메뉴 건너뛰기




Volumn 18, Issue 6, 2012, Pages 405-412

Controlling morphology of peptide-based soft structures by covalent modifications

Author keywords

Diphenylalanine; Lectin; Mannose; Nanotubes; Self assembly; Vesicles

Indexed keywords

AMINO ACID; CARBOHYDRATE; CONCANAVALIN A; DIPEPTIDE; DIPHENYLALANINE DIPEPTIDE; LECTIN; MANNOSE; PEPTIDE NANOTUBE; THIOL; UNCLASSIFIED DRUG;

EID: 84861235124     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.2411     Document Type: Article
Times cited : (23)

References (56)
  • 1
    • 68149110370 scopus 로고    scopus 로고
    • Tuning the amphiphilicity of building blocks: controlled self-assembly and disassembly for functional supramolecular materials
    • Wang Y, Xu H, Zhang X. Tuning the amphiphilicity of building blocks: controlled self-assembly and disassembly for functional supramolecular materials. Adv. Mater. 2009; 21: 2849-2864.
    • (2009) Adv. Mater. , vol.21 , pp. 2849-2864
    • Wang, Y.1    Xu, H.2    Zhang, X.3
  • 3
    • 32044472480 scopus 로고    scopus 로고
    • Controlled self-assembly of amphiphilic oligopeptides into shape-specific nanoarchitectures
    • Koga T, Higuchi M, Kinoshita T, Higashi N. Controlled self-assembly of amphiphilic oligopeptides into shape-specific nanoarchitectures. Chem. Eur. J. 2006; 12: 1360-1367.
    • (2006) Chem. Eur. J. , vol.12 , pp. 1360-1367
    • Koga, T.1    Higuchi, M.2    Kinoshita, T.3    Higashi, N.4
  • 4
    • 28044456966 scopus 로고    scopus 로고
    • Controlled self-assembly of carbohydrate conjugate rod-coil amphiphiles for supramolecular multivalent ligands
    • Kim B-S, Hong D-J, Bae J, Lee M. Controlled self-assembly of carbohydrate conjugate rod-coil amphiphiles for supramolecular multivalent ligands. J. Am. Chem. Soc. 2005; 127: 16333-16337.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 16333-16337
    • Kim, B.-S.1    Hong, D.-J.2    Bae, J.3    Lee, M.4
  • 5
    • 17944363470 scopus 로고    scopus 로고
    • Supramolecular nanotube architectures based on amphiphilic molecules
    • Shimizu T, Masuda M, Minamikawa H. Supramolecular nanotube architectures based on amphiphilic molecules. Chem. Rev. 2005; 105: 1401-1443.
    • (2005) Chem. Rev. , vol.105 , pp. 1401-1443
    • Shimizu, T.1    Masuda, M.2    Minamikawa, H.3
  • 6
    • 70349333526 scopus 로고    scopus 로고
    • Self-assembly and transformation of hybrid nanoscale objects under equilibrium and non-equilibrium conditions
    • Mann S. Self-assembly and transformation of hybrid nanoscale objects under equilibrium and non-equilibrium conditions. Nature Mater. 2009; 8: 781-792.
    • (2009) Nature Mater. , vol.8 , pp. 781-792
    • Mann, S.1
  • 7
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • Hartgerink JD, Beniash E, Stupp SI. Self-assembly and mineralization of peptide-amphiphile nanofibers. Science 2001; 294: 1684-1688.
    • (2001) Science , vol.294 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 8
    • 80555144149 scopus 로고    scopus 로고
    • Self-assembly of short peptide amphiphiles: the cooperative effect of hydrophobic interaction and hydrogen bonding
    • Han S; Cao S, Wang Y, Wang J, Xia D, Xu H, Zhao X, Lu JR. Self-assembly of short peptide amphiphiles: the cooperative effect of hydrophobic interaction and hydrogen bonding. Eur. J. Chem. 2011; 17: 13095-13102.
