The conformation of peptide thymosin α1 in solution and in a membrane- like environment by circular dichroism and NMR spectroscopy. A possible model for its interaction with the lymphocyte membrane

Peptides

Volumn 19, Issue 10, 1998, Pages 1731-1738

  Grottesi, Alessandro ^a   Sette, Marco ^a   Palamara, Anna Teresa ^a   Rotilio, Giuseppe ^a   Garaci, Enrico ^a   Paci, Maurizio ^a  

^a UNIVERSITY OF ROME TOR VERGATA   (Italy)

Author keywords

Circular dichroism; Immunogenic peptide; Lymphocytes; NMR; Thymosin 1

Indexed keywords

THYMOSIN; THYMOSIN ALPHA1;

ARTICLE; CELL DIFFERENTIATION; CELL MEMBRANE; CIRCULAR DICHROISM; LYMPHOCYTE PROLIFERATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE ANALYSIS; PRIORITY JOURNAL; THYMUS;

ADJUVANTS, IMMUNOLOGIC; CELL MEMBRANE; CIRCULAR DICHROISM; LYMPHOCYTES; MEMBRANES, ARTIFICIAL; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; THYMOSIN;

EID: 0032435181     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0196-9781(98)00132-6     Document Type: Article

References (31)

1. Bax, A.; Davis, D. G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:355-360; 1985.
2. Brandhuber, B. J.; Boone, T.; Kenney, W. C.; McKay, D. B. Three-dimensional structure of IL-2. Science. 238:1707-1709; 1987.
3. Braunschweiler, L.; Ernst, R. R. Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53:521-528; 1983.
4. Chupin, V.; Killian, J. A.; Breg, J.; de Jongh, H. H. J.; Boelens, R.; Kaptein, R.; de Kruijff, B. PHOE signal peptide inserts into micelles as a dynamic helix-break-helix structure which is modulated by the environment. A two-dimensional NMR study. Biochemistry. 34:11617-11624; 1995.
5. Curtis Johnson, Jr., W. Protein secondary structure and circular dichroism: a practical guide. Proteins: structure, functions, and genetics. 7:205-214; 1990.
6. Goldstein, A. L.; Low, T. L. K.; Thurman, G. B.; Zatz, M. M.; Hall, N.; Chen, C. P.; Hu, S. K.; Naylor, P. H.; McClure, J. E. Current status of thymosin and other hormones of the thymus gland. Recent Progr. Horm. Res. 37:369-415; 1981.
7. Gomez-Marquez, J.; Segade, F.; Dosil, M.; Pichel, J. G.; Bustelo, X. R.; Freire, M. The expression of prothymosin α gene in T lymphocytes and leukemic lymphoid cells is tied to lymphocyte proliferation. J. Biol. Chem. 264:8451-8455; 1989.
8. Gravenstein, S. Augmentation of influenza antibody response in elderly men by thymosin α 1: a double-blind placebo-controlled clinical study. J. Am. Geriatrics Soc. 1:1-8; 1989.
9. Jen, T. Y.; Chuen-shang, C. W.; Martinez, H. M. Calculation of protein conformation from CD. Methods in enzimology. 130:208-269; 1986.
10. Jeener, J.; Meier, B. H.; Bachmann, P.; Ernst, R. R. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71:4546-4553; 1979.
11. Ju, G. L.; Collins, K. L.; Kaffka, W-H.; Tsien, R.; Chizzonite, R.; Crowl, R.; Batt, P.; Kilian, L. Structure function analysis of human interleukin-2 (IL-2), J. Biol. Chem. 262:5723-5731; 1987.
12. Leichtling, K. D.; Serrate, S. A.; Sztein, M. B. Thymosin α1 modulates the expression of high-affinity IL-2 receptor on normal human lymphocytes. Int. J. Immunopharmacol. 1:19-29; 1990.
13. Li, S. C.; Deber, C. M. Peptide environment specifies conformation helicity of hydrophobic segments compared in aqueous, organic, and membrane environment. J. Biol. Chem. 268:22975-22978; 1993.
14. Macquarie, F.; Baleux, F.; Huynh-Dinh, T.; Rouge, D.; Neumann J.-M.; Sanson, A. Proton NMR conformational study of an Annexin I fragment: influence of a phospholipidic micellar environment. Biochemistry. 32:7244-7254; 1993.
15. Manrow, R. E.; Sburlati, A. R.; Hanover, J. A.; Berger, S. L. Nuclear targeting of prothymosin. J. Biol. Chem. 266:3916-3924; 1991.
16. 1H spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 113:967-974; 1983.
17. Mastino, A.; Favalli, C.; Grelli, S; Innocenti, F.; Garaci, E. Thymosina α1 potentiates interleukin 2-induced cytotoxic activity in mice. Cellular Immunology. 133:196-205; 1991.
18. Mutchnick, M. G.; Appelman, H. D.; Chung, H. T.; Aragona, E.; Gupta, T. P.; Cummings, G. D.; Waggoner, J. G.; Hoofnagle, J. H.; Shafritz, D. A. Treatment of chronic hepatitis B: a placebo-controlled pilot trial. Hepatology. 14:409-415; 1991.
19. Naylor, P. H.; Low, T. L. K.; Goldstein, A. L. The thymus-AIDS connection: thymosin in the diagnosis and treatment of individuals at high risk for AIDS. Bioassays 1. 63:80-87; 1984.
20. Rizo, J.; Blanco, F. J.; Kobe, B.; Bruch, M. D.; Gierash, L. M. Conformation behavior of Escherichia coli OmpA signal peptide in membrane mimetic environments. Biochemistry. 32:4881-4894; 1993.
21. Rajan, R.; Balaram, P. A model for interaction of trifluoroethanol with peptides and proteins. Int. J. Peptide Protein Res. 48:328-336; 1996.
22. Roise, D.; Horwath, S. J.; Tomich, J. M.; Richards, J. H.; Schatz, G. A chemically synthesized pre-sequence of an imported mitocondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers. The EMBO J. 6:1327-1334; 1986.
23. Sargent, D. F.; Shwyzer, R. Membrane lipid phase as catalyst for peptide-receptor interactions. Proc. Nat. Soc. Sci. USA. 83:5774-5778; 1988.
24. Shen, S. Y. Effect of thymosin α 1 on Heptavax B among hemodialysis patients. Kidney Int. 31:217-223; 1987.
25. Schulof, R. S.; Goldstein, A. L. Clinical applications of thymosin and other thymic hormones. Rec. Adv. Clin. Immun. 3:243-286; 1983.
26. Shiau, A. L.; Wu, C. L.; Huang, K. Y. The effect of thymosin on experimental herpes simplex virus infections. J. Formosan Med. