PEGylation of melittin: Structural characterization and hemostatic effects

Journal of Bioactive and Compatible Polymers

Volumn 25, Issue 1, 2010, Pages 75-97

  Peng, Henry T ^a   Huang Huang, ^a   Shek, Pang N ^a   Charbonneau, Sophie ^b   Blostein, Mark D ^b  

^a DEFENCE RESEARCH AND DEVELOPMENT CANADA   (Canada)

^b MCGILL UNIVERSITY   (Canada)

Author keywords

Bioconjugation.; Blood coagulation; Hemolysis; Melittin; PEGylation

Indexed keywords

BICINCHONINIC ACIDS; BIO-CONJUGATION; BIOMEDICAL APPLICATIONS; BLOOD COAGULATION; CIRCULAR DICHROISM; FTIR; HELICITIES; MALDI-MS; MELITTIN; N-HYDROXYSUCCINIMIDE; PEGYLATION; REACTION CONDITIONS; STRUCTURAL CHARACTERIZATION;

BLOOD; COAGULATION; DICHROISM; ESTERS; ETHYLENE; ETHYLENE GLYCOL; FOURIER TRANSFORM INFRARED SPECTROSCOPY; PEPTIDES; POLYETHYLENE OXIDES;

POLYETHYLENE GLYCOLS;

DIMETHYL SULFOXIDE; MACROGOL; MELITTIN; N HYDROXYSUCCINIMIDE;

ARTICLE; BIOMEDICINE; CIRCULAR DICHROISM; CONTROLLED STUDY; FOURIER TRANSFORMATION; HEMOSTASIS; HUMAN; HUMAN CELL; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE; THROMBOELASTOGRAPHY;

EID: 76149136924     PISSN: 08839115     EISSN: 15308030     Source Type: Journal    
DOI: 10.1177/0883911509354230     Document Type: Article

References (64)

