Interaction of recombinant analogs of spider silk proteins 1F9 and 2E12 with phospholipid membranes

Biochimica et Biophysica Acta - Biomembranes

Volumn 1798, Issue 6, 2010, Pages 1172-1178

  Antonenko, Yuri N ^a   Perevoshchikova, Irina V ^a   Davydova, Lyubov I ^b   Agapov, Igor A ^c   Bogush, Vladimir G ^b  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b STATE RESEARCH INSTITUTE OF GENETICS AND SELECTION OF INDUSTRIAL MICROORGANISMS   (Russian Federation)

^c SHUMAKOV NATIONAL MEDICAL RESEARCH CENTER OF TRANSPLANTOLOGY AND ARTIFICIAL ORGANS   (Russian Federation)

Author keywords

Aggregation; Bilayer lipid membrane; Biomaterial; Circular dichroism; FCS; Fusion; Leakage; Liposome; Protein structure; Spidroin

Indexed keywords

ALANINE; CALCIUM; GLYCINE; LIPOSOME; PHOSPHATIDYLSERINE; PROLINE; RHODAMINE; SILK FIBROIN; SPIDROIN 1; SPIDROIN 2; UNCLASSIFIED DRUG;

ACIDITY; ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE CORRELATION SPECTROSCOPY; HYDROPHOBICITY; LIPID VESICLE; MEMBRANE BINDING; PHOSPHOLIPID MEMBRANE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT;

ANIMALS; CALCIUM; LIPOSOMES; PHOSPHOLIPIDS; PROTEIN STRUCTURE, SECONDARY; SILK; SPIDERS;

ARANEAE;

EID: 77952543591     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.03.006     Document Type: Article

References (43)

