메뉴 건너뛰기




Volumn 18, Issue 9, 2012, Pages 588-598

Synthesis and properties of cyclic gomesin and analogues

Author keywords

Antimicrobial peptide; Head to tail cyclization; High temperatures; Peptide truncation

Indexed keywords

DIMETHYL SULFOXIDE; GOMESIN DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT; PYROGLUTAMIC ACID; RESIN; UNCLASSIFIED DRUG;

EID: 84865177197     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.2439     Document Type: Article
Times cited : (14)

References (63)
  • 1
    • 33745770017 scopus 로고    scopus 로고
    • Epidemiology study of Candida infections in blood: susceptibilities of Candida spp. to antifungal agents, and clinical features associated with the candidemia
    • Nakamura T, Takahashi H. Epidemiology study of Candida infections in blood: susceptibilities of Candida spp. to antifungal agents, and clinical features associated with the candidemia. J. Infect. Chemother. 2006; 12: 132-138.
    • (2006) J. Infect. Chemother. , vol.12 , pp. 132-138
    • Nakamura, T.1    Takahashi, H.2
  • 2
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: effectors in innate immunity and novel antimicrobials
    • Hancock, REW. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 2001; 1: 156-164.
    • (2001) Lancet Infect. Dis. , vol.1 , pp. 156-164
    • Hancock, R.E.W.1
  • 4
    • 0026076922 scopus 로고
    • Direct virus inactivation of tachyplesin I and its isopeptides from horseshoe crab hemocytes
    • Murakami T, Niwa M, Tokumaga F, Miyata T, Iwanaga S. Direct virus inactivation of tachyplesin I and its isopeptides from horseshoe crab hemocytes. Chemotherapy 1991; 37: 327-334.
    • (1991) Chemotherapy , vol.37 , pp. 327-334
    • Murakami, T.1    Niwa, M.2    Tokumaga, F.3    Miyata, T.4    Iwanaga, S.5
  • 7
    • 0034044911 scopus 로고    scopus 로고
    • In vitro characterization of the anticancer activity of membrane-active cationic peptides. I. Peptide-mediated cytotoxicity and peptide-enhanced cytotoxic activity of doxorubicin against wild-type and p-glycoprotein over-expressing tumor cell lines
    • Johnstone SA, Gelmon K, Mayer LD, Hancock REW, Bally MB. In vitro characterization of the anticancer activity of membrane-active cationic peptides. I. Peptide-mediated cytotoxicity and peptide-enhanced cytotoxic activity of doxorubicin against wild-type and p-glycoprotein over-expressing tumor cell lines. Anticancer Drug Des. 2000; 15: 151-160.
    • (2000) Anticancer Drug Des. , vol.15 , pp. 151-160
    • Johnstone, S.A.1    Gelmon, K.2    Mayer, L.D.3    Hancock, R.E.W.4    Bally, M.B.5
  • 8
    • 0027166016 scopus 로고
    • Anticancer efficacy of magainin 2 and analogue peptides
    • Baker MA, Maloy WL, Zasloff M, Jacob LS. Anticancer efficacy of magainin 2 and analogue peptides. Cancer Res. 1993; 53: 3052-3057.
    • (1993) Cancer Res. , vol.53 , pp. 3052-3057
    • Baker, M.A.1    Maloy, W.L.2    Zasloff, M.3    Jacob, L.S.4
  • 9
  • 10
    • 25444458008 scopus 로고    scopus 로고
    • Anti-endotoxin properties of cationic host defence peptides and protein
    • Bowdish, DME, Hancock REW. Anti-endotoxin properties of cationic host defence peptides and protein. J. Endotoxin Res. 2005; 11: 230-236.
    • (2005) J. Endotoxin Res. , vol.11 , pp. 230-236
    • Bowdish, D.M.E.1    Hancock, R.E.W.2
  • 11
  • 12
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 2003; 55: 27-55.
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 13
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: from invertebrates to vertebrates
    • Bulet P, Stöcklin R, Menin L. Anti-microbial peptides: from invertebrates to vertebrates. Immunol. Rev. 2004; 198: 169-184.
    • (2004) Immunol. Rev. , vol.198 , pp. 169-184
    • Bulet, P.1    Stöcklin, R.2    Menin, L.3
  • 14
    • 0034721871 scopus 로고    scopus 로고
    • Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family
    • Silva Jr. PI, Daffre S, Bulet P. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. J. Biol. Chem. 2000; 275: 33464-33470.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33464-33470
    • Silva Jr, P.I.1    Daffre, S.2    Bulet, P.3
  • 15
    • 33751084109 scopus 로고    scopus 로고
    • Differentiation of Leishmania major is impaired by over-expression of pyroglutamyl peptidase I
    • Schaeffer M, de Miranda A, Mottram JC, Coombs GH. Differentiation of Leishmania major is impaired by over-expression of pyroglutamyl peptidase I. Mol. Biochem. Parasitol. 2006; 150: 318-329.
    • (2006) Mol. Biochem. Parasitol. , vol.150 , pp. 318-329
    • Schaeffer, M.1    de Miranda, A.2    Mottram, J.C.3    Coombs, G.H.4
  • 17
    • 34547901750 scopus 로고    scopus 로고
    • Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole
    • Barbosa FM, Daffre S, Maldonado RA, Miranda A, Nimrichter L, Rodrigues ML. Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole. FEMS Microbiol. Lett. 2007; 274: 279-286.
    • (2007) FEMS Microbiol. Lett. , vol.274 , pp. 279-286
    • Barbosa, F.M.1    Daffre, S.2    Maldonado, R.A.3    Miranda, A.4    Nimrichter, L.5    Rodrigues, M.L.6
  • 18
    • 77951108517 scopus 로고    scopus 로고
    • Gomesin: a powerful antimicrobial peptide isolated from the Brazilian tarantula spider Acanthoscurria gomesiana
    • Lima MH, Pimenta AMC, Martin-Eauclaire MF (eds). Editora UFMG: Belo Horizonte
    • Miranda A, Miranda MTM, Jouvensal L, Volvelle F, Bulet P; Daffre S. Gomesin: a powerful antimicrobial peptide isolated from the Brazilian tarantula spider Acanthoscurria gomesiana. In: Animal Toxins: State of the art. Perspectives in Health and Biotechnology, Lima MH, Pimenta AMC, Martin-Eauclaire MF (eds). Editora UFMG: Belo Horizonte, 2009; 323-343.
    • (2009) Animal Toxins: State of the art. Perspectives in Health and Biotechnology , pp. 323-343
    • Miranda, A.1    Miranda, M.T.M.2    Jouvensal, L.3    Volvelle, F.4    Bulet, P.5    Daffre, S.6
  • 19
    • 0036178451 scopus 로고    scopus 로고
    • The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider
    • Mandard N, Bulet P, Caille A, Daffre S, Vovelle F. The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider. Eur. J. Biochem. 2002; 269: 1190-1198.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1190-1198
    • Mandard, N.1    Bulet, P.2    Caille, A.3    Daffre, S.4    Vovelle, F.5
  • 20
    • 33645739232 scopus 로고    scopus 로고
    • Structure-activity relationship studies of gomesin: importance of the disulfide bridges for conformation, bioactivities, and serum stability
    • Fázio MA, Oliveira VX, Bulet P, Miranda MTM, Daffre S, Miranda A. Structure-activity relationship studies of gomesin: importance of the disulfide bridges for conformation, bioactivities, and serum stability. Biopolymers 2006; 84: 205-218.
    • (2006) Biopolymers , vol.84 , pp. 205-218
    • Fázio, M.A.1    Oliveira, V.X.2    Bulet, P.3    Miranda, M.T.M.4    Daffre, S.5    Miranda, A.6
  • 21
    • 34248377855 scopus 로고    scopus 로고
    • Biological and structural characterization of new linear gomesin analogues with improved therapeutic indices
    • Fázio MA, Jouvensal L, Vovelle F, Bulet P, Miranda MTM, Daffre S, Miranda A. Biological and structural characterization of new linear gomesin analogues with improved therapeutic indices. Biopolymers 2007; 88: 386-400.