    • (2011) Eur. J. Chem. , vol.17 , pp. 13095-13102
    • Han, S.1    Cao, S.2    Wang, Y.3    Wang, J.4    Xia, D.5    Xu, H.6    Zhao, X.7    Lu, J.R.8
  • 9
    • 77955795393 scopus 로고    scopus 로고
    • More than just bare scaffolds: towards multi-component and decorated fibrous biomaterials
    • Woolfson DN, Mahmoud ZN. More than just bare scaffolds: towards multi-component and decorated fibrous biomaterials. Chem. Soc. Rev. 2010; 39: 3464-3479.
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 3464-3479
    • Woolfson, D.N.1    Mahmoud, Z.N.2
  • 10
    • 61749104320 scopus 로고    scopus 로고
    • Morphology modulation of polymeric assemblies by guest drug molecules: TEM study and compatibility evaluation
    • Zhang J, Li S, Li X, Li X, Zhu K. Morphology modulation of polymeric assemblies by guest drug molecules: TEM study and compatibility evaluation. Polymer 2009; 50: 1778-1789.
    • (2009) Polymer , vol.50 , pp. 1778-1789
    • Zhang, J.1    Li, S.2    Li, X.3    Li, X.4    Zhu, K.5
  • 11
    • 48149087825 scopus 로고    scopus 로고
    • Vesicle-to-spherical, micelle-to-tubular nanostructure transition of monomethoxy-poly (ethylene glycol)-poly (trimethylene carbonate) diblock copolymer
    • Kim SY, Lee KE, Han SS, Jeong B. Vesicle-to-spherical, micelle-to-tubular nanostructure transition of monomethoxy-poly (ethylene glycol)-poly (trimethylene carbonate) diblock copolymer. J. Phys. Chem. B 2008; 112: 7420-7423.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 7420-7423
    • Kim, S.Y.1    Lee, K.E.2    Han, S.S.3    Jeong, B.4
  • 12
    • 34250841766 scopus 로고    scopus 로고
    • Transition of cationic dipeptide nanotubes into vesicles and oligonucleotide delivery
    • Yan X, He Q, Wang, K, Duan L, Cui Y, Li J. Transition of cationic dipeptide nanotubes into vesicles and oligonucleotide delivery. Angew. Chem. Int. Ed. 2007; 46: 2431-2434.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 2431-2434
    • Yan, X.1    He, Q.2    Wang, K.3    Duan, L.4    Cui, Y.5    Li, J.6
  • 13
    • 31944436026 scopus 로고    scopus 로고
    • Cyclodextrin-covered organic nanotubes derived from self-assembly of dendrons and their supramolecular transformation
    • Park C, Lee IH, Lee S, Song Y, Rhue M, Kim C. Cyclodextrin-covered organic nanotubes derived from self-assembly of dendrons and their supramolecular transformation. Proc. Natl. Acad. Sci. 2006; 103: 1199-1203.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 1199-1203
    • Park, C.1    Lee, I.H.2    Lee, S.3    Song, Y.4    Rhue, M.5    Kim, C.6
  • 14
    • 34547316314 scopus 로고    scopus 로고
    • Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization
    • Gazit E. Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization. Chem. Soc. Rev. 2007; 36: 1263-1269.
    • (2007) Chem. Soc. Rev. , vol.36 , pp. 1263-1269
    • Gazit, E.1
  • 15
    • 41149104937 scopus 로고    scopus 로고
    • Designing peptide based nanomaterials
    • Ulijn RV, Smith AM. Designing peptide based nanomaterials. Chem. Soc. Rev. 2008; 37: 664-675.
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 664-675
    • Ulijn, R.V.1    Smith, A.M.2
  • 16
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • Zhang S. Fabrication of novel biomaterials through molecular self-assembly. Nat. Biotechnol. 2003; 21: 1171-1178.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 17
    • 63049121072 scopus 로고    scopus 로고
    • Recent advances in functional supramolecular nanostructures assembled from bioactive building blocks
    • Lim YB, Moon KS, Lee M. Recent advances in functional supramolecular nanostructures assembled from bioactive building blocks. Chem. Soc. Rev. 2009; 38: 925-934.
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 925-934
    • Lim, Y.B.1    Moon, K.S.2    Lee, M.3
  • 18
    • 79961148136 scopus 로고    scopus 로고
    • Toroidal β-barrels from self-assembling β-sheet peptides
    • Lim Y-B, Lee M. Toroidal β-barrels from self-assembling β-sheet peptides. J. Mater. Chem. 2011; 21: 11680-11685.
