptides. I. Polycondensation of glycine in aqueous ammonia
    • Oro, J.; Guidry, C. L. Direct synthesis of polypeptides. I. Polycondensation of glycine in aqueous ammonia Arch. Biochem. Biophys. 1961, 93, 166-171
    • (1961) Arch. Biochem. Biophys. , vol.93 , pp. 166-171
    • Oro, J.1    Guidry, C.L.2
  • 17
    • 0021309670 scopus 로고
    • Acyl silicates and acyl aluminates as activated intermediates in peptide formation on clays
    • White, D. H.; Kennedy, R. M.; Macklin, J. Acyl silicates and acyl aluminates as activated intermediates in peptide formation on clays Origins Life 1984, 14, 273-278
    • (1984) Origins Life , vol.14 , pp. 273-278
    • White, D.H.1    Kennedy, R.M.2    MacKlin, J.3
  • 18
    • 18444408087 scopus 로고    scopus 로고
    • Condensation reactions of amino acids under hydrothermal conditions with adiabatic expansion cooling
    • Gato, T.; Futamura, Y.; Yamaguchi, Y.; Yamamoto, K. Condensation reactions of amino acids under hydrothermal conditions with adiabatic expansion cooling J. Chem. Eng. Jpn. 2005, 38, 295-299
    • (2005) J. Chem. Eng. Jpn. , vol.38 , pp. 295-299
    • Gato, T.1    Futamura, Y.2    Yamaguchi, Y.3    Yamamoto, K.4
  • 19
    • 84887409672 scopus 로고    scopus 로고
    • http://www.origin-life.gr.jp/3304/3304269/3304269.pdf
  • 20
    • 0026649231 scopus 로고
    • Directed evolution of an RNA enzyme
    • Beaudry, A. A.; Joyce, G. F. Directed evolution of an RNA enzyme Science 1992, 257, 635-641
    • (1992) Science , vol.257 , pp. 635-641
    • Beaudry, A.A.1    Joyce, G.F.2
  • 21
    • 0028911845 scopus 로고
    • In vitro evolution of a self-alkylating ribozyme
    • Wilson, C.; Szostak, J. W. In vitro evolution of a self-alkylating ribozyme Nature 1995, 374, 777-782
    • (1995) Nature , vol.374 , pp. 777-782
    • Wilson, C.1    Szostak, J.W.2
  • 22
    • 0028533798 scopus 로고
    • A hypothesis: Reciprocal information transfer between oligoribonucleotides and oligopeptides in prebiotic molecular evolution
    • Zhang, S.; Egli, M. A hypothesis: Reciprocal information transfer between oligoribonucleotides and oligopeptides in prebiotic molecular evolution Origins Life Evol. Biospheres 1994, 24, 495-505
    • (1994) Origins Life Evol. Biospheres , vol.24 , pp. 495-505
    • Zhang, S.1    Egli, M.2
  • 23
    • 84989446769 scopus 로고
    • A proposed complementary pairing mode between single-stranded nucleic acids and β-stranded peptides: A possible pathway for generating complex biological molecules
    • Zhang, S.; Egli, M. A proposed complementary pairing mode between single-stranded nucleic acids and β-stranded peptides: A possible pathway for generating complex biological molecules Complexity 1995, 1, 49-56
    • (1995) Complexity , vol.1 , pp. 49-56
    • Zhang, S.1    Egli, M.2
  • 24
    • 0037117535 scopus 로고    scopus 로고
    • Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles
    • Vauthey, S.; Santoso, S.; Gong, H.; Watson, N.; Zhang, S. Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 5355-5360
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5355-5360
    • Vauthey, S.1    Santoso, S.2    Gong, H.3    Watson, N.4    Zhang, S.5
  • 25
    • 0001608018 scopus 로고    scopus 로고
    • Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles
    • Santoso, S.; Hwang, W.; Hartman, H.; Zhang, S. Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles Nano Lett. 2002, 2, 687-691