1. Altman G.H., Diaz F., Jakuba C., Calabro T., Horan R.L., Chen J., Lu H., Richmond J., Kaplan D.L. Silk-based biomaterials. Biomaterials 2003, 24:401-416.
2. Scheibel T. Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins. Microb. Cell Fact. 2004, 3:14.
3. Kluge J.A., Rabotyagova O., Leisk G.G., Kaplan D.L. Spider silks and their applications. Trends Biotechnol. 2008, 26:244-251.
4. Guerette P.A., Ginzinger D.G., Weber B.H., Gosline J.M. Silk properties determined by gland-specific expression of a spider fibroin gene family. Science 1996, 272:112-115.
5. Romer L., Scheibel T. The elaborate structure of spider silk: structure and function of a natural high performance fiber. Prion 2008, 2:154-161.
6. Vepari C., Kaplan D.L. Silk as a Biomaterial. Prog. Polym. Sci. 2007, 32:991-1007.
7. Agapov I.I., Pustovalova O.L., Moisenovich M.M., Bogush V.G., Sokolova O.S., Sevastyanov V.I., Debabov V.G., Kirpichnikov M.P. Three-dimensional scaffold made from recombinant spider Silk protein for tissue engineering. Dokl. Biochem. Biophys. 2009, 426:127-130.
8. Min B.M., Jeong L., Nam Y.S., Kim J.M., Kim J.Y., Park W.H. Formation of silk fibroin matrices with different texture and its cellular response to normal human keratinocytes. Int. J. Biol. Macromol. 2004, 34:281-288.
9. Gellynck K., Verdonk P.C., Van Nimmen E., Almqvist K.F., Gheysens T., Schoukens G., Van Langenhove L., Kiekens P., Mertens J., Verbruggen G. Silkworm and spider silk scaffolds for chondrocyte support. J. Mater. Sci. Mater. Med. 2008, 19:3399-3409.
10. Wang X., Wenk E., Matsumoto A., Meinel L., Li C., Kaplan D.L. Silk microspheres for encapsulation and controlled release. J. Control. Release 2007, 117:360-370.
11. Kluge J.A., Rabotyagova O., Leisk G.G., Kaplan D.L. Spider silks and their applications. Trends Biotechnol. 2008, 26:244-251.
12. Bogush V.G., Sokolova O.S., Davydova L.I., Klinov D.V., Sidoruk K.V., Esipova N.G., Neretina T.V., Orchanskyi I.A., Makeev V.Y., Tumanyan V.G., Shaitan K.V., Debabov V.G., Kirpichnikov M.P. A novel model system for design of biomaterials based on recombinant analogs of spider silk proteins. J. Neuroimmune Pharmacol. 2009, 4:17-27.
13. Piruzian E.S., Bogush V.G., Sidoruk K.V., Goldenkova I.V., Musiichuk K.A., Debabov V.G. Construction of the synthetic genes for protein analogs of spider silk carcass spidroin 1 and their expression in tobacco plants. Mol. Biol. (Mosk) 2003, 37:654-662.
14. Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157:105-132.
15. Meidleman S.L. Phospholipids Handbook 1993, 23-38. Marcel Dekker, New York. G. Cevc (Ed.).
16. Bogush V.G., Sazykin A.Y., Davydova L.I., Martirosyan V.V., Sidoruk K.V., Glazunov A.V., Akishina R.I., Shmatchenkov A., Debabov V.G. Obtaining, purification and silking of recombinant analog of spidroin 1. Biotechnologiya (Russian) 2006, 4(1):3-12.
17. Mao D., Wallace B.A. Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles. Biochemistry 1984, 23:2667-2673.
18. Hoekstra D., de Boer T., Klappe K., Wilschut J. Fluorescence method for measuring the kinetics of fusion between biological membranes. Biochemistry 1984, 23:5675-5681.
19. Zakharov S.D., Hulleman J.D., Dutseva E.A., Antonenko Y.N., Rochet J.C., Cramer W.A. Helical alpha-synuclein forms highly conductive ion channels. Biochemistry 2007, 46:14369-14379.
20. Magde D., Elson E.L., Webb W.W. Fluorescence correlation spectroscopy. II. An experimental realization. Biopolymers 1974, 13:29-61.
21. Rigler R., Mets U., Widengren J., Kask P. Fluorescence correlation spectroscopy with high count rate and low background: analysis of translational diffusion. Eur. Biophys. J. 1993, 22(2):169-175.
22. Rusu L., Gambhir A., Mclaughlin S., Radler J. Fluorescence correlation spectroscopy studies of peptide and protein binding to phospholipid vesicles. Biophys. J. 2004, 87:1044-1053.
23. Mueller P., Rudin D.O., Tien H.T., Wescott W.C. Methods for the formation of single bimolecular lipid membranes in aqueous solution. J. Phys. Chem. 1963, 67:534-535.
24. van der Bogaart G., Kusters I., Velasquez J., Mika J.T., Krasnikov V., Driessen A.J., Poolman B. Dual-color fluorescence-burst analysis to study pore formation and protein-protein interactions. Methods 2008, 46:123-130.
25. Nomikos M., Mulgrew-Nesbitt A., Pallavi P., Mihalyne G., Zaitseva I., Swann K., Lai F.A., Murray D., Mclaughlin S. Binding of phosphoinositide-specific phospholipase C-zeta (PLC-zeta) to phospholipid membranes: potential role of an unstructured cluster of basic residues. J Biol. Chem. 2007, 282:16644-16653.
26. Matsuzaki K., Harada M., Handa T., Funakoshi S., Fujii N., Yajima H., Miyajima K. Magainin 1-induced leakage of entrapped calcein out of negatively-charged lipid vesicles. Biochim. Biophys. Acta 1989, 981:130-134.
27. Zakharov S.D., Cramer W.A. Insertion intermediates of pore-forming colicins in membrane two-dimensional space. Biochimie 2002, 84:465-475.
28. Nagarajan S., Ramalingam K., Neelakanta R.P., Cereghetti D.M., Padma Malar E.J., Rajadas J. Lipid-induced conformational transition of the amyloid core fragment Abeta(28-35) and its A30G and A30I mutants. FEBS J. 2008, 275:2415-2427.
29. Gad A.E., Silver B.L., Eytan G.D. Polycation-induced fusion of negatively-charged vesicles. Biochim. Biophys. Acta 1982, 690:124-132.
30. Matsuzaki K. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta 1999, 1462:1-10.
31. Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1999, 1462:55-70.
32. Rhoades E., Ramlall T.F., Webb W.W., Eliezer D. Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy. Biophys. J. 2006, 90:4692-4700.
33. Krylova O.O., Melik-Nubarov N.S., Badun G.A., Ksenofontov A.L., Menger F.M., Yaroslavov A.A. Pluronic L61 accelerates flip-flop and transbilayer doxorubicin permeation. Chemistry 2003, 9:3930-3936.
34. Kabanov A.V., Vinogradov S.V. Nanogels as pharmaceutical carriers: finite networks of infinite capabilities. Angew. Chem. Int. Ed. Engl. 2009, 5418-5429.
35. Kabanov A.V., Okano T. Challenges in polymer therapeutics: state of the art and prospects of polymer drugs. Adv. Exp. Med. Biol. 2003, 519:1-27.
36. Epand R.M. Lipid polymorphism and protein-lipid interactions. Biochim. Biophys. Acta 1998, 1376:353-368.
37. Subramanian M., Jutila A., Kinnunen P.K. Binding and dissociation of cytochrome c to and from membranes containing acidic phospholipids. Biochemistry 1998, 37:1394-1402.
38. Arnold K., Hoekstra D., Ohki S. Association of lysozyme to phospholipid surfaces and vesicle fusion. Biochim. Biophys. Acta 1992, 1124:88-94.
39. Vechetti G.F., de Arcuri B.F., Posse E., Arrondo J.L., Morero R.D. Aggregation, fusion and aqueous content release from liposomes induced by lysozyme derivatives: effect on the lytic activity. Mol. Membr. Biol. 1997, 14:137-142.
40. Gorbenko G.P., Ioffe V.M., Kinnunen P.K. Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane association. Biophys. J. 2007, 93:140-153.
41. Menestrina G., Dalla S.M., Comai M., Coraiola M., Viero G., Werner S., Colin D.A., Monteil H., Prevost G. Ion channels and bacterial infection: the case of beta-barrel pore-forming protein toxins of Staphylococcus aureus. FEBS Lett. 2003, 552:54-60.
42. Andreeva-Kovalevskaya Z., Solonin A.S., Sineva E.V., Ternovsky V.I. Pore-forming proteins and adaptation of living organisms to environmental conditions. Biochemistry (Mosc.) 2008, 73:1473-1492.
43. van den Brink-van der Laan, Killian J.A., de Kruijff B. Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile. Biochim. Biophys. Acta 2004, 1666:275-288.