    • (2011) J. Mater. Chem. , vol.21 , pp. 11680-11685
    • Lim, Y.-B.1    Lee, M.2
  • 19
    • 36048941372 scopus 로고    scopus 로고
    • Peptide fibrillization
    • Hamley IW. Peptide fibrillization. Angew. Chem. Int. Ed. 2007; 46: 8128-8147.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 8128-8147
    • Hamley, I.W.1
  • 20
    • 44249120377 scopus 로고    scopus 로고
    • Nanovesicles based on self-assembly of conformationally constrained aromatic residue containing amphiphilic dipeptides
    • Mishra A, Panda JJ, Basu A, Chauhan VS. Nanovesicles based on self-assembly of conformationally constrained aromatic residue containing amphiphilic dipeptides. Langmuir 2008; 24: 4571-4576.
    • (2008) Langmuir , vol.24 , pp. 4571-4576
    • Mishra, A.1    Panda, J.J.2    Basu, A.3    Chauhan, V.S.4
  • 21
    • 79955028241 scopus 로고    scopus 로고
    • Tubulation on peptide vesicles by phase-separation of a binary mixture of amphiphilic right-handed and left-handed helical peptides
    • Ueda M, Makino A, Imai T, Sugiyama J, Kimura S. Tubulation on peptide vesicles by phase-separation of a binary mixture of amphiphilic right-handed and left-handed helical peptides. Soft Matter 2011; 7: 4143-4146.
    • (2011) Soft Matter , vol.7 , pp. 4143-4146
    • Ueda, M.1    Makino, A.2    Imai, T.3    Sugiyama, J.4    Kimura, S.5
  • 23
    • 65249112128 scopus 로고    scopus 로고
    • Self-assembly of nanodonut structure from a cone-shaped designer lipid-like peptide surfactant
    • Khoe U, Yang Y, Zhang S. Self-assembly of nanodonut structure from a 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
  • 24
    • 0035802949 scopus 로고    scopus 로고
    • Nanotube formation by hydrophobic dipeptides
    • Görbitz CH. Nanotube formation by hydrophobic dipeptides. Chem. Eur. J. 2001; 7: 5153-5159.
    • (2001) Chem. Eur. J. , vol.7 , pp. 5153-5159
    • Görbitz, C.H.1
  • 25
    • 1642538387 scopus 로고    scopus 로고
    • Nanotubes from hydrophobic dipeptides: pore size regulation through side chain substitution
    • Görbitz CH. Nanotubes from hydrophobic dipeptides: pore size regulation through side chain substitution. New J. Chem. 2003; 27: 1789-1793.
    • (2003) New J. Chem. , vol.27 , pp. 1789-1793
    • Görbitz, C.H.1
  • 26
    • 25144496453 scopus 로고    scopus 로고
    • Microporous organic crystals: an unusual case for L-leucyl-L-serine
    • Görbitz CH, Nilsen M, Szeto K, Tangen LW. Microporous organic crystals: an unusual case for L-leucyl-L-serine. Chem. Commun. 2005; 4288-4290.
    • (2005) Chem. Commun. , pp. 4288-4290
    • Görbitz, C.H.1    Nilsen, M.2    Szeto, K.3    Tangen, L.W.4
  • 27
    • 23144442139 scopus 로고    scopus 로고
    • Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures
    • Kol N, Adler-Abramovich L, Barlam D, Shneck RZ, Gazit E, Rousso I. Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures. Nano Lett. 2005; 5: 1343-1346.
    • (2005) Nano Lett. , vol.5 , pp. 1343-1346
    • Kol, N.1    Adler-Abramovich, L.2    Barlam, D.3    Shneck, R.Z.4    Gazit, E.5    Rousso, I.6
  • 28
    • 34547217464 scopus 로고    scopus 로고
    • Using the bending beam model to estimate the elasticity of diphenylalanine nanotubes
    • Niu L, Chen X, Allen S, Tendler SJB. Using the bending beam model to estimate the elasticity of diphenylalanine nanotubes. Langmuir 2007; 23: 7443-7446.