1. Gauldie, J., Hanson, J.M., Rumjanek, F.D., Shipolini, R.A. and Vernon, C.A. (1976). The Peptide Components of Bee Venom, Eur. J. Biochem., 61: 369-376.
2. Terwilliger, T.C. and Eisenberg, D. (1982). The Structure of Melittin II. Interpretation of the Structure, J. Biol. Chem., 257: 6016-6022.
3. Bazzo, R., Tappin, M.J., Pastore, A., Harvey, T.S., Carver, J.A. and Campbell, I.D. (1998). The Structure of Melittin A 1H-NMR Study in Methanol, Eur. J. Biochem., 173: 139-146.
4. Weaver, A.J., Kemple, M.D. and Prendergast, F.G. (1989). Characterization of Selectively 13C-labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy, Biochemistry, 28: 8614-8623.
5. Bello, J., Bello, H.R. and Grandados, E. (1982). Conformation and Aggregation of Melittin: Dependence on pH and Concentration, Biochemistry, 2: 461-465.
6. Terra, R.M.S., Guimar£es, J.A. and Verli, H. (2007). Structural and Functional Behavior of Biologically Active Monomeric Melittin, J. Mol. Graph. Model, 25: 767-772.
7. Asthana, N., Yadav, S.P. and Ghosh, J.K. (2004). Dissection of Antibacterial and Toxic Activity of Melittin, J. Biol. Chem., 279: 55042-55050.
8. Park, H.J., Son, D.J., Lee, C.W., Choi, M.S., Lee, U.S., Song, H.S. et al. (2007). Melittin Inhibits Inflammatory Target Gene Expression and Mediator Generation via Interaction with Iκb Kinase, Biochem. Pharmacol., 73: 237-247.
9. Boeckle, S., Fahrmeir, J., Roedl, W., Ogris, M. and Wagner, E. (2006). Melittin Analogs with High Lytic Activity at Endosomal pH Enhance Transfection with Purified Targeted PEI Polyplexes, J. Control. Rel., 112: 240-248.
10. Cui, F., Cun, D., Tao, A., Yang, M., Shi, K., Zhao, M. et al. (2005). Preparation and Characterization of Melittin-loaded Poly(DL-lactic acid) or Poly(DL-lactic-co-glycolic acid) Microspheres Made by the Double Emulsion Method, J. Control. Rel., 107: 310-319.
11. Holle, L., Song, W., Holle, E., Wei, Y.-Z., Wagner, T. and Yu, X.-Z. (2003). A Matrix Metalloproteinase 2 Cleavable Melittin/Advidin Conjugate Specifically Targets Tumor Cells In Vitro and In Vivo, Int. J. Oncol., 22: 93-98.
12. Yalcin, M., Ak, F. and Erturk, M. (2006). The Role of the Central Thromboxane A2 in Cardiovascular Effects of a Phospholipase A2 Activator Melittin Administrated Intracerebroventricularly in Normotensive Conscious Rats, Neuropeptides, 40: 207-212.
13. Morgan, N.G., Rumford, G.M. and Montague, W. (1985). Studies on the Mechanism by which Melittin Stimulates Insulin Secretion from Isolated Rate Islets of Langerhans, Biochim. Biophys. Acta, 845: 525-532.
14. Zhao, Z., Rolli, H. and Schneider, C.H. (1995). Immunogenicity of Dinitrocarboxyphenylated Melittin: The Influence of C-Terminal Chain Shortening, N-Terminal Substitution and Prolin Insertion at Positions 5 and 10, J. Pept. Sci., 1: 140-148.
15. Hider, R.C., Khader, F. and Tatham, A.S. (1983). Lytic Activity of Monomeric and Oligomeric Melittin, Biochim. Biophys. Acta, 728: 206-214.
16. Ramalingam, K., Aimoto, S. and Bello, J. (1992). Conformational Studies of Anionic Melittin Analogues: Effect of Peptide Concentration, pH, Ionic Strength, and Temperature-Models for Protein Folding and Halophilic Proteins, Biopolymers, 32: 981-992.
17. Lavignac, N., Lazenby, M., Franchini, J., Ferruti, P. and Duncan, R. (2005). Synthesis and Preliminary Evaluation of Poly(Amidoamine)-Melittin Conjugates as Endosomolytic Polymers and/or Potential Anticancer Therapeutics, Int. J. Pharm., 300: 102-112.
18. Legendre, J.Y., Trzeciak, A., Bohrmann, B., Deuschle, U., Kitas, E. and Supersaxo, A. (1997). Dioleoylmelittin as a Novel Serum-Insensitive Reagent for Efficient Transfection of Mammalian Cells, Bioconjug. Chem., 8: 57-63.
19. Asthana, N., Yadav, S.P. and Ghosh, J.K. (2004). Dissection of Antibacterial and Toxic Activity of Melittin, J. Biol. Chem., 279: 55042-55050.
20. Sun, X., Chen, S., Li, S., Yan, H., Fan, Y. and Mi, H. (2005). Deletion of Two C-Terminal Gln Residues of 12-26-Residue Fragment of Melittin Improves its Antimicrobial Activity, Peptides, 26: 369-375.
21. Ahmad, A., Yadav, S.P., Asthana, N., Mitra, K., Srivastava, S.P. and Ghosh, J.K. (2006). Utilization of an Amphipathic Leucine Zipper Sequence to Design Antibacterial Peptides with Simultaneous Modulation of Toxic Activity against Human Red Blood Cells, J. Biol. Chem., 281: 22029-22038.
