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Volumn 26, Issue 9, 2015, Pages 1972-1980

Supramolecular surface immobilization of knottin derivatives for dynamic display of high affinity binders

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; ESCHERICHIA COLI; SELF ASSEMBLED MONOLAYERS;

EID: 84941686603     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/acs.bioconjchem.5b00419     Document Type: Article
Times cited : (17)

References (50)
  • 1
    • 43549102692 scopus 로고    scopus 로고
    • Alternative binding proteins: Biological activity and therapeutic potential of cystine-knot miniproteins
    • Kolmar, H. (2008) Alternative binding proteins: Biological activity and therapeutic potential of cystine-knot miniproteins FEBS J. 275, 2684-2690 10.1111/j.1742-4658.2008.06440.x
    • (2008) FEBS J. , vol.275 , pp. 2684-2690
    • Kolmar, H.1
  • 2
    • 71049186869 scopus 로고    scopus 로고
    • Biosynthesis and biological screening of a genetically encoded library based on the cyclotide MCoTI-I
    • Austin, J., Wang, W., Puttamadappa, S., Shekhtman, A., and Camarero, J. A. (2009) Biosynthesis and biological screening of a genetically encoded library based on the cyclotide MCoTI-I ChemBioChem 10, 2663-2670 10.1002/cbic.200900534
    • (2009) ChemBioChem , vol.10 , pp. 2663-2670
    • Austin, J.1    Wang, W.2    Puttamadappa, S.3    Shekhtman, A.4    Camarero, J.A.5
  • 3
    • 0345864014 scopus 로고    scopus 로고
    • The KNOTTIN website and database: A new information system dedicated to the knottin scaffold
    • Gelly, J., Gracy, J., Kaas, Q., Le-Nguyen, D., Heitz, A., and Chiche, L. (2004) The KNOTTIN website and database: a new information system dedicated to the knottin scaffold Nucleic Acids Res. 32, 156D-159D 10.1093/nar/gkh015
    • (2004) Nucleic Acids Res. , vol.32 , pp. 156D-159D
    • Gelly, J.1    Gracy, J.2    Kaas, Q.3    Le-Nguyen, D.4    Heitz, A.5    Chiche, L.6
  • 5
    • 84861322262 scopus 로고    scopus 로고
    • Cyclotides, a novel ultrastable polypeptide scaffold for drug discovery
    • Gould, A., Ji, Y., Aboye, T. L., and Camarero, J. A. (2011) Cyclotides, a novel ultrastable polypeptide scaffold for drug discovery Curr. Pharm. Des. 17, 4294-4307 10.2174/138161211798999438
    • (2011) Curr. Pharm. Des. , vol.17 , pp. 4294-4307
    • Gould, A.1    Ji, Y.2    Aboye, T.L.3    Camarero, J.A.4
  • 6
    • 84865689360 scopus 로고    scopus 로고
    • Knottins: Disulfide-bonded therapeutic and diagnostic peptides
    • Moore, S. J., Leung, C. L., and Cochran, J. R. (2012) Knottins: disulfide-bonded therapeutic and diagnostic peptides Drug Discovery Today: Technol. 9, e3-e11 10.1016/j.ddtec.2011.07.003
    • (2012) Drug Discovery Today: Technol. , vol.9 , pp. e3-e11
    • Moore, S.J.1    Leung, C.L.2    Cochran, J.R.3
  • 7
    • 84880545300 scopus 로고    scopus 로고
    • Replacing antibodies: Engineering new binding proteins
    • Banta, S., Dooley, K., and Shur, O. (2013) Replacing antibodies: engineering new binding proteins Annu. Rev. Biomed. Eng. 15, 93-113 10.1146/annurev-bioeng-071812-152412
    • (2013) Annu. Rev. Biomed. Eng. , vol.15 , pp. 93-113
    • Banta, S.1    Dooley, K.2    Shur, O.3
  • 8
    • 29344448254 scopus 로고    scopus 로고
    • A new generation of protein display scaffolds for molecular recognition
    • Hosse, R. J., Rothe, A., and Power, B. E. (2006) A new generation of protein display scaffolds for molecular recognition Protein Sci. 15, 14-27 10.1110/ps.051817606
    • (2006) Protein Sci. , vol.15 , pp. 14-27
    • Hosse, R.J.1    Rothe, A.2    Power, B.E.3
