參考文獻 |
1. Hsu, C.H., et al., Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA. Nucleic Acids Research, 2005. 33(13): p. 4053-4064.
2. Marsha, S.H. and G. Arenas, Antimicrobial peptides: A natural alternative to chemical antibiotics and a potential for applied biotechnology. Electronic Journal of Biotechnology 2003. 6.
3. Hancock, R.E.W. and D.S. Chapple, Peptide antibiotics. Antimicrobial Agents and Chemotherapy, 1999. 43(6): p. 1317-1323.
4. Wimley, W.C. and S.H. White, Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nature Structural Biology, 1996. 3(10): p. 842-848.
5. Michl, H. and A. Csordas, Isolation and structure of a haemolytic polypeptide from the defensive secretion of European Bombina species. Chemical Monthly, 1970. 101: p. 182-189.
6. Habermann, E., Bee and Wasp Venoms Science, 1972. 177: p. 314-322
7. Boman, H.G., Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature, 1981. 292: p. 246-248.
8. Lehrer, R., Microbicidal Cationic Proteins in Rabbit Alveolar Macrophages: a Potential Host Defense Mechanism. INFECTION AND IMMUNITY, 1980. 30: p. 180-192.
9. Lehrer, R., Defensins:Natural Peptide Antibiotics of Human Neutrophils. J. Clin. Invest., 1985. 76: p. 1427-1435.
10. Matanic, V.C.A. and V. Castilla, Antiviral activity of antimicrobial cationic peptides against Junin virus and herpes simplex virus. International Journal of Antimicrobial Agents, 2004. 23(4): p. 382-389.
11. Morikawa, N., K. Hagiwaraa, and T. Nakajima, Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa. 1992. 189: p. 184-90.
12. Zasloff, M., Magainins, a class of antimicrobial peptides from Xenopus skin:Isolation, characterization of two active forms, and partial cDNA sequence of a precursor. PNAS, 1987. 84: p. 5449-5453.
13. Selsted, M.E., et al., Indolicidin, a Novel Bactericidal Tridecapeptide Amide from Neutrophils. Journal of Biological Chemistry, 1992. 267(7): p. 4292-4295.
14. Lawyer, C., et al., Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides. Febs Letters, 1996. 390(1): p. 95-98.
15. CABIAUX, V., et al., Secondary structure and membrane interaction of PR-39,a Pro+Arg-rich antibacterial peptide. Eur. J. Biochem., 1994. 224: p. 1019-1027.
16. Radermacher, S., V. Schoop, and H. Schluesener, Bactenecin, a leukocytic antimicrobial peptide, is cytotoxic to neuronal and glial cells. J Neurosci Res, 1993. 15: p. 657-662.
17. Ding, B., et al., Correlation of the antibacterial activities of cationic peptide antibiotics and cationic steroid antibiotics. Journal of Medicinal Chemistry, 2002. 45(3): p. 663-669.
18. Falla, T.J., D.N. Karunaratne, and R.E.W. Hancock, Mode of action of the antimicrobial peptide indolicidin. Journal of Biological Chemistry, 1996. 271(32): p. 19298-19303.
19. Yang, L., et al., Barrel-stave model or toroidal model? A case study on melittin pores. Biophysical Journal, 2001. 81(3): p. 1475-1485.
20. Biggin, P.C. and M.S.P. Sansom, Interactions of alpha-helices with lipid bilayers: a review of simulation studies. Biophysical Chemistry, 1999. 76(3): p. 161-183.
21. Miteva, M., et al., Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK-lysin. Febs Letters, 1999. 462(1-2): p. 155-158.
22. Pokorny, A. and P.F.F. Almeida, Kinetics of dye efflux and lipid flip-flop induced by delta-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, alpha-helical peptides. Biochemistry, 2004. 43(27): p. 8846-8857.
23. Chan, D.I., E.J. Prenner, and H.J. Vogel, Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action. Biochimica Et Biophysica Acta-Biomembranes, 2006. 1758(9): p. 1184-1202.