    • (2007) Biopolymers , vol.88 , pp. 386-400
    • Fázio, M.A.1    Jouvensal, L.2    Vovelle, F.3    Bulet, P.4    Miranda, M.T.M.5    Daffre, S.6    Miranda, A.7
  • 22
    • 64549117769 scopus 로고    scopus 로고
    • Effect of ring size on conformation and biological activity of cyclic cationic antimicrobial peptides
    • Jelokhani-Niaraki M, Kondejewski LH, Wheaton LC, Hodges RS. Effect of ring size on conformation and biological activity of cyclic cationic antimicrobial peptides. J. Med. Chem. 2009; 52: 2090-2097.
    • (2009) J. Med. Chem. , vol.52 , pp. 2090-2097
    • Jelokhani-Niaraki, M.1    Kondejewski, L.H.2    Wheaton, L.C.3    Hodges, R.S.4
  • 23
    • 0034635459 scopus 로고    scopus 로고
    • Engineered salt-insensitive α-defensins with end-to-end circularized structures
    • Yu Q, Lehrer RI, Tam JP. Engineered salt-insensitive α-defensins with end-to-end circularized structures. J. Biol. Chem. 2000; 275: 3943-3949.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3943-3949
    • Yu, Q.1    Lehrer, R.I.2    Tam, J.P.3
  • 24
    • 3142691160 scopus 로고    scopus 로고
    • Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan- containing hexapeptides
    • Dathe M, Nikolenko H, Klose J, Bienert M. Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan- containing hexapeptides. Biochemistry 2004; 43: 9140-9150.
    • (2004) Biochemistry , vol.43 , pp. 9140-9150
    • Dathe, M.1    Nikolenko, H.2    Klose, J.3    Bienert, M.4
  • 25
    • 0034113230 scopus 로고    scopus 로고
    • Membranolytic selectivity of cystine-stabilized cyclic protegrins
    • Tam JP, Wu CW, Yang JL. Membranolytic selectivity of cystine-stabilized cyclic protegrins. Eur. J. Biochem. 2000; 267: 3289-3300.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3289-3300
    • Tam, J.P.1    Wu, C.W.2    Yang, J.L.3
  • 26
    • 0029816946 scopus 로고    scopus 로고
    • Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs
    • Kondejewski LH, Farmer SW, Wishart DS, Kay CM, Hancock REW, Hodges RS. Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs. J. Biol. Chem. 1996; 271: 25261-25268.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25261-25268
    • Kondejewski, L.H.1    Farmer, S.W.2    Wishart, D.S.3    Kay, C.M.4    Hancock, R.E.W.5    Hodges, R.S.6
  • 27
    • 33750080503 scopus 로고    scopus 로고
    • De novo designed cyclic cationic peptides as inhibitors of plant pathogenic bacteria
    • Monroc S, Badosa EFL, Planas M, Montesinos E, Bardaji E. De novo designed cyclic cationic peptides as inhibitors of plant pathogenic bacteria. Peptides 2006; 27: 2567-2574.
    • (2006) Peptides , vol.27 , pp. 2567-2574
    • Monroc, S.1    Badosa, E.F.L.2    Planas, M.3    Montesinos, E.4    Bardaji, E.5
  • 29
    • 2142812891 scopus 로고    scopus 로고
    • Racemization in stepwise solid-phase peptide synthesis at elevated temperature
    • Souza MP, Tavares MFM, Miranda MTM. Racemization in stepwise solid-phase peptide synthesis at elevated temperature. Tetrahedron 2004; 60: 4671-4681.
    • (2004) Tetrahedron , vol.60 , pp. 4671-4681
    • Souza, M.P.1    Tavares, M.F.M.2    Miranda, M.T.M.3
  • 30
    • 60149097224 scopus 로고    scopus 로고
    • Acanthoscurrin fragment 101-132: total synthesis at 60°C of a novel difficult sequence
    • Remuzgo C, Andrade GFS, Temperini MLA, Miranda MTM. Acanthoscurrin fragment 101-132: total synthesis at 60°C of a novel difficult sequence. Biopolymers 2009; 92: 65-75.