  • 9
    • 80052005787 scopus 로고    scopus 로고
    • Protease-resistant peptide ligands from a knottin scaffold library
    • Getz, J. A., Rice, J. J., and Daugherty, P. S. (2011) Protease-resistant peptide ligands from a knottin scaffold library ACS Chem. Biol. 6, 837-844 10.1021/cb200039s
    • (2011) ACS Chem. Biol. , vol.6 , pp. 837-844
    • Getz, J.A.1    Rice, J.J.2    Daugherty, P.S.3
  • 10
    • 84879005229 scopus 로고    scopus 로고
    • Design of a cyclotide antagonist of neuropilin-1 and -2 that potently inhibits endothelial cell migration
    • Getz, J. A., Cheneval, O., Craik, D. J., and Daugherty, P. S. (2013) Design of a cyclotide antagonist of neuropilin-1 and -2 that potently inhibits endothelial cell migration ACS Chem. Biol. 8, 1147-1154 10.1021/cb4000585
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1147-1154
    • Getz, J.A.1    Cheneval, O.2    Craik, D.J.3    Daugherty, P.S.4
  • 11
    • 0033543156 scopus 로고    scopus 로고
    • Min-21 and Min-23, the smallest peptides that fold like a cystine-stabilized β-sheet motif: Design, solution structure, and thermal stability
    • Heitz, A., Le-Nguyen, D., and Chiche, L. (1999) Min-21 and Min-23, the smallest peptides that fold like a cystine-stabilized β-sheet motif: design, solution structure, and thermal stability Biochemistry 38, 10615-10625 10.1021/bi990821k
    • (1999) Biochemistry , vol.38 , pp. 10615-10625
    • Heitz, A.1    Le-Nguyen, D.2    Chiche, L.3
  • 12
    • 18544368988 scopus 로고    scopus 로고
    • New binding specificities derived from Min-23, a small cystine-stabilized peptidic scaffold
    • Souriau, C., Chiche, L., Irving, R., and Hudson, P. (2005) New binding specificities derived from Min-23, a small cystine-stabilized peptidic scaffold Biochemistry 44, 7143-7155 10.1021/bi0481592
    • (2005) Biochemistry , vol.44 , pp. 7143-7155
    • Souriau, C.1    Chiche, L.2    Irving, R.3    Hudson, P.4
  • 14
    • 77950880605 scopus 로고    scopus 로고
    • Engineering anti-vascular endothelial growth factor single chain disulfide-stabilized antibody variable fragments (sc-dsFv) with phage-displayed sc-dsFv libraries
    • Huang, Y.-J., Chen, I.-C., Yu, C.-M., Lee, Y.-C., Hsu, H.-J., Ching, A. T. C., Chang, H.-J., and Yang, A.-S. (2010) Engineering anti-vascular endothelial growth factor single chain disulfide-stabilized antibody variable fragments (sc-dsFv) with phage-displayed sc-dsFv libraries J. Biol. Chem. 285, 7880-7891 10.1074/jbc.M109.061457
    • (2010) J. Biol. Chem. , vol.285 , pp. 7880-7891
    • Huang, Y.-J.1    Chen, I.-C.2    Yu, C.-M.3    Lee, Y.-C.4    Hsu, H.-J.5    Ching, A.T.C.6    Chang, H.-J.7    Yang, A.-S.8
  • 15
    • 58149336794 scopus 로고    scopus 로고
    • Engineered cystine-knot peptides that Bind αvβ3 integrin with antibody-like affinities
    • Silverman, A. P., Levin, A. M., Lahti, J. L., and Cochran, J. R. (2009) Engineered cystine-knot peptides that Bind αvβ3 integrin with antibody-like affinities J. Mol. Biol. 385, 1064-1075 10.1016/j.jmb.2008.11.004
    • (2009) J. Mol. Biol. , vol.385 , pp. 1064-1075
    • Silverman, A.P.1    Levin, A.M.2    Lahti, J.L.3    Cochran, J.R.4
  • 16
    • 70349462873 scopus 로고    scopus 로고
    • Engineered cystine knot peptides that bind αvβ3, αvβ5, and α5β1 integrins with low-nanomolar affinity
    • Kimura, R. H., Levin, A. M., Cochran, F. V., and Cochran, J. R. (2009) Engineered cystine knot peptides that bind αvβ3, αvβ5, and α5β1 integrins with low-nanomolar affinity Proteins: Struct., Funct., Genet. 77, 359-369 10.1002/prot.22441
