메뉴 건너뛰기




Volumn 33, Issue 1, 2000, Pages 49-53

Structure and Antibiotic Activity of a Porcine Myeloid Antibacterial Peptide, PMAP-23 and its Analogues

Author keywords

Antibacterial activity; Antitumor activity; Phospholipid vesicle disrupting activity; PMAP 23; Secondary structure

Indexed keywords


EID: 0034419840     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (5)

References (22)
  • 1
    • 0026570489 scopus 로고
    • Shortened cecropin A-melittin hybrids: Significant size reduction retains potent antibiotic activity
    • Andreu, D., Ubach, J., Boman, A., Wahlin, D., Wade, D., Merrifield, R.B. and Boman, G. (1992) Shortened cecropin A-melittin hybrids: Significant size reduction retains potent antibiotic activity. FEBS Lett. 296, 190-194.
    • (1992) FEBS Lett. , vol.296 , pp. 190-194
    • Andreu, D.1    Ubach, J.2    Boman, A.3    Wahlin, D.4    Wade, D.5    Merrifield, R.B.6    Boman, G.7
  • 2
    • 0028834275 scopus 로고
    • cDNA sequences of three sheep myeloid cathelicidins
    • Baegella, L., Scocchi, M. and Zanetti, M (1995) cDNA sequences of three sheep myeloid cathelicidins. FEBS Lett. 376, 225-228.
    • (1995) FEBS Lett. , vol.376 , pp. 225-228
    • Baegella, L.1    Scocchi, M.2    Zanetti, M.3
  • 3
    • 0016169865 scopus 로고
    • Helix and β-form of proteins in aqueous solution by circular dichroism
    • Chen, Y. -H., Yang, J. T. and Chau, K. H. (1974) Helix and β-form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 6
    • 0031009432 scopus 로고    scopus 로고
    • Identication of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse
    • Gallo, R. L., Kim, K, J., Bernfield, M., Kozak, C. A., Zanetti, M., Merluzzi, L., and Gennaro, R. (1997) Identication of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse. J. Biol. Chem. 272, 13088-13093.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13088-13093
    • Gallo, R.L.1    Kim, K.J.2    Bernfield, M.3    Kozak, C.A.4    Zanetti, M.5    Merluzzi, L.6    Gennaro, R.7
  • 7
    • 0031046654 scopus 로고    scopus 로고
    • Antimicrobial peptides of leukocytes
    • Ganz T., and Lehrer, R. I. (1997) Antimicrobial peptides of leukocytes. Curr. Opin. Hematol. 4, 53-58.
    • (1997) Curr. Opin. Hematol. , vol.4 , pp. 53-58
    • Ganz, T.1    Lehrer, R.I.2
  • 8
    • 0029893253 scopus 로고    scopus 로고
    • The human gene FALL-39 and processing of the cathelin precursor to the antibacterial peptide LL-39 in granulocytes
    • Gudmundsson, G. H., Agerberth, H. B., Odeberg, J., Bergman, T., Olsson, B. and Salcedo, R. (1996) The human gene FALL-39 and processing of the cathelin precursor to the antibacterial peptide LL-39 in granulocytes. Eur. J. Biochem. 238, 325-332.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 325-332
    • Gudmundsson, G.H.1    Agerberth, H.B.2    Odeberg, J.3    Bergman, T.4    Olsson, B.5    Salcedo, R.6
  • 9
    • 0033476111 scopus 로고    scopus 로고
    • Synthesis and characterization of GGN4 and its tryptophan substituted analogue peptides
    • Kim, S., Kim, J.-Y., Lee, B.-J. and Kim, S.-J. (1999) Synthesis and characterization of GGN4 and its tryptophan substituted analogue peptides. J. Biochem. Mol. Biol. 32, 12-19.
    • (1999) J. Biochem. Mol. Biol. , vol.32 , pp. 12-19
    • Kim, S.1    Kim, J.-Y.2    Lee, B.-J.3    Kim, S.-J.4
  • 10
    • 0029584314 scopus 로고
    • Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptides
    • Mahoney, M. M., Lee, A. Y., Brezinski-Caliguri, D. J. and Huttner, K. M. (1995) Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptides. FEBS Lett. 377, 519-522.
    • (1995) FEBS Lett. , vol.377 , pp. 519-522
    • Mahoney, M.M.1    Lee, A.Y.2    Brezinski-Caliguri, D.J.3    Huttner, K.M.4
  • 11
    • 0022699646 scopus 로고
    • Solid phase synthesis
    • Merrifield, R. B. (1986) Solid phase synthesis. Science 232, 341-347.
    • (1986) Science , vol.232 , pp. 341-347
    • Merrifield, R.B.1
  • 12
    • 0031028188 scopus 로고    scopus 로고
    • Porcine polymorphonuclear leukocytes generate extracelluar microbial activity by elastase-mediated activation of secreted proprotegrins
    • Panyutich, A., Shi, J., Boutz, P. L., Zhao, C. and Ganz, T (1997) Porcine polymorphonuclear leukocytes generate extracelluar microbial activity by elastase-mediated activation of secreted proprotegrins. Infect. Immun. 65, 978-985.