    • (2009) Biopolymers , vol.92 , pp. 65-75
    • Remuzgo, C.1    Andrade, G.F.S.2    Temperini, M.L.A.3    Miranda, M.T.M.4
  • 31
    • 73349124783 scopus 로고    scopus 로고
    • Microwave-assisted solid phase peptide synthesis at 60°C: alternative conditions with low enantiomerization
    • Loffredo C, Assunção NA, Gerhardt J, Miranda MTM. Microwave-assisted solid phase peptide synthesis at 60°C: alternative conditions with low enantiomerization. J. Pept. Sci. 2009; 15, 808-817.
    • (2009) J. Pept. Sci. , vol.15 , pp. 808-817
    • Loffredo, C.1    Assunção, N.A.2    Gerhardt, J.3    Miranda, M.T.M.4
  • 32
    • 34248370596 scopus 로고    scopus 로고
    • Truncation of amidated fragment 33-61 of bovine α-hemoglobin: effects on the structure and anticandidal activity
    • Machado A, Sforça ML, Miranda A, Daffre S, Pertinhez TA, Spisni A, Miranda MTM. Truncation of amidated fragment 33-61 of bovine α-hemoglobin: effects on the structure and anticandidal activity. Biopolymers 2007; 88: 413-426.
    • (2007) Biopolymers , vol.88 , pp. 413-426
    • Machado, A.1    Sforça, M.L.2    Miranda, A.3    Daffre, S.4    Pertinhez, T.A.5    Spisni, A.6    Miranda, M.T.M.7
  • 33
    • 0014772602 scopus 로고
    • Color test for the detection of free terminal amino groups in the solid-phase synthesis of peptides
    • Kaiser E, Colescott RL, Bossinger CD, Cook PI. Color test for the detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal. Biochem. 1970; 34: 595-598.
    • (1970) Anal. Biochem. , vol.34 , pp. 595-598
    • Kaiser, E.1    Colescott, R.L.2    Bossinger, C.D.3    Cook, P.I.4
  • 34
    • 0026690649 scopus 로고
    • Synthesis of 'head-to-tail' cyclized peptides on solid support by Fmoc chemistry
    • Trzeciak A, Bannwarth W. Synthesis of 'head-to-tail' cyclized peptides on solid support by Fmoc chemistry. Tetrahedron Lett. 1992; 33: 4557-4560.
    • (1992) Tetrahedron Lett. , vol.33 , pp. 4557-4560
    • Trzeciak, A.1    Bannwarth, W.2
  • 35
    • 0026320903 scopus 로고
    • Solid phase synthesis of a cyclic peptide using Fmoc chemistry
    • McMurray JS. Solid phase synthesis of a cyclic peptide using Fmoc chemistry. Tetrahedron Lett. 1991; 32: 7679-7682.
    • (1991) Tetrahedron Lett. , vol.32 , pp. 7679-7682
    • McMurray, J.S.1
  • 36
    • 0025730051 scopus 로고
    • Synthesis of cyclic peptides on solid support
    • Rovero P, Quartara L, Fabbri G. Synthesis of cyclic peptides on solid support. Tetrahedron Lett. 1991; 32: 2639-2642.
    • (1991) Tetrahedron Lett. , vol.32 , pp. 2639-2642
    • Rovero, P.1    Quartara, L.2    Fabbri, G.3
  • 37
    • 84865188598 scopus 로고    scopus 로고
    • Lactam bridge formation at high temperature
    • (Proc. 18th. Am. Pept. Symp.) Chorev M, Sawyer TK (eds). American Peptide Society: San Diego
    • Machado A, Xavier GC, Miranda A, Miranda MTM. Lactam bridge formation at high temperature. In Peptide Revolution: Genomics, Proteomics & Therapeutics (Proc. 18th. Am. Pept. Symp.) Chorev M, Sawyer TK (eds). American Peptide Society: San Diego, 2004; 192-193.
    • (2004) Peptide Revolution: Genomics, Proteomics & Therapeutics , pp. 192-193
    • Machado, A.1    Xavier, G.C.2    Miranda, A.3    Miranda, M.T.M.4
  • 39
    • 0028587829 scopus 로고
    • Insect immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides
    • Fehlbaum P, Bulet P, Michaut L, Lagueux M, Broekaert WF, Hetru C, Hoffmann JA. Insect immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides. J. Biol. Chem. 1994; 269: 33159-33163.