    • (2009) Proteins: Struct., Funct., Genet. , vol.77 , pp. 359-369
    • Kimura, R.H.1    Levin, A.M.2    Cochran, F.V.3    Cochran, J.R.4
  • 17
    • 84921030306 scopus 로고    scopus 로고
    • A chemically cross-linked knottin dimer binds integrins with picomolar affinity and inhibits tumor cell migration and proliferation
    • Kim, J. W., Cochran, F. V., and Cochran, J. R. (2015) A chemically cross-linked knottin dimer binds integrins with picomolar affinity and inhibits tumor cell migration and proliferation J. Am. Chem. Soc. 137, 6-9 10.1021/ja508416e
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 6-9
    • Kim, J.W.1    Cochran, F.V.2    Cochran, J.R.3
  • 18
    • 84874819064 scopus 로고    scopus 로고
    • Expression of fluorescent cyclotides using protein trans-splicing for easy monitoring of cyclotide-protein interactions
    • Jagadish, K., Borra, R., Lacey, V., Majumder, S., Shekhtman, A., Wang, L., and Camarero, J. A. (2013) Expression of fluorescent cyclotides using protein trans-splicing for easy monitoring of cyclotide-protein interactions Angew. Chem., Int. Ed. 52, 3126-3131 10.1002/anie.201209219
    • (2013) Angew. Chem., Int. Ed. , vol.52 , pp. 3126-3131
    • Jagadish, K.1    Borra, R.2    Lacey, V.3    Majumder, S.4    Shekhtman, A.5    Wang, L.6    Camarero, J.A.7
  • 19
    • 65549092007 scopus 로고    scopus 로고
    • Engineered knottin peptides: A new class o f agents for imaging integrin expression in living subjects
    • Kimura, R. H., Cheng, Z., Gambhir, S. S., and Cochran, J. R. (2009) Engineered knottin peptides: a new class o f agents for imaging integrin expression in living subjects Cancer Res. 69, 2435-2442 10.1158/0008-5472.CAN-08-2495
    • (2009) Cancer Res. , vol.69 , pp. 2435-2442
    • Kimura, R.H.1    Cheng, Z.2    Gambhir, S.S.3    Cochran, J.R.4
  • 20
  • 22
    • 84927127151 scopus 로고    scopus 로고
    • Self-assembled monolayers and nanocomposite hydrogels of functional nanomaterials for tissue engineering applications
    • Kehr, N. S., Atay, S., and Ergün, B. (2015) Self-assembled monolayers and nanocomposite hydrogels of functional nanomaterials for tissue engineering applications Macromol. Biosci. 15, 445-463 10.1002/mabi.201400363
    • (2015) Macromol. Biosci. , vol.15 , pp. 445-463
    • Kehr, N.S.1    Atay, S.2    Ergün, B.3
  • 23
    • 84923934657 scopus 로고    scopus 로고
    • Engineering and functionalization of biomaterials via surface modification
    • Wu, G., Li, P., Feng, H., Zhang, X., and Chu, P. K. (2015) Engineering and functionalization of biomaterials via surface modification J. Mater. Chem. B 3, 2024-2042 10.1039/C4TB01934B
    • (2015) J. Mater. Chem. B , vol.3 , pp. 2024-2042
    • Wu, G.1    Li, P.2    Feng, H.3    Zhang, X.4    Chu, P.K.5
  • 24
    • 70349900170 scopus 로고    scopus 로고
    • Molecular and supramolecular networks on surfaces: From two-dimensional crystal engineering to reactivity
    • Elemans, J. A. A. W., Lei, S., and De Feyter, S. (2009) Molecular and supramolecular networks on surfaces: from two-dimensional crystal engineering to reactivity Angew. Chem., Int. Ed. 48, 7298-7332 10.1002/anie.200806339
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 7298-7332
    • Elemans, J.A.A.W.1    Lei, S.2    De Feyter, S.3
  • 25
    • 77954899257 scopus 로고    scopus 로고
    • Combining supramolecular chemistry with biology
    • Uhlenheuer, D. A., Petkau, K., and Brunsveld, L. (2010) Combining supramolecular chemistry with biology Chem. Soc. Rev. 39, 2817-2826 10.1039/b820283b
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 2817-2826
