메뉴 건너뛰기




Volumn 7, Issue 7, 1998, Pages 1583-1592

A biomimetic strategy in the synthesis and fragmentation of cyclic protein

Author keywords

Circulin; Cyclic protein; Cyclopsychotride; Cystine knot motif; Orthogonal ligation; Partial acid hydrolysis; Thia zip reaction; Two step disulfide formation

Indexed keywords

DNA FRAGMENT;

EID: 0031822610     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070712     Document Type: Article
Times cited : (111)

References (44)
  • 2
    • 0001153517 scopus 로고
    • Selective reduction of disulfides by Tris(2-carboxyethyl) phosphine
    • Burns JA, Butler JC, Movan J, Whitesides GM. 1991. Selective reduction of disulfides by Tris(2-carboxyethyl) phosphine. J Org Chem 56:2648-2650.
    • (1991) J Org Chem , vol.56 , pp. 2648-2650
    • Burns, J.A.1    Butler, J.C.2    Movan, J.3    Whitesides, G.M.4
  • 3
    • 49549139072 scopus 로고
    • Reactifs de couplage peptidique IV (1)-1′hexafluorophosphate de benzotriazolyl N-oxytrisodiumethylamino phosphonium (B.O.P.)
    • Castro B, Dormoy JR, Evin G, Selve C. 1975. Reactifs de couplage peptidique IV (1)-1′hexafluorophosphate de benzotriazolyl N-oxytrisodiumethylamino phosphonium (B.O.P.). Tetrahedron Lett 14:1219-1222.
    • (1975) Tetrahedron Lett , vol.14 , pp. 1219-1222
    • Castro, B.1    Dormoy, J.R.2    Evin, G.3    Selve, C.4
  • 4
    • 0029116947 scopus 로고
    • Protein splicing: Self-splicing of genetically mobile elements at the protein level
    • Cooper AA, Stevens TH. 1995. Protein splicing: Self-splicing of genetically mobile elements at the protein level. Trends Biosci 20:351-356.
    • (1995) Trends Biosci , vol.20 , pp. 351-356
    • Cooper, A.A.1    Stevens, T.H.2
  • 5
    • 0027122245 scopus 로고
    • Crystal structure of transforming growth factor-beta 2: An unusual fold for the superfamily
    • Daopin S, Pier KA, Ogawa Y, Davies D. 1992. Crystal structure of transforming growth factor-beta 2: An unusual fold for the superfamily. Science 257:369-373.
    • (1992) Science , vol.257 , pp. 369-373
    • Daopin, S.1    Pier, K.A.2    Ogawa, Y.3    Davies, D.4
  • 7
    • 0000014794 scopus 로고
    • Oxytoic principle found in Oldenlandia affinis. An indigenous, congolese drug "Kalata-Kalata" used to accelerate the delivery
    • Gran L. 1970. Oxytoic principle found in Oldenlandia affinis. An indigenous, congolese drug "Kalata-Kalata" used to accelerate the delivery. Medd Nor Fram Selsk 32:173-180.
    • (1970) Medd Nor Fram Selsk , vol.32 , pp. 173-180
    • Gran, L.1
  • 8
    • 0015723952 scopus 로고
    • Effect of a polypeptide isolated from Kalata-Kalata (Oldenlandia affinis) on the estrogen dominated uterus
    • Gran L. 1973. Effect of a polypeptide isolated from Kalata-Kalata (Oldenlandia affinis) on the estrogen dominated uterus. Acta Pharmacol Toxicol 32:400-408.
    • (1973) Acta Pharmacol Toxicol , vol.32 , pp. 400-408
    • Gran, L.1
  • 9
    • 0027448780 scopus 로고
    • Disulfide structures of highly bridged peptides: A new strategy for analysis
    • Gray WR. 1993a. Disulfide structures of highly bridged peptides: A new strategy for analysis. Protein Sci 2:1732-1748.
    • (1993) Protein Sci , vol.2 , pp. 1732-1748
    • Gray, W.R.1
  • 10
    • 0027429593 scopus 로고
    • Echistatin disulfide bridges: Selective reduction and linkage assignment
    • Gray WR. 1993b. Echistatin disulfide bridges: Selective reduction and linkage assignment. Protein Sci 2:1749-1755.
    • (1993) Protein Sci , vol.2 , pp. 1749-1755
    • Gray, W.R.1
  • 12
    • 0024975550 scopus 로고
    • 2D NMR and distance geometry study of the folding of Ecballium elaterium trypsin inhibitor, a member of the squash inhibitors family
    • 2D NMR and distance geometry study of the folding of Ecballium elaterium trypsin inhibitor, a member of the squash inhibitors family. Biochemistry 25:2392-2398.