    • (1994) J. Biol. Chem. , vol.269 , pp. 33159-33163
    • Fehlbaum, P.1    Bulet, P.2    Michaut, L.3    Lagueux, M.4    Broekaert, W.F.5    Hetru, C.6    Hoffmann, J.A.7
  • 41
    • 2042487484 scopus 로고
    • Conformational analysis of pseudocyclic hexapeptides based on quantitative circular dichroism (CD), NOE, and X-ray data. The pure CD spectra of type I and II β-turns
    • Perczel A, Hollósi M, Foxman BM, Fasman GD. Conformational analysis of pseudocyclic hexapeptides based on quantitative circular dichroism (CD), NOE, and X-ray data. The pure CD spectra of type I and II β-turns. J. Am. Chem. Soc. 1991; 113: 9772-9784.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9772-9784
    • Perczel, A.1    Hollósi, M.2    Foxman, B.M.3    Fasman, G.D.4
  • 42
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield NJ, Fasman GD. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 1969; 8: 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.J.1    Fasman, G.D.2
  • 43
    • 84872602077 scopus 로고    scopus 로고
    • Synthesis of conformationally constrained head-to-tail cyclic gomesin
    • (Proc. 27th. Eur. Pept. Symp.), Benedetti E., Pedone C (eds.). Edizione Ziino: Napoli, Italy, Abstract published in J. Pept. Sci., 2002; 8: S88 (PA44).
    • Machado A, Fázio, MA, Miranda A, Daffre S, Miranda MTM. Synthesis of conformationally constrained head-to-tail cyclic gomesin. In: Peptides 2002 (Proc. 27th. Eur. Pept. Symp.), Benedetti E., Pedone C (eds.). Edizione Ziino: Napoli, Italy, 2002; 224-225. Abstract published in J. Pept. Sci., 2002; 8: S88 (PA44).
    • (2002) Peptides 2002 , pp. 224-225
    • Machado, A.1    Fázio, M.A.2    Miranda, A.3    Daffre, S.4    Miranda, M.T.M.5
  • 44
    • 0343770890 scopus 로고
    • (Proc. 13th. Am. Pept. Symp.), Hodges RS, Smith JA (eds.). Escom Science Publishers BV: Leiden, The Netherlands
    • Rabinovich AK, Rivier JE. In Peptides: Chemistry, Structure and Biology (Proc. 13th. Am. Pept. Symp.), Hodges RS, Smith JA (eds.). Escom Science Publishers BV: Leiden, The Netherlands, 1994; 71-73.
    • (1994) Peptides: Chemistry, Structure and Biology , pp. 71-73
    • Rabinovich, A.K.1    Rivier, J.E.2
  • 45
    • 0030743067 scopus 로고    scopus 로고
    • Solid-phase peptide synthesis at elevated temperature: a search for an optimized synthesis condition of unsulfated cholecystokinin-12
    • Varanda LM, Miranda MTM. Solid-phase peptide synthesis at elevated temperature: a search for an optimized synthesis condition of unsulfated cholecystokinin-12. J. Pept. Res. 1997; 50: 102-108.
    • (1997) J. Pept. Res. , vol.50 , pp. 102-108
    • Varanda, L.M.1    Miranda, M.T.M.2
  • 46
    • 68649128681 scopus 로고    scopus 로고
    • Solid-phase peptide synthesis at elevated temperature
    • E22a, Goodman M, Felix A, Moroder L, Toniolo C (eds.). Thieme: Stuttgart
    • Rivier JE, Miranda MTM. Solid-phase peptide synthesis at elevated temperature. In: Synthesis of Peptides and Peptidomimetics, vol. E22a, Goodman M, Felix A, Moroder L, Toniolo C (eds.). Thieme: Stuttgart, 2002; 806-813.