24. Ludtke, S.J., et al., Membrane pores induced by magainin. Biochemistry, 1996. 35(43): p. 13723-13728.
25. Matsuzaki, K., Why and how are peptide^lipid interactions utilized for self-defense?
Magainins and tachyplesins as archetypes. Biochimica Et Biophysica Acta-Biomembranes, 1999. 1462(1-10).
26. Kawano, K., et al., Antimicrobial Peptide, Tachyplesin-I, Isolated from Hemocytes of the Horseshoe-Crab (Tachypleus-Tridentatus) - Nmr Determination of the Beta-Sheet Structure. Journal of Biological Chemistry, 1990. 265(26): p. 15365-15367.
27. Matsuzaki, K., et al., Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, tachyplesin I, and its linear analog. Biochemistry, 1997. 36(32): p. 9799-9806.
28. Rozek, A., C.L. Friedrich, and R.E.W. Hancock, Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry, 2000. 39(51): p. 15765-15774.
29. Lee, D.G., et al., Fungicidal effect of indolicidin and its interaction with phospholipid membranes. Biochemical and Biophysical Research Communications, 2003. 305(2): p. 305-310.
30. Robinson, W.E., et al., Anti-HIV-1 activity of indolicidin, an antimicrobial peptide from neutrophils. Journal of Leukocyte Biology, 1998. 63(1): p. 94-100.
31. Schluesener, H.J., et al., Leukocytic Antimicrobial Peptides Kill Autoimmune T-Cells. Journal of Neuroimmunology, 1993. 47(2): p. 199-202.
32. Ahmad, I., et al., Liposomal Entrapment of the Neutrophil-Derived Peptide Indolicidin Endows It with in-Vivo Antifungal Activity. Biochimica Et Biophysica Acta-Biomembranes, 1995. 1237(2): p. 109-114.
33. Subbalakshmi, C., et al., Requirements for antibacterial and hemolytic activities in the bovine neutrophil derived 13-residue peptide indolicidin. Febs Letters, 1996. 395(1): p. 48-52.
34. Halevy, R., et al., Membrane binding and permeation by indolicidin analogs studied by a biomimetic lipid/polydiacetylene vesicle assay. Peptides, 2003. 24(11): p. 1753-1761.
35. Subbalakshmi, C. and N. Sitaram, Mechanism of antimicrobial action of indolicidin. Fems Microbiology Letters, 1998. 160(1): p. 91-96.
36. Marchand, C., et al., Covalent binding of the natural antimicrobial peptide indolicidin to DNA abasic sites. Nucleic Acids Research, 2006. 34(18): p. 5157-5165.
37. Staubitz, P., et al., Structure-function relationships in the tryptophan-rich, antimicrobial peptide indolicidin. Journal of Peptide Science, 2001. 7(10): p. 552-564.
38. Yang, S.T., et al., Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide. Biochemical and Biophysical Research Communications, 2002. 296(5): p. 1044-1050.
39. Falla, T.J. and R.E.W. Hancock, Improved activity of a synthetic indolicidin analog. Antimicrobial Agents and Chemotherapy, 1997. 41(4): p. 771-775.
40. Wu, M.H., et al., Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry, 1999. 38(22): p. 7235-7242.
41. Rozek, A., et al., Structure-based design of an indolicidin peptide analogue with increased protease stability. Biochemistry, 2003. 42(48): p. 14130-14138.
42. Friedrich, C.L., et al., Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria. Journal of Biological Chemistry, 2001. 276(26): p. 24015-24022.
43. Friedrich, C.L., et al., Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria. Antimicrobial Agents and Chemotherapy, 2000. 44(8): p. 2086-2092.
44. Yew, W.S. and H.E. Khoo, The role of tryptophan residues in the hemolytic activity of stonustoxin, a lethal factor from stonefish (Synanceja horrida) venom. Biochimie, 2000. 82(3): p. 251-257.
45. Subbalakshmi, C., et al., Antibacterial and hemolytic activities of single tryptophan analogs of indolicidin. Biochemical and Biophysical Research Communications, 2000. 274(3): p. 714-716.
46. Ladokhin, A.S., M.E. Selsted, and S.H. White, Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids. Biophysical Journal, 1997. 72(2): p. 794-805.