22. Harris, J.M. and Chess, R.B. (2003). Effect of Pegylation on Pharmaceuticals, Nat. Rev. Drug Discov., 2: 214-221.
23. Veronese, F.M. and Pasut, G. (2005). PEGylation, Successful Approach to Drug Delivery, Drug Discov. Today, 10: 1451-1458.
24. Vandermeulen, G.W.M., Hinderberger, D., Xu, H., Sheiko, S.S., Jeschke, G. and Klok, H.-A. (2004). Structure and Dynamics of Self-Assembled Poly(Ethylene Glycol) Based Coiled-Coil Nano-Objects, ChemPhysChem., 5: 488-494.
25. Lih, E., Joung, Y.K., Bae, J.W. and Park, K.D. (2008). An In Situ Gel-Forming Heparin-Conjugated PLGA-PEG-PLGA Copolymer, J. Bioact. Compat. Polym., 23: 444-457.
26. Sanborn, T.J., Messersmith, P.B. and Barron, A.E. (2002). In Situ Crosslinking of a Biomimetic Peptide-PEG Hydrogel via Thermally Triggered Activation of Factor XIII, Biomaterials, 23: 2703-2710.
27. Fichter, K.M., Zhang, L., Kiick, K.L. and Reineke, T.M. (2008). Peptide-Functionalized Poly(Ethylene Glycol) Star Polymers: DNA Delivery Vehicles with Multivalent Molecular Architecture, Bioconjug. Chem., 19: 76-88.
28. Schmieder, A.H., Grabski, L.E., Moore, N.M., Dempsey, L.A. and Sakiyama-Elbert, S.E. (2007). Development of Novel Poly(Ethylene Glycol)-based Vehicles for Gene Delivery, Biotechnol. Bioeng., 96: 967-976.
29. Schiavon, O., Pasut, G., Moro, S., Orsolini, P., Guiotto, A. and Veronese, F.M. (2004). PEG-Ara-C Conjugates for Controlled Release, Eur. J. Med. Chem., 39: 123-133.
30. Mero, A., Schivavon, O., Pasut, G., Veronese, F.M., Emilitri, E. and Ferruti, P. (2009). A Biodegradable Polymeric Carrier Based on PEG for Drug Delivery, J. Bioact. Compat. Polym., 24: 220-234.
31. Blostein, M.D., Rigby, A.C., Furie, B., Furie, B.C. and Gilbert, G.G. (2000). Amphipathic Helices Support Function of Blood Coagulation Factor IXa, Biochemistry, 39: 12000-12006.
32. Stief, T.W. (2007). Thrombin Generation by Hemolysis, Blood Coagul. Fibrinolysis, 18: 61-66.
33. Triantaphyllopoulos, E. (1970). Hemolysis and Blood Coagulation: Evidence of Inhibitory Effects, Life Sci., 7, part II: 99-110.
34. Woolfson, D.N. and Ryadnov, M.G. (2006). Peptide-Based Fibrous Biomaterials: Some Things Old, New and Borrowed, Curr. Opin. Chem. Biol., 10: 559-567.
35. Klok, H.-A. (2005). Biological-Synthetic Hybrid Block Copolymers: Combining the Best from Two Worlds, J. Polym. Sci., 43: 1-17.
36. Ellis-Behnke, R.G., Liang, Y.-X., Tay, D.K.C., Kau, P.W.F., Schneider, G.E., Zhang, S. et al. (2006). Nano Hemostat Solution: Immediate Hemostasis at the Nanoscale, Nanomed: Nanotech. Biol. Med., 2: 207-215.
37. Chowdhury, S.P., Doleman, M. and Johnston, D. (1995). Fingerprinting Proteins Coupled with Polymers by Mass Spectrometry: Investigation of Polyethylene Glycol-Conjugate Superoxide Dismutase, J. Am. Soc. Mass Spectrom., 6: 478-487.
38. Na, D.H., Youn, Y.S. and Lee, K.C. (2003). Optimization of the Pegylation Process of a Peptide by Monitoring with Matrix-assisted Laser Desorption/ Ionization Time-Of-Flight Mass Spectrometry, Rapid Commun. Mass Spectrom., 17: 2241-2244.
39. Lauterwein, J., Brown, L.R. and Wüthrich, K. (1980). High-Resolution 1H-NMR Studies of Monomeric Melittin in Aqueous Solution, Biochim. Biophys. Acta, 622: 219-230.
40. Digilio, G., Barbero, L., Bracco, C., Corpillo, D., Esposito, P., Piquet, G. et al. (2003). NMR Structure of Two Novel Polyethylene Glycol Conjugates of the Human Growth Hormone-Releasing Factor, Hgrf(1-29)-NH2, J. Am. Chem. Soc., 125: 3458-3470.
41. Belcheva, N., Baldwin, S.P. and Saltzman, W.M. (1998). Synthesis and Characterization of Polymer-(Multi)-Peptide Conjugates for Control of Specific Cell Aggregation, J. Biomater. Sci. Polym. End., 9: 207-226.
42. Zhang, L., Furst, E.M. and Kiick, K.L. (2006). Manipulation of Hydrogel Assembly and Growth Factor Delivery via the Use of Peptide-Polysaccharide Interactions, J. Control. Rel., 114: 130-142.
43. Okada, A., Wakamatsu, K., Miyazawa, T. and Higashijima, T. (1994). Vesicle-Bound Conformation of Melittin: Transferred Nuclear Overhauser Enhancement Analysis in the Presence of Perdeuterated Phosphatidylcholine Vesicles, Biochemistry, 33: 9438-9446.
44. Vig, S., Chitolie, A., Bevan, D., Haliday, A. and Dormandy, J. (2001). Thromboelastography: A Reliable Test? Blood Coagul. Fibrinolysis, 12: 555-561.
45. Zhao, H., Rubio, B., Sapra, P., Wu, D., Reddy, P., Sai, P. et al. (2008). Novel Prodrugs of SN38 Using Multiarm Poly(Ethylene Glycol) Linkers, Bioconjug. Chem., 19: 849-859.
46. Yu, H., Feng, Z.-G., Zhang, A.-Y., Sun, L.-G. and Qian, L. (2006). Synthesis and Characterization of Three-Dimensional Crosslinked Networks Based on Self-Assembly of ±-Cyclodextrins with Thiolated 4-Arm PEG Using a Three-Step Oxidation, Soft Matter, 2: 343-349.
47. Wallace, D.G., Cruise, G.M., Rhee, W.M., Schroeder, J.A., Prior, J.J., Ju, J. et al. (2001). A Tissue Sealant Based on Reactive Multifunctional Polyethylene Glycol, J. Biomed. Mater. Res., 58: 545-555.
48. Seal, B.L. and Panitch, A. (2006). Physical Matrices Stabilized by Enzymatically Sensitive Covalent Crosslinks, Acta Biomater., 2: 241-251.
49. Xu, H., Kaar, J.L., Russell, A.J. and Wagner, W.R. (2006). Characterizing the Modification of Surface Proteins with Poly(Ethylene Glycol) to Interrupt Platelet Adhesion, Biomaterials, 27: 3125-3135.
50. Na, D.H., Youn, Y.S. and Lee, K.C. (2003). Optimization of the Pegylation Process of a Peptide by Monitoring with Matrix-Assisted Laser Desorption/ Ionization Time-Of-Flight Mass Spectrometry, Rapid Commun. Mass Spectrom., 17: 2241-2244.
51. Larson, R.S., Menard, V., Jacobs, H. and Kim, S.W. (2001). Physicochemical Characterization of Poly(Ethylene Glycol)-Modified Anti-GAD Antibodies, Bioconjug. Chem., 12: 861-869.
52. Barker, T.H., Fuller, G.M., Klinger, M.M., Feldman, D.S. and Hagood, J.S. (2001). Modification of Fibrinogen with Poly(Ethylene Glycol) and its Effects on Fibrin Clot Characteristics, J. Biomed. Mater. Res., 56: 529-535.
53. Ramalingam, K., Bello, J. and Aimoto, S. (1993). Permethylation Alters the Conformational Transitions and the Complexing Ability of Melittin: A Model for Methylated Proteins, Biopolymers, 33: 305-314.
54. Sumbatyan, N.V., Mandrugin, V.A., Deroussent, A., Bertrand, J.R., Majer, Z., Malvy, C. et al. (2004). The Solution Synthesis of Antisense Oligonucleotide-Peptide Conjugates Directly Linked via Phosphoramide Bond by Using a Fragment Coupling Approach, Nucleos. Nucleot. Nucleic Acids, 23: 1911-1927.
55. Kinstler, O.B., Brems, D.N., Lauren, S.L., Paige, A.G., Hamburger, J.B. and Treuheit, M.J. (1996). Characterization and Stability of N-terminally PEGylated rhG-CSF, Pharm. Res., 13: 996-1002.
56. Maulet, Y., Mathey-Prevot, B., Kaiser, G., Rüegg, U.T. and Fulpius, B.W. (1980). Purification and Chemical Characterization of Melittin and Acetylated Derivatives, Biochim. Biophys. Acta, 625: 274-280.
57. Morpurgo, M. and Veronese, F.M. (2004). Conjugates of Peptide and Proteins to Polyethylene Glycol, Methods Mol. Biol., 283: 45-70.
58. Goto, Y. and Hagihara, Y. (1992). Mechanism of the Conformational Transition of Melittin, Biochemistry, 31: 732-738.
59. Kemple, M.D., Buckley, P., Yuan, P. and Prendergast, F.G. (1997). Main Chain and Side Chain Dynamics of Peptides in Liquid Solution from 13C NMR: Melittin as a Model Peptide, Biochemistry, 36: 1678-1688.
60. Stigsnaes, P., Frokjaer, S., Bjerregaard, S., van de Weert, M., Kingshott, P. and Moeller, E.H. (2007). Characterisation and Physical Stability of PEGylated Glucagon, Int. J. Pharm., 330: 89-98.
61. Ius, A., Bacigalupo, M.A., Longhi, R. and Meroni, G. (2000). Selectively Conjugated Melittins for Liposome Time-Resolved Fluoroinnumoassay of Theophylline in Serum, Fresenius J. Anal. Chem., 366: 869-872.
62. Werkmeister, J.A., Hewish, D.R., Kirkpatrick, A. and Rivett, D.E. (2002). Sequence Requirements for the Activity of Membrane-active Peptides, J. Pept Res., 60: 232-238.
63. Blondelle, S.E. and Houghten, R.A. (1991). Hemolytic and Antimicrobial Activities of the Twenty-Four Individual Omission Analogues of Melittin, Biochemistry, 30: 4671-4678.
64. Lin, S.C., Huang, T.F. and Ouyang, C. (1983). Characterization of the Purified Anticoagulant Principles from Apis Mellifera (Honey Bee) Venom, J. Formos. Med. Assoc., 82: 629-639.