    • (1989) Biochemistry , vol.25 , pp. 2392-2398
    • Heitz, A.1    Chiche, L.2    Le-Nguyen, D.3    Castro, B.4
  • 15
    • 0024815191 scopus 로고
    • Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamatical simulated annealing
    • Holak T, Gondol D, Otlewski J, Wilusz T. 1989. Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamatical simulated annealing. J Mol Biol 210:635-648.
    • (1989) J Mol Biol , vol.210 , pp. 635-648
    • Holak, T.1    Gondol, D.2    Otlewski, J.3    Wilusz, T.4
  • 16
    • 0014772602 scopus 로고
    • Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides
    • Kaiser E, Colescott RL, Bossinger CD, Cook PI. 1970. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal Biochem 34:595-599.
    • (1970) Anal Biochem , vol.34 , pp. 595-599
    • Kaiser, E.1    Colescott, R.L.2    Bossinger, C.D.3    Cook, P.I.4
  • 17
    • 84943706546 scopus 로고
    • The synthesis of cystine peptides by iodine oxidation of S-trityl-cysteine and S-acetamidomethyl-cysteine peptides
    • Kamber B, Hartmann A, Eisler K, Riniker B, Rink H, Sieber P, Rittel W. 1980. The synthesis of cystine peptides by iodine oxidation of S-trityl-cysteine and S-acetamidomethyl-cysteine peptides. Helv Chim Acta 65:899-915.
    • (1980) Helv Chim Acta , vol.65 , pp. 899-915
    • Kamber, B.1    Hartmann, A.2    Eisler, K.3    Riniker, B.4    Rink, H.5    Sieber, P.6    Rittel, W.7
  • 19
    • 0001525470 scopus 로고
    • Peptide synthesis by prior thiol capture. 1. A convenient synthesis of 4-hydroxy-6-mercaptodibenzofuran and novel solid-phase synthesis of peptide-derived 4-(acyloxy)-6-mercaptodibenzofurans
    • Kemp DS, Galakatos NG. 1986. Peptide synthesis by prior thiol capture. 1. A convenient synthesis of 4-hydroxy-6-mercaptodibenzofuran and novel solid-phase synthesis of peptide-derived 4-(acyloxy)-6-mercaptodibenzofurans. J Org Chem 51:1821-1829.
    • (1986) J Org Chem , vol.51 , pp. 1821-1829
    • Kemp, D.S.1    Galakatos, N.G.2
  • 20
    • 0001445223 scopus 로고
    • Peptide synthesis by thiol capture. 2. Design of templates for intramolecular O,N-acyl transfer. 4,6-disubstituted dibenzofurans as optimal spacing elements
    • Kemp DS, Galakatos NG, Bowen B, Tan K. 1986. Peptide synthesis by thiol capture. 2. Design of templates for intramolecular O,N-acyl transfer. 4,6-disubstituted dibenzofurans as optimal spacing elements. J Org Chem 51:1829-1838.
    • (1986) J Org Chem , vol.51 , pp. 1829-1838
    • Kemp, D.S.1    Galakatos, N.G.2    Bowen, B.3    Tan, K.4
  • 21
    • 0025677740 scopus 로고
    • Enzymatic and chemical digestion of proteins for mass spectrometry
    • Lee TD, Shively JE. 1990. Enzymatic and chemical digestion of proteins for mass spectrometry. Methods Enzymol 193:361-373.
    • (1990) Methods Enzymol , vol.193 , pp. 361-373
    • Lee, T.D.1    Shively, J.E.2
  • 22
    • 0038197659 scopus 로고
    • Partial acid hydrolysis
    • Light A. 1967. Partial acid hydrolysis. Methods Enzymol 11:417-420.
    • (1967) Methods Enzymol , vol.11 , pp. 417-420
    • Light, A.1
  • 23
    • 0028223433 scopus 로고
    • Peptide segment ligation strategy without use of protecting groups
    • Liu C-F, Tam JP. 1994. Peptide segment ligation strategy without use of protecting groups. Proc Natl Acad Sci USA 91:6584-6588.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6584-6588
    • Liu, C.-F.1    Tam, J.P.2
  • 24
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis I. The synthesis of a tetrapeptide
    • Merrifield RB. 1963. Solid phase peptide synthesis I. The synthesis of a tetrapeptide. J Am Chem Soc 85:2149-2154.
    • (1963) J Am Chem Soc , vol.85 , pp. 2149-2154
    • Merrifield, R.B.1
  • 25
    • 0000243053 scopus 로고
    • Solid phase peptide synthesis
    • Merrifield RB. 1986. Solid phase peptide synthesis. Science 57:1619-1625.
    • (1986) Science , vol.57 , pp. 1619-1625
    • Merrifield, R.B.1
  • 26
    • 0028175628 scopus 로고
    • 1H NMR determination of the three-dimensional structure of mirror-image forms of a Leu-5 variant of the trypsin inhibitor from Ecballium elaterium (EETI-II)
    • 1H NMR determination of the three-dimensional structure of mirror-image forms of a Leu-5 variant of the trypsin inhibitor from Ecballium elaterium (EETI-II). Protein Sci 3:291-302.
    • (1994) Protein Sci , vol.3 , pp. 291-302
    • Nielsen, K.J.1    Alewood, D.2    Andrews, J.3    Kent, S.B.4    Craik, D.J.5
  • 27
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded beta-sheet in toxic and inhibitory polypeptides
    • Pallaghy PK, Nielsen KJ, Craik DJ, Norton RS. 1994. A common structural motif incorporating a cystine knot and a triple-stranded beta-sheet in toxic and inhibitory polypeptides. Protein Sci 3:1833-1839.
    • (1994) Protein Sci , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 28
    • 85038535247 scopus 로고    scopus 로고
    • Three highly constrained tricyclic peptide libraries containing three disulfide bonds
    • Kaumaya P, Hodges TP, Robert S, eds. UK: Mayflower Scientific Ltd.
    • Rao C, Tam JP. 1996. Three highly constrained tricyclic peptide libraries containing three disulfide bonds. In: Kaumaya P, Hodges TP, Robert S, eds. Peptide: Chemistry, structure and biology. Proceedings of the Fourteenth American Peptide Symposium. UK: Mayflower Scientific Ltd. pp 299-300.
    • (1996) Peptide: Chemistry, Structure and Biology. Proceedings of the Fourteenth American Peptide Symposium , pp. 299-300
    • Rao, C.1    Tam, J.P.2
  • 29
    • 0019052776 scopus 로고
    • Structure of the potato inhibitor complex of carboxypeptidase a at 2.5-a resolution
    • Rees DC, Lipscomb WN. 1980. Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-A resolution. Proc Natl Acad Sci USA 77:4633-4637.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 4633-4637
    • Rees, D.C.1    Lipscomb, W.N.2
  • 30
    • 0028927655 scopus 로고
    • Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide Kalata B1
    • Saether O, Craik DJ, Campbell ID, Sletten K, Juul J, Norman DG. 1995. Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide Kalata B1. Biochemistry 54:4147-4158.
    • (1995) Biochemistry , vol.54 , pp. 4147-4158
    • Saether, O.1    Craik, D.J.2    Campbell, I.D.3    Sletten, K.4    Juul, J.5    Norman, D.G.6
  • 31
    • 33947476461 scopus 로고
    • An approach to the specific cleavage of peptide bonds. 1. The acyl migration in dipeptides containing hydroxyamino acids in anhydrous hydrogen fluoride
    • Sakakibara K, Shin KH, Hess GP. 1962. An approach to the specific cleavage of peptide bonds. 1. The acyl migration in dipeptides containing hydroxyamino acids in anhydrous hydrogen fluoride. J Am Chem Soc 84:4921.
    • (1962) J Am Chem Soc , vol.84 , pp. 4921
    • Sakakibara, K.1    Shin, K.H.2    Hess, G.P.3
  • 32
    • 0026633842 scopus 로고
    • An unusual feature revealed by the crystal structure at 2.2 a resolution of human transforming growth factor-beta 2
    • Schlunegger MP, Grutter MG. 1992. An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2. Nature 358:430-434.
    • (1992) Nature , vol.358 , pp. 430-434
    • Schlunegger, M.P.1    Grutter, M.G.2
  • 33
    • 77957010574 scopus 로고
    • Cleavage at aspartic acid
    • Schultz J. 1967. Cleavage at aspartic acid. Method Enzymol 11:255-263.
    • (1967) Method Enzymol , vol.11 , pp. 255-263
    • Schultz, J.1
  • 34
    • 77956987576 scopus 로고
    • Techniques in enzymic hydrolysis
    • Smyth DG. 1967. Techniques in enzymic hydrolysis. Methods Enzymol 11:214-231.
    • (1967) Methods Enzymol , vol.11 , pp. 214-231
    • Smyth, D.G.1
  • 35
    • 0030808964 scopus 로고    scopus 로고
    • Synthesis of large cyclic cystine-knot peptide by orthogonal coupling strategy using unprotected peptide precursor
    • Tam JP, Lu Y-A. 1997. Synthesis of large cyclic cystine-knot peptide by orthogonal coupling strategy using unprotected peptide precursor. Tetrahedron Lett 38:5599-5602.
    • (1997) Tetrahedron Lett , vol.38 , pp. 5599-5602
    • Tam, J.P.1    Lu, Y.-A.2
  • 36
    • 0029559773 scopus 로고
    • Peptide synthesis using unprotected peptides through orthogonal coupling methods
    • Tam JP, Lu Y-A, Liu C-F, Shao J. 1995. Peptide synthesis using unprotected peptides through orthogonal coupling methods. Proc Natl Acad Sci USA 92:12485-12489.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12485-12489
    • Tam, J.P.1    Lu, Y.-A.2    Liu, C.-F.3    Shao, J.4
  • 37
    • 12044255356 scopus 로고
    • Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications
    • Tam JP, Wu CR, Liu W, Zhang JW. 1991. Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications. J Am Chem Soc 113:6657-66622.
    • (1991) J Am Chem Soc , vol.113 , pp. 6657-66622
    • Tam, J.P.1    Wu, C.R.2    Liu, W.3    Zhang, J.W.4
  • 38
    • 0021117745 scopus 로고
    • Nonenzymatic formation and isomerization of protein disulfides
    • Wetlaufer DB. 1984. Nonenzymatic formation and isomerization of protein disulfides. Methods Enzymol 107:301-304.
    • (1984) Methods Enzymol , vol.107 , pp. 301-304
    • Wetlaufer, D.B.1
  • 39
    • 84939246733 scopus 로고
    • Polypeptides synthesis. VIII. Formation of sulfur containing peptides by the intramolecular migration of aminoacyl groups
    • Wieland T, Bokelmann E, Bauer L, Lang HU, Lau H, Schafer W. 1953. Polypeptides synthesis. VIII. Formation of sulfur containing peptides by the intramolecular migration of aminoacyl groups. Ann Chem Liebigs 583:129-149.
    • (1953) Ann Chem Liebigs , vol.583 , pp. 129-149
    • Wieland, T.1    Bokelmann, E.2    Bauer, L.3    Lang, H.U.4    Lau, H.5    Schafer, W.6
  • 41
    • 0027753790 scopus 로고
    • In vitro protein splicing of purified precursor and the identification of a branched intermediate
    • Xu MQ, Southworth MW, Mersha FB, Hornstra LJ, Perler FB. 1993. In vitro protein splicing of purified precursor and the identification of a branched intermediate. Cell 75:1371-1377.
    • (1993) Cell , vol.75 , pp. 1371-1377
    • Xu, M.Q.1    Southworth, M.W.2    Mersha, F.B.3    Hornstra, L.J.4    Perler, F.B.5
  • 42
    • 0027935844 scopus 로고
    • Two-step selective formation of three disulfide bridges in the synthesis of the C-terminal epidermal growth factor-like domain in human blood coagulation factor IX
    • Yang Y, Sweeney WV, Schneider K, Chait B, Tam JP. 1994. Two-step selective formation of three disulfide bridges in the synthesis of the C-terminal epidermal growth factor-like domain in human blood coagulation factor IX. Protein Sci 3:1267-1275.
    • (1994) Protein Sci , vol.3 , pp. 1267-1275
    • Yang, Y.1    Sweeney, W.V.2    Schneider, K.3    Chait, B.4    Tam, J.P.5
  • 43
    • 0030897311 scopus 로고    scopus 로고
    • Synthesis and application of unprotected cyclic peptides as building blocks for peptide dendrimers
    • Zhang L, Tam JP. 1997. Synthesis and application of unprotected cyclic peptides as building blocks for peptide dendrimers. J Am Chem Soc 119:2363-2370.
    • (1997) J Am Chem Soc , vol.119 , pp. 2363-2370
    • Zhang, L.1    Tam, J.P.2
  • 44
    • 0025695802 scopus 로고
    • Assignment of disulfide bonds in protein by partial acid hydrolysis and mass spectrometry
    • Zhou Z, Smith DL. 1990. Assignment of disulfide bonds in protein by partial acid hydrolysis and mass spectrometry. J Protein Chem 9:523-532.
    • (1990) J Protein Chem , vol.9 , pp. 523-532
    • Zhou, Z.1    Smith, D.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.