    • (2007) Langmuir , vol.23 , pp. 7443-7446
    • Niu, L.1    Chen, X.2    Allen, S.3    Tendler, S.J.B.4
  • 29
    • 34247243833 scopus 로고    scopus 로고
    • Controlled patterning of aligned self-assembled peptide nanotubes
    • Reches M, Gazit E. Controlled patterning of aligned self-assembled peptide nanotubes. Nat. Nanotechnol. 2006; 1: 195-200.
    • (2006) Nat. Nanotechnol. , vol.1 , pp. 195-200
    • Reches, M.1    Gazit, E.2
  • 30
    • 2342595738 scopus 로고    scopus 로고
    • Formation of closed-cage nanostructures by self-assembly of aromatic dipeptides
    • Reches M, Gazit E. Formation of closed-cage nanostructures by self-assembly of aromatic dipeptides. Nano Lett. 2004; 4: 581-585.
    • (2004) Nano Lett. , vol.4 , pp. 581-585
    • Reches, M.1    Gazit, E.2
  • 31
    • 65449164627 scopus 로고    scopus 로고
    • Bending of peptide nanotubes by focused electron and ion beams
    • Gour N, Verma S. Bending of peptide nanotubes by focused electron and ion beams. Soft Matter. 2009; 5: 1789-1791.
    • (2009) Soft Matter. , vol.5 , pp. 1789-1791
    • Gour, N.1    Verma, S.2
  • 32
    • 53849102590 scopus 로고    scopus 로고
    • Templated growth of hybrid structures at the peptide-peptide interface
    • Ghosh S, Verma S. Templated growth of hybrid structures at the peptide-peptide interface. Chem. Eur. J. 2008; 14: 1415-1419.
    • (2008) Chem. Eur. J. , vol.14 , pp. 1415-1419
    • Ghosh, S.1    Verma, S.2
  • 33
    • 34247626389 scopus 로고    scopus 로고
    • Bioinspired design of nano-cages by self-assembling triskelion peptide elements
    • Ghosh S, Reches M, Gazit E, Verma S. Bioinspired design of nano-cages by self-assembling triskelion peptide elements. Angew. Chem. Int. Ed. 2007; 119: 2002-2004.
    • (2007) Angew. Chem. Int. Ed. , vol.119 , pp. 2002-2004
    • Ghosh, S.1    Reches, M.2    Gazit, E.3    Verma, S.4
  • 34
    • 42249087956 scopus 로고    scopus 로고
    • Ditryptophan conjugation triggers conversion of biotin fibers into soft spherical structures
    • Joshi KB, Verma S. Ditryptophan conjugation triggers conversion of biotin fibers into soft spherical structures. Angew. Chem. Int. Ed. 2008; 47: 2860-2863.
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 2860-2863
    • Joshi, K.B.1    Verma, S.2
  • 35
    • 84873569695 scopus 로고    scopus 로고
    • See Supporting Information.
    • See Supporting Information.
  • 36
    • 57749208165 scopus 로고    scopus 로고
    • Mannosylated self-assembled structures for molecular confinement and gene delivery applications
    • Gour N, Purohit CS, Verma S, Puri R, Ganesh S. Mannosylated self-assembled structures for molecular confinement and gene delivery applications. Biochem. Biophys. Res. Commun. 2009; 378: 503-506.
    • (2009) Biochem. Biophys. Res. Commun. , vol.378 , pp. 503-506
    • Gour, N.1    Purohit, C.S.2    Verma, S.3    Puri, R.4    Ganesh, S.5
  • 38
    • 0342669137 scopus 로고
    • The nature of the co-solvent effects on the aqueous solubilities of hydrocarbons
    • Janado M, Yano Y. The nature of the co-solvent effects on the aqueous solubilities of hydrocarbons. Bull. Chem. Soc. Jpn. 1985; 58: 1913-1917.