    • Uhlenheuer, D.A.1    Petkau, K.2    Brunsveld, L.3
  • 27
    • 84922553980 scopus 로고    scopus 로고
    • Biomedical applications of supramolecular systems based on host-guest interactions
    • Ma, X. and Zhao, Y. (2014) Biomedical applications of supramolecular systems based on host-guest interactions Chem. Rev. 115, 7794 10.1021/cr500392w
    • (2014) Chem. Rev. , vol.115 , pp. 7794
    • Ma, X.1    Zhao, Y.2
  • 28
    • 84896397684 scopus 로고    scopus 로고
    • Supramolecular materials for regenerative medicine
    • Boekhoven, J. and Stupp, S. I. (2014) Supramolecular materials for regenerative medicine Adv. Mater. 26, 1642-1659 10.1002/adma.201304606
    • (2014) Adv. Mater. , vol.26 , pp. 1642-1659
    • Boekhoven, J.1    Stupp, S.I.2
  • 31
    • 84910071843 scopus 로고    scopus 로고
    • Optical control over bioactive ligands at supramolecular surfaces
    • Voskuhl, J., Sankaran, S., and Jonkheijm, P. (2014) Optical control over bioactive ligands at supramolecular surfaces Chem. Commun. 50, 15144-15147 10.1039/C4CC03184A
    • (2014) Chem. Commun. , vol.50 , pp. 15144-15147
    • Voskuhl, J.1    Sankaran, S.2    Jonkheijm, P.3
  • 32
    • 84928967026 scopus 로고    scopus 로고
    • Incorporating bacteria as a living component in supramolecular self-assembled monolayers through dynamic nanoscale interactions
    • Sankaran, S., Kiren, M. C., and Jonkheijm, P. (2015) Incorporating bacteria as a living component in supramolecular self-assembled monolayers through dynamic nanoscale interactions ACS Nano 9, 3579-3586 10.1021/acsnano.5b00694
    • (2015) ACS Nano , vol.9 , pp. 3579-3586
    • Sankaran, S.1    Kiren, M.C.2    Jonkheijm, P.3
  • 33
    • 84859124323 scopus 로고    scopus 로고
    • Cucurbituril chemistry: A tale of supramolecular success
    • Masson, E., Ling, X., Joseph, R., Kyeremeh-Mensah, L., and Lu, X. (2012) Cucurbituril chemistry: a tale of supramolecular success RSC Adv. 2, 1213-1247 10.1039/C1RA00768H
    • (2012) RSC Adv. , vol.2 , pp. 1213-1247
    • Masson, E.1    Ling, X.2    Joseph, R.3    Kyeremeh-Mensah, L.4    Lu, X.5
  • 34
    • 0041472445 scopus 로고    scopus 로고
    • Cucurbituril homologues and derivatives: New opportunities in supramolecular chemistry
    • Lee, J. W., Samal, S., Selvapalam, N., Kim, H.-J., and Kim, K. (2003) Cucurbituril homologues and derivatives: new opportunities in supramolecular chemistry Acc. Chem. Res. 36, 621-630 10.1021/ar020254k
    • (2003) Acc. Chem. Res. , vol.36 , pp. 621-630
    • Lee, J.W.1    Samal, S.2    Selvapalam, N.3    Kim, H.-J.4    Kim, K.5
  • 37
    • 84896464547 scopus 로고    scopus 로고
    • Dual stimuli-responsive self-assembled supramolecular nanoparticles
    • Stoffelen, C., Voskuhl, J., Jonkheijm, P., and Huskens, J. (2014) Dual stimuli-responsive self-assembled supramolecular nanoparticles Angew. Chem., Int. Ed. 53, 3400-3404 10.1002/anie.201310829
    • (2014) Angew. Chem., Int. Ed. , vol.53 , pp. 3400-3404
    • Stoffelen, C.1    Voskuhl, J.2    Jonkheijm, P.3    Huskens, J.4
  • 38
    • 84921334737 scopus 로고    scopus 로고
    • Facile method for preparing surface-mounted cucurbit[8]uril-based rotaxanes
    • Hu, C., Lan, Y., Tian, F., West, K. R., and Scherman, O. A. (2014) Facile method for preparing surface-mounted cucurbit[8]uril-based rotaxanes Langmuir 30, 10926-10932 10.1021/la5026125
    • (2014) Langmuir , vol.30 , pp. 10926-10932
    • Hu, C.1    Lan, Y.2    Tian, F.3    West, K.R.4    Scherman, O.A.5
  • 41
    • 26844563376 scopus 로고    scopus 로고
    • Charge-mediated recognition of N-terminal tryptophan in aqueous solution by a synthetic host