    • (2002) Synthesis of Peptides and Peptidomimetics , pp. 806-813
    • Rivier, J.E.1    Miranda, M.T.M.2
  • 47
    • 34249998983 scopus 로고    scopus 로고
    • A convenient microwave-enhanced solid-phase synthesis of difficult peptide sequences: case study of gramicidin A and CSF114(Glc)
    • Rizzolo F, Sabatino G, Chelli M, Rovero P, Papini AM. A convenient microwave-enhanced solid-phase synthesis of difficult peptide sequences: case study of gramicidin A and CSF114(Glc). Int. J. Pept. Protein Chem. Bio. 2007; 13: 203-208.
    • (2007) Int. J. Pept. Protein Chem. Bio. , vol.13 , pp. 203-208
    • Rizzolo, F.1    Sabatino, G.2    Chelli, M.3    Rovero, P.4    Papini, A.M.5
  • 48
    • 54549091070 scopus 로고    scopus 로고
    • Advances in automatic, manual and microwave-assisted solid-phase peptide synthesis
    • Sabatino G, Papini AM. Advances in automatic, manual and microwave-assisted solid-phase peptide synthesis. Curr. Opin. Drug Discov. Devel. 2008; 11: 762-770.
    • (2008) Curr. Opin. Drug Discov. Devel. , vol.11 , pp. 762-770
    • Sabatino, G.1    Papini, A.M.2
  • 49
    • 33750086978 scopus 로고    scopus 로고
    • Rapid solid-phase peptide synthesis using thermal and controlled microwave irradiation
    • Bacsa B, Desai B, Gábar D, Kappe CO. Rapid solid-phase peptide synthesis using thermal and controlled microwave irradiation. J. Pept. Sci. 2006; 12: 633-638.
    • (2006) J. Pept. Sci. , vol.12 , pp. 633-638
    • Bacsa, B.1    Desai, B.2    Gábar, D.3    Kappe, C.O.4
  • 50
    • 53049110370 scopus 로고    scopus 로고
    • Solid-phase synthesis of difficult peptide sequences at elevated temperatures: a critical comparison of microwave and conventional heating technologies
    • Bacsa B, Horváti K, Bosze S, Andreae F, Kappe CO. Solid-phase synthesis of difficult peptide sequences at elevated temperatures: a critical comparison of microwave and conventional heating technologies. J. Org. Chem. 2008; 73: 7532-7542.
    • (2008) J. Org. Chem. , vol.73 , pp. 7532-7542
    • Bacsa, B.1    Horváti, K.2    Bosze, S.3    Andreae, F.4    Kappe, C.O.5
  • 51
    • 84865183888 scopus 로고    scopus 로고
    • Enhanced microwave assisted on-bead disulfide bond formation method. Synthesis of alpha-conotoxin MII
    • Galanis AS, Albericio F, Grotli M. Enhanced microwave assisted on-bead disulfide bond formation method. Synthesis of alpha-conotoxin MII. J. Pept. Sci. 2008; 14: 73-74.
    • (2008) J. Pept. Sci. , vol.14 , pp. 73-74
    • Galanis, A.S.1    Albericio, F.2    Grotli, M.3
  • 52
    • 74749087800 scopus 로고    scopus 로고
    • Microwave-assisted TFA cleavage of peptides from Merrifield resin
    • Kluczyk A, Rudowska M, Stefanowicz P, Szewczuk Z. Microwave-assisted TFA cleavage of peptides from Merrifield resin. J. Pept. Sci. 2009; 16: 31-39.
    • (2009) J. Pept. Sci. , vol.16 , pp. 31-39
    • Kluczyk, A.1    Rudowska, M.2    Stefanowicz, P.3    Szewczuk, Z.4
  • 55
    • 37349099056 scopus 로고    scopus 로고
    • Fast Fmoc synthesis of hAmylin(1-37) with pseudoproline assisted on-resin disulfide formation
    • Page K, Hood CA, Patel H, Fuentes G, Menakuru M, Park JH. Fast Fmoc synthesis of hAmylin(1-37) with pseudoproline assisted on-resin disulfide formation. J. Pept. Sci. 2007; 13: 833-838.