    • (2002) Nano Lett. , vol.2 , pp. 687-691
    • Santoso, S.1    Hwang, W.2    Hartman, H.3    Zhang, S.4
  • 26
    • 0038237370 scopus 로고    scopus 로고
    • Positively charged surfactant-like peptides self-assemble into nanostructures
    • von Maltzahn, G.; Vauthey, S.; Santoso, S.; Zhang, S. Positively charged surfactant-like peptides self-assemble into nanostructures Langmuir 2003, 19, 4332-4337
    • (2003) Langmuir , vol.19 , pp. 4332-4337
    • Von Maltzahn, G.1    Vauthey, S.2    Santoso, S.3    Zhang, S.4
  • 27
    • 33746849348 scopus 로고    scopus 로고
    • Self-assembling behavior of designer lipid-like peptides
    • Yang, S.; Zhang, S. Self-assembling behavior of designer lipid-like peptides Supramol. Chem. 2006, 18, 389-396
    • (2006) Supramol. Chem. , vol.18 , pp. 389-396
    • Yang, S.1    Zhang, S.2
  • 30
    • 79958780734 scopus 로고    scopus 로고
    • Ultrasmall natural peptides self-assemble to strong temperature-resistant helical fibers in scaffolds suitable for tissue engineering
    • Mishra, A.; Loo, Y.; Deng, R.; Chuah, Y. J.; Hee, H. T.; Ying, J. Y.; Hauser, C. A. E. Ultrasmall natural peptides self-assemble to strong temperature-resistant helical fibers in scaffolds suitable for tissue engineering NanoToday 2011, 6, 232-239
    • (2011) NanoToday , vol.6 , pp. 232-239
    • Mishra, A.1    Loo, Y.2    Deng, R.3    Chuah, Y.J.4    Hee, H.T.5    Ying, J.Y.6    Hauser, C.A.E.7
  • 31
    • 80053200885 scopus 로고    scopus 로고
    • Ultrasmall peptides self-assemble into diverse nanostructures: Morphological evaluation and potential implications
    • Lakshmanan, A.; Hauser, C. A. E. Ultrasmall peptides self-assemble into diverse nanostructures: Morphological evaluation and potential implications Int. J. Mol. Sci. 2011, 12, 5736-5746
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 5736-5746
    • Lakshmanan, A.1    Hauser, C.A.E.2
  • 33
    • 77955809474 scopus 로고    scopus 로고
    • Structure of single-wall peptide nanotubes: In situ flow aligning X-ray diffraction
    • Castelletto, V.; Nutt, D. R.; Hamley, I. W.; Bucak, S.; Cenker, C.; Olsson, U. Structure of single-wall peptide nanotubes: In situ flow aligning X-ray diffraction Chem. Commun. 2010, 46, 6270-6272
    • (2010) Chem. Commun. , vol.46 , pp. 6270-6272
    • Castelletto, V.1    Nutt, D.R.2    Hamley, I.W.3    Bucak, S.4    Cenker, C.5    Olsson, U.6
  • 34
    • 0030087980 scopus 로고    scopus 로고
    • Microinjection into giant vesicles and light microscopy investigation of enzyme-mediated vesicle transformations
    • Wick, R.; Angelova, M. I.; Walde, P.; Luisi, L. Microinjection into giant vesicles and light microscopy investigation of enzyme-mediated vesicle transformations Chem. Biol. 1996, 3, 105-111
    • (1996) Chem. Biol. , vol.3 , pp. 105-111
    • Wick, R.1    Angelova, M.I.2    Walde, P.3    Luisi, L.4
  • 35
    • 65249112128 scopus 로고    scopus 로고
    • Self-assembly of nano-donut structure from cone-shaped designer lipid-like peptide surfactant
    • Khoe, U.; Yang, Y.; Zhang, S. Self-assembly of nano-donut structure from cone-shaped designer lipid-like peptide surfactant Langmuir 2009, 25, 4111-4114
    • (2009) Langmuir , vol.25 , pp. 4111-4114
    • Khoe, U.1    Yang, Y.2    Zhang, S.3
  • 37
    • 84055193706 scopus 로고    scopus 로고
    • 6D adopt α-helical structures useful for membrane protein stabilization