    • (1985) Bull. Chem. Soc. Jpn. , vol.58 , pp. 1913-1917
    • Janado, M.1    Yano, Y.2
  • 39
    • 0027314952 scopus 로고
    • X-ray crystal structure of a pea lectin-trimannoside complex at 2.6 Å resolution
    • Rini JM, Hardman KD, Einspahr H, Suddath FL, Carver JP. X-ray crystal structure of a pea lectin-trimannoside complex at 2.6 Å resolution. J. Biol. Chem. 1993; 268: 10126-10132.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10126-10132
    • Rini, J.M.1    Hardman, K.D.2    Einspahr, H.3    Suddath, F.L.4    Carver, J.P.5
  • 40
    • 34247481360 scopus 로고    scopus 로고
    • Carbohydrate-coated supramolecular structures: transformation of nanofibers into spherical micelles triggered by guest encapsulation
    • Ryu J, Lee E, Lim Y, Lee M. Carbohydrate-coated supramolecular structures: transformation of nanofibers into spherical micelles triggered by guest encapsulation. J. Am. Chem. Soc. 2007; 129: 4808-4814.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4808-4814
    • Ryu, J.1    Lee, E.2    Lim, Y.3    Lee, M.4
  • 41
    • 2542532174 scopus 로고    scopus 로고
    • A quantum dot conjugated sugar ball and its cellular uptake. On the size effects of endocytosis in the subviral region
    • Osaki F, Kanamori T, Sando S, Sera T, Aoyama Y. A quantum dot conjugated sugar ball and its cellular uptake. On the size effects of endocytosis in the subviral region. J. Am. Chem. Soc. 2004; 126: 6520-6521.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 6520-6521
    • Osaki, F.1    Kanamori, T.2    Sando, S.3    Sera, T.4    Aoyama, Y.5
  • 42
    • 0037011939 scopus 로고    scopus 로고
    • Inter-receptor communication through arrays of bacterial chemoreceptors
    • Gestwicki JE, Kiessling LL. Inter-receptor communication through arrays of bacterial chemoreceptors. Nature 2002; 415: 81-84.
    • (2002) Nature , vol.415 , pp. 81-84
    • Gestwicki, J.E.1    Kiessling, L.L.2
  • 43
    • 0036462602 scopus 로고    scopus 로고
    • The cluster glycoside effect
    • Lundquist JJ, Toone EJ. The cluster glycoside effect. Chem. Rev. 2002; 102: 555-578.
    • (2002) Chem. Rev. , vol.102 , pp. 555-578
    • Lundquist, J.J.1    Toone, E.J.2
  • 44
    • 0038648179 scopus 로고    scopus 로고
    • Synthesis of an amphiphilic tetraantennary mannosyl conjugate and incorporation into liposome carriers
    • Espuelas S, Haller P, Schuber F, Frisch B. Synthesis of an amphiphilic tetraantennary mannosyl conjugate and incorporation into liposome carriers. Bioorg. Med. Chem. Lett. 2003; 13: 2557-2560.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 2557-2560
    • Espuelas, S.1    Haller, P.2    Schuber, F.3    Frisch, B.4
  • 45
    • 33746685001 scopus 로고    scopus 로고
    • Carbohydrate-functionalized dendrimers to investigate the predictable tunability of multivalent interactions
    • Wolfenden M, Cloninger M. Carbohydrate-functionalized dendrimers to investigate the predictable tunability of multivalent interactions. Bioconj. Chem. 2006; 17: 958-966.
    • (2006) Bioconj. Chem. , vol.17 , pp. 958-966
    • Wolfenden, M.1    Cloninger, M.2
  • 46
    • 79959464070 scopus 로고    scopus 로고
    • Glycan microarrays for decoding the glycome
    • Rillahan CD, Paulson JC. Glycan microarrays for decoding the glycome. Annu. Rev. Biochem. 2011; 80: 797-823.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 797-823
    • Rillahan, C.D.1    Paulson, J.C.2
  • 47
    • 77956154558 scopus 로고    scopus 로고
    • Use of glycan microarrays to explore specificity of glycan-binding proteins
    • Smith DF, Song X, Cummings RD. Use of glycan microarrays to explore specificity of glycan-binding proteins. Methods Enzymol. 2010; 480: 417-444.
    • (2010) Methods Enzymol. , vol.480 , pp. 417-444
    • Smith, D.F.1    Song, X.2    Cummings, R.D.3
  • 48
    • 70450175085 scopus 로고    scopus 로고
    • Multivalent ligand presentation as a central concept to study intricate carbohydrate-protein interactions
    • Jayaraman N. Multivalent ligand presentation as a central concept to study intricate carbohydrate-protein interactions. Chem. Soc. Rev. 2009; 38: 3463-3483.