    • (2007) J. Pept. Sci. , vol.13 , pp. 833-838
    • Page, K.1    Hood, C.A.2    Patel, H.3    Fuentes, G.4    Menakuru, M.5    Park, J.H.6
  • 56
    • 0001340257 scopus 로고    scopus 로고
    • Infuence of proline and β-turn mimetics on the cyclization of penta- and hexapeptides
    • Klose, J, Ehrlich, A, Bienert, M. Infuence of proline and β-turn mimetics on the cyclization of penta- and hexapeptides. Lett. Pept. Sci. 1998; 5: 129-131.
    • (1998) Lett. Pept. Sci. , vol.5 , pp. 129-131
    • Klose, J.1    Ehrlich, A.2    Bienert, M.3
  • 57
    • 79951558237 scopus 로고    scopus 로고
    • An efficient approach for the total synthesis of cyclotides by microwave assisted Fmoc-SPPS
    • Park S, Gunasekera S, Leta Aboye T, Göransson U. An efficient approach for the total synthesis of cyclotides by microwave assisted Fmoc-SPPS. Int. J. Pept. Res. Ther. 2010; 16: 167-176
    • (2010) Int. J. Pept. Res. Ther. , vol.16 , pp. 167-176
    • Park, S.1    Gunasekera, S.2    Leta Aboye, T.3    Göransson, U.4
  • 59
    • 79960514193 scopus 로고    scopus 로고
    • Photocontrol of peptide function: backbone cyclization strategy with photocleavable amino acid
    • Umezawa N, Noro Y, Ukai K, Katao N, Higuchi T. Photocontrol of peptide function: backbone cyclization strategy with photocleavable amino acid. Chembiochem, 2011; 12: 1694-8.
    • (2011) Chembiochem , vol.12 , pp. 1694-1698
    • Umezawa, N.1    Noro, Y.2    Ukai, K.3    Katao, N.4    Higuchi, T.5
  • 60
    • 0041475925 scopus 로고    scopus 로고
    • The cyclization of peptides and depsipeptides
    • Davies JS. The cyclization of peptides and depsipeptides. J. Pept. Sci. 2003; 9: 471-501.
    • (2003) J. Pept. Sci. , vol.9 , pp. 471-501
    • Davies, J.S.1
  • 61
    • 0029831079 scopus 로고    scopus 로고
    • Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations
    • Harwig SSL, Waring A, Yang HJ, Cho Y, Tan L, Lehrer RI. Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations. Eur. J. Biohem. 1996; 240: 352-357.
    • (1996) Eur. J. Biohem. , vol.240 , pp. 352-357
    • Harwig, S.S.L.1    Waring, A.2    Yang, H.J.3    Cho, Y.4    Tan, L.5    Lehrer, R.I.6
  • 62
    • 34548336781 scopus 로고    scopus 로고
    • Molecular dynamics simulations of free protegrin-type antimicrobial peptides: interplay between charges at the termini, β-sheet structure and amphiphilic interactions
    • Bolintineanu DS, Langham, AA, Davis HT, Kaznessis YN. Molecular dynamics simulations of free protegrin-type antimicrobial peptides: interplay between charges at the termini, β-sheet structure and amphiphilic interactions. Mol. Simul. 2007; 33: 809-819.
    • (2007) Mol. Simul. , vol.33 , pp. 809-819
    • Bolintineanu, D.S.1    Langham, A.A.2    Davis, H.T.3    Kaznessis, Y.N.4
  • 63
    • 0037662757 scopus 로고    scopus 로고
    • Antibacterial properties of the sperm-binding proteins and peptides of human epididymis 2 (HE2) family; salt sensitivity, structural dependence and their interaction with outer and cytoplasmic membranes of Escherichia coli
    • Yenugu S, Hamil KG, Birse CE, Ruben SM, French FS, Hall SH. Antibacterial properties of the sperm-binding proteins and peptides of human epididymis 2 (HE2) family; salt sensitivity, structural dependence and their interaction with outer and cytoplasmic membranes of Escherichia coli. Biochem. J. 2003; 372: 473-483.
    • (2003) Biochem. J. , vol.372 , pp. 473-483
    • Yenugu, S.1    Hamil, K.G.2    Birse, C.E.3    Ruben, S.M.4    French, F.S.5    Hall, S.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.