    • 6D adopt α-helical structures useful for membrane protein stabilization Membranes 2011, 1, 314-326
    • (2011) Membranes , vol.1 , pp. 314-326
    • Zhuang, F.1    Ogleì̈cka, K.2    Hauser, C.A.E.3
  • 38
    • 56149098552 scopus 로고    scopus 로고
    • Tuning curvature and stability of monoolein bilayers by designer lipid-like peptide surfactants
    • Yaghmur, A.; Laggner, P.; Zhang, S.; Rappolt, M. Tuning curvature and stability of monoolein bilayers by designer lipid-like peptide surfactants PLoS ONE 2007, 2 e479
    • (2007) PLoS ONE , vol.2
    • Yaghmur, A.1    Laggner, P.2    Zhang, S.3    Rappolt, M.4
  • 39
    • 29344466943 scopus 로고    scopus 로고
    • Peptergent: Peptide detergents that improve stability and functionality of a membrane protein glycerol-3-phosphate dehydrogenase
    • Yeh, J. I.; Du, S.; Tordajada, A.; Paulo, J.; Zhang, S. Peptergent: Peptide detergents that improve stability and functionality of a membrane protein glycerol-3-phosphate dehydrogenase Biochemistry 2005, 44, 16912-16919
    • (2005) Biochemistry , vol.44 , pp. 16912-16919
    • Yeh, J.I.1    Du, S.2    Tordajada, A.3    Paulo, J.4    Zhang, S.5
  • 40
    • 22744432209 scopus 로고    scopus 로고
    • Self-assembling peptide detergents stabilize isolated photosystem i on a dry surface for an extended time
    • Kiley, P.; Zhao, X.; Vaughn, M.; Baldo, M.; Bruce, B. D.; Zhang, S. Self-assembling peptide detergents stabilize isolated photosystem I on a dry surface for an extended time PLoS Biol. 2005, 3, 1181-1186
    • (2005) PLoS Biol. , vol.3 , pp. 1181-1186
    • Kiley, P.1    Zhao, X.2    Vaughn, M.3    Baldo, M.4    Bruce, B.D.5    Zhang, S.6
  • 41
    • 61749086899 scopus 로고    scopus 로고
    • Designer lipid-like peptide surfactants stabilize functional photosystem i membrane complex in solution
    • Matsumoto, K.; Koutsopoulos, S.; Vaughn, M.; Bruce, B. D.; Zhang, S. Designer lipid-like peptide surfactants stabilize functional photosystem I membrane complex in solution J. Phys. Chem. B 2009, 113, 75-83
    • (2009) J. Phys. Chem. B , vol.113 , pp. 75-83
    • Matsumoto, K.1    Koutsopoulos, S.2    Vaughn, M.3    Bruce, B.D.4    Zhang, S.5
  • 42
    • 33845230242 scopus 로고    scopus 로고
    • Designer lipid-like peptides significantly stabilize G-protein coupled receptor bovine rhodopsin
    • Zhao, X.; Nagai, Y.; Revees, P.; Kiley, P.; Khorana, H. G.; Zhang, S. Designer lipid-like peptides significantly stabilize G-protein coupled receptor bovine rhodopsin Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 17707-17712
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 17707-17712
    • Zhao, X.1    Nagai, Y.2    Revees, P.3    Kiley, P.4    Khorana, H.G.5    Zhang, S.6
  • 43
    • 79959357733 scopus 로고    scopus 로고
    • Designer lipid-like peptide surfactants for cell-free production of diverse functional G-protein coupled receptors
    • Wang, X.; Corin, K.; Wienken, C. J.; Jerabek-Willemsen, M.; Duhr, S.; Braun, D.; Zhang, S. Designer lipid-like peptide surfactants for cell-free production of diverse functional G-protein coupled receptors Proc. Natl. Acad. Sci. U.S.A. 2011, 118, 9049-9054
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.118 , pp. 9049-9054
    • Wang, X.1    Corin, K.2    Wienken, C.J.3    Jerabek-Willemsen, M.4    Duhr, S.5    Braun, D.6    Zhang, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.