    • (1997) Infect. Immun. , vol.65 , pp. 978-985
    • Panyutich, A.1    Shi, J.2    Boutz, P.L.3    Zhao, C.4    Ganz, T.5
  • 14
    • 3042953076 scopus 로고    scopus 로고
    • Antibacterial activities of peptides designed as hybrids of antimicrobial peptides
    • Shin, S. Y., Kang, J. H., Lee, M. K. and Hahm, K.-S. (1996) Antibacterial activities of peptides designed as hybrids of antimicrobial peptides. J. Biochem. Mol. Biol. 29, 545-548.
    • (1996) J. Biochem. Mol. Biol. , vol.29 , pp. 545-548
    • Shin, S.Y.1    Kang, J.H.2    Lee, M.K.3    Hahm, K.-S.4
  • 15
    • 0000378555 scopus 로고    scopus 로고
    • Structure-antitumor and hemolytic activity cecropin A-magainin 2 and cecropin A-melittin hybrid peptides
    • Shin, S. Y., Lee, M. K., Kim, K. L. and Hahm, K.-S. (1997) Structure-antitumor and hemolytic activity cecropin A-magainin 2 and cecropin A-melittin hybrid peptides. J. Peptide Res. 50, 279-285.
    • (1997) J. Peptide Res. , vol.50 , pp. 279-285
    • Shin, S.Y.1    Lee, M.K.2    Kim, K.L.3    Hahm, K.-S.4
  • 16
    • 0033028126 scopus 로고    scopus 로고
    • Structure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides
    • Shin, S. Y., Kang, J. H. and Hahm, K.-S. (1999) Structure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides. J. Peptide Res. 53, 82-90.
    • (1999) J. Peptide Res. , vol.53 , pp. 82-90
    • Shin, S.Y.1    Kang, J.H.2    Hahm, K.-S.3
  • 17
    • 0029961492 scopus 로고    scopus 로고
    • Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities
    • Skerlavaj, B., Gennaro, R., Bagella, L., Merluzzi, L., Risso, A. and Zanetti, M. (1996) Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J. Biol. Chem. 271, 375-381.
    • (1996) J. Biol. Chem. , vol.271 , pp. 375-381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.3    Merluzzi, L.4    Risso, A.5    Zanetti, M.6
  • 18
    • 0027453329 scopus 로고
    • A cDNA derived from pig bone marrow cells contains a sequence identical to the intestinal antimicrobial peptide PR-39
    • Storici, P. and Zanetti, M. (1993) A cDNA derived from pig bone marrow cells contains a sequence identical to the intestinal antimicrobial peptide PR-39. Biochem. Biophys. Res. Commun. 196, 1058-1065.
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 1058-1065
    • Storici, P.1    Zanetti, M.2
  • 19
    • 0028904007 scopus 로고
    • Porcine myeloid antimicrobial peptide, PMAP-37, a novel antimicrobial peptide from pig myeloid cell: CDNA cloning, chemical synthesis and activity
    • Tossi, A., Scocchi, M., Zanetti, M., Storici, P. and Gennaro, R. (1995) Porcine myeloid antimicrobial peptide, PMAP-37, a novel antimicrobial peptide from pig myeloid cell: cDNA cloning, chemical synthesis and activity. Eur. J. Biochem. 228, 941-946.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 941-946
    • Tossi, A.1    Scocchi, M.2    Zanetti, M.3    Storici, P.4    Gennaro, R.5
  • 20
    • 0027472180 scopus 로고
    • The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor, that is common to other neutrophil antibiotics
    • Zanetti, M., Del Sal, G., Storici, P., Schneider, C. and Romeo, D. (1993) The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor, that is common to other neutrophil antibiotics. J. Biol. Chem. 268, 522-526.
    • (1993) J. Biol. Chem. , vol.268 , pp. 522-526
    • Zanetti, M.1    Del Sal, G.2    Storici, P.3    Schneider, C.4    Romeo, D.5
  • 21
    • 0028244635 scopus 로고
    • Molecular cloning and chemical synthesis of a novel antimicrobial peptide derived from pig myeloid cells
    • Zanetti, M., Storici, P., Tossi. A., Scocchi, M. and Gennaro, R. (1994) Molecular cloning and chemical synthesis of a novel antimicrobial peptide derived from pig myeloid cells. J. Biol. Chem. 269, 7855-7858.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7855-7858
    • Zanetti, M.1    Storici, P.2    Tossi, A.3    Scocchi, M.4    Gennaro, R.5
  • 22
    • 0028263457 scopus 로고
    • Identification of a new member of the protegrin family by cDNA cloning
    • Zhao, C., Liu, L. and Lehrer, R. I. (1994) Identification of a new member of the protegrin family by cDNA cloning. FEBS Lett. 346, 285-288.
    • (1994) FEBS Lett. , vol.346 , pp. 285-288
    • Zhao, C.1    Liu, L.2    Lehrer, R.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.