47. Zhao, H.X., et al., Comparison of the membrane association of two antimicrobial peptides, magainin 2 and indolicidin. Biophysical Journal, 2001. 81(5): p. 2979-2991.
48. Schibli, D.J., et al., Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions. Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire, 2002. 80(5): p. 667-677.
49. Tsai, C.W., et al. Molecular dynamic simulation of the penetration of indolicidin into lipid bilayer. in 6th Asia-Europe Biorecognition Engineering Society Meeting. 2007. Jong-Li, Taiwan.
50. Skoog, D.A., et al., Principles of instrumental analysis. 1997: Brooks/Cole.
51. Wetlaufer, D.B., Ultraviolet spectra of proteins and amino acids. Advances in Protein Chemistry 1962. 17: p. 303–390.
52. Teale, F.W.J. and G. Weber, Ultraviolet Fluorescence of the Aromatic Amino Acids. Biochem. J., 1957. 65: p. 476-482.
53. Petsko, G.A. and D. Ringe, Protein Structure and Function. January 2004: Sinauer Associates. 180.
54. ChooSmith, L.P. and W.K. Surewicz, The interaction between Alzheimer amyloid beta(1-40) peptide and ganglioside G(M1)-containing membranes. Febs Letters, 1997. 402(2-3): p. 95-98.
55. Ladokhin, A.S., M.E. Selsted, and S.H. White, CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix. Biochemistry, 1999. 38(38): p. 12313-12319.
56. Andrushchenko, V.V., H.J. Vogel, and E.J. Prenner, Solvent-dependent structure of two tryptophan-rich antimicrobial peptides and their analogs studied by FTIR and CD spectroscopy. Biochimica Et Biophysica Acta-Biomembranes, 2006. 1758(10): p. 1596-1608.
57. Yan, H.S., et al., Individual substitution analogs of Mel(12-26), melittin's C-terminal 15-residue peptide: their antimicrobial and hemolytic actions. Febs Letters, 2003. 554(1-2): p. 100-104.
58. Sun, X.J., et al., Deletion of two C-terminal Gln residues of 12-26-residue fragment of melittin improves its antimicrobial activity. Peptides, 2005. 26(3): p. 369-375.
59. Dykes, G.A., S. Aimoto, and J.W. Hastings, Modification of a synthetic antimicrobial peptide (ESF1) for improved inhibitory activity. Biochemical and Biophysical Research Communications, 1998. 248(2): p. 268-272.
60. Gazit, E., et al., Mode of Action of the Antibacterial Cecropin B2 - a Spectrofluorometric Study. Biochemistry, 1994. 33(35): p. 10681-10692.
61. Jureti, D., et al., Magainin 2 amide and analogues Antimicrobial activity, membrane depolarization and susceptibility to proteolysis FEBS Letters, 1989. 249: p. 219–23.
62. Groisman, E.A., et al., Resistance to Host Antimicrobial Peptides Is Necessary for Salmonella Virulence. Proceedings of the National Academy of Sciences of the United States of America, 1992. 89(24): p. 11939-11943.
63. Stumpe, S., et al., Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli. Journal of Bacteriology, 1998. 180(15): p. 4002-4006.
64. Ulvatne, H., et al., Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B. Journal of Antimicrobial Chemotherapy, 2002. 50(4): p. 461-467.
65. Li, Q.S., et al., A tridecapeptide possesses both antimicrobial and protease-inhibitory activities. Peptides, 2002. 23(1): p. 1-6.
66. McInturff, J.E., et al., Granulysin-derived peptides demonstrate antimicrobial and anti-inflammatory effects against Propionibacterium acnes. Journal of Investigative Dermatology, 2005. 125(2): p. 256-263.
67. Perczel, A., et al., Convex Constraint Analysis - a Natural Deconvolution of Circular-Dichroism Curves of Proteins. Protein Engineering, 1991. 4(6): p. 669-679.
68. Andrade, M.A., et al., Evaluation of Secondary Structure of Proteins from Uv Circular-Dichroism Spectra Using an Unsupervised Learning Neural-Network. Protein Engineering, 1993. 6(4): p. 383-390. |