    • Bush, M. E., Bouley, N. D., and Urbach, A. R. (2005) Charge-mediated recognition of N-terminal tryptophan in aqueous solution by a synthetic host J. Am. Chem. Soc. 127, 14511-14517 10.1021/ja0548440
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 14511-14517
    • Bush, M.E.1    Bouley, N.D.2    Urbach, A.R.3
  • 42
    • 10644277283 scopus 로고    scopus 로고
    • A fusion protein system for the recombinant production of short disulfide bond rich cystine knot peptides using barnase as a purification handle
    • Schmoldt, H.-U., Wentzel, A., Becker, S., and Kolmar, H. (2005) A fusion protein system for the recombinant production of short disulfide bond rich cystine knot peptides using barnase as a purification handle Protein Expression Purif. 39, 82-89 10.1016/j.pep.2004.09.016
    • (2005) Protein Expression Purif. , vol.39 , pp. 82-89
    • Schmoldt, H.-U.1    Wentzel, A.2    Becker, S.3    Kolmar, H.4
  • 43
    • 0024959382 scopus 로고
    • The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes
    • Bode, W., Greyling, H. J., Huber, R., Otlewski, J., and Wilusz, T. (1989) The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes FEBS Lett. 242, 285-292 10.1016/0014-5793(89)80486-7
    • (1989) FEBS Lett. , vol.242 , pp. 285-292
    • Bode, W.1    Greyling, H.J.2    Huber, R.3    Otlewski, J.4    Wilusz, T.5
  • 44
    • 0014454095 scopus 로고
    • Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
    • Morrison, J. F. (1969) Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors Biochim. Biophys. Acta BBA-Enzymol 185, 269-286 10.1016/0005-2744(69)90420-3
    • (1969) Biochim. Biophys. Acta BBA - Enzymol , vol.185 , pp. 269-286
    • Morrison, J.F.1
  • 46
    • 75749107430 scopus 로고    scopus 로고
    • Protein dimerization induced by supramolecular interactions with cucurbit[8]uril
    • Nguyen, H. D., Dang, D. T., van Dongen, J. L. J., and Brunsveld, L. (2010) Protein dimerization induced by supramolecular interactions with cucurbit[8]uril Angew. Chem. 122, 907-910 10.1002/ange.200904413
    • (2010) Angew. Chem. , vol.122 , pp. 907-910
    • Nguyen, H.D.1    Dang, D.T.2    Van Dongen, J.L.J.3    Brunsveld, L.4
  • 47
    • 84888018824 scopus 로고    scopus 로고
    • Advances in contact printing technologies of carbohydrate, peptide and protein arrays
    • Voskuhl, J., Brinkmann, J., and Jonkheijm, P. (2014) Advances in contact printing technologies of carbohydrate, peptide and protein arrays Curr. Opin. Chem. Biol. 18, 1-7 10.1016/j.cbpa.2013.10.022
    • (2014) Curr. Opin. Chem. Biol. , vol.18 , pp. 1-7
    • Voskuhl, J.1    Brinkmann, J.2    Jonkheijm, P.3
  • 48
    • 77950924422 scopus 로고    scopus 로고
    • Site-Selective Immobilization of colloids on Au substrates via a noncovalent supramolecular "handcuff"
    • Tian, F., Cheng, N., Nouvel, N., Geng, J., and Scherman, O. A. (2010) Site-Selective Immobilization of colloids on Au substrates via a noncovalent supramolecular "Handcuff" Langmuir 26, 5323-5328 10.1021/la9033386
    • (2010) Langmuir , vol.26 , pp. 5323-5328
    • Tian, F.1    Cheng, N.2    Nouvel, N.3    Geng, J.4    Scherman, O.A.5
  • 49
    • 84055200072 scopus 로고    scopus 로고
    • Determination of the purity of cucurbit[n]uril (n = 7, 8) host samples
    • Yi, S. and Kaifer, A. E. (2011) Determination of the purity of cucurbit[n]uril (n = 7, 8) host samples J. Org. Chem. 76, 10275-10278 10.1021/jo2018312
    • (2011) J. Org. Chem. , vol.76 , pp. 10275-10278
    • Yi, S.1    Kaifer, A.E.2


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