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 3463-3483
    • Jayaraman, N.1
  • 49
    • 34247116961 scopus 로고    scopus 로고
    • 24 molecular spheres that form aggregates by multi-interaction with proteins
    • 24 molecular spheres that form aggregates by multi-interaction with proteins. J. Am. Chem. Soc. 2007; 129: 3816-3817.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 3816-3817
    • Kamiya, N.1    Tominaga, M.2    Sato, S.3    Fujita, M.4
  • 50
    • 0032573844 scopus 로고    scopus 로고
    • Ternary complexation involving protein. Molecular transport to saccharide-binding proteins using macrocyclic saccharide cluster as specific transporter
    • Fujimoto T Shimizu C, Hayashida O, Aoyama Y. Ternary complexation involving protein. Molecular transport to saccharide-binding proteins using macrocyclic saccharide cluster as specific transporter. J. Am. Chem. Soc. 1998; 120: 601-602.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 601-602
    • Fujimoto, T.1    Shimizu, C.2    Hayashida, O.3    Aoyama, Y.4
  • 51
    • 0030971899 scopus 로고    scopus 로고
    • Synthesis of new R-thiosialodendrimers and their binding properties to the sialic acid specific lectin from Limax flavus
    • Zanini D, Roy R. Synthesis of new R-thiosialodendrimers and their binding properties to the sialic acid specific lectin from Limax flavus. J. Am. Chem. Soc. 1997; 119: 2088-2095.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2088-2095
    • Zanini, D.1    Roy, R.2
  • 52
    • 0001002781 scopus 로고
    • Globular carbohydrate macromolecule "Sugar Balls". 1. Synthesis of novel sugar-persubstituted poly (amido amine) dendrimers
    • Aoi K, Itoh K, Okada M. Globular carbohydrate macromolecule "Sugar Balls". 1. Synthesis of novel sugar-persubstituted poly (amido amine) dendrimers. Macromolecules 1995; 28: 5391-5393.
    • (1995) Macromolecules , vol.28 , pp. 5391-5393
    • Aoi, K.1    Itoh, K.2    Okada, M.3
  • 53
    • 45449106145 scopus 로고    scopus 로고
    • Synthesis and AFM studies of lectin-carbohydrate self-assemblies
    • Gour N, Verma S. Synthesis and AFM studies of lectin-carbohydrate self-assemblies. Tetrahedron 2008; 64: 7331-7337.
    • (2008) Tetrahedron , vol.64 , pp. 7331-7337
    • Gour, N.1    Verma, S.2
  • 54
    • 52649096966 scopus 로고    scopus 로고
    • Glycoarrays-tools for determining protein-carbohydrate interactions and glycoenzyme specificity
    • Laurent N, Voglmeir J, Flitsch SL. Glycoarrays-tools for determining protein-carbohydrate interactions and glycoenzyme specificity. Chem. Commun. 2008; 4400-4412.
    • (2008) Chem. Commun. , pp. 4400-4412
    • Laurent, N.1    Voglmeir, J.2    Flitsch, S.L.3
  • 55
    • 52449127409 scopus 로고    scopus 로고
    • Carbohydrate microarrays as powerful tools in studies of carbohydrate-mediated biological processes
    • Park S, Lee M-R, Shin I. Carbohydrate microarrays as powerful tools in studies of carbohydrate-mediated biological processes. Chem. Commun. 2008; 4389-4399.
    • (2008) Chem. Commun. , pp. 4389-4399
    • Park, S.1    Lee, M.-R.2    Shin, I.3
  • 56
    • 18044371446 scopus 로고    scopus 로고
    • Carbohydrate-coated nanocapsules from amphiphilic rod-coil molecule: binding to bacterial type 1 pili
    • Kim BS, Yang WY, Ryu JH, Yoo YS, Lee M. Carbohydrate-coated nanocapsules from amphiphilic rod-coil molecule: binding to bacterial type 1 pili. Chem. Commun. 2005; 2035-2037.
    • (2005) Chem. Commun. , pp. 2035-2037
    • Kim, B.S.1    Yang, W.Y.2    Ryu, J.H.3    Yoo, Y.S.4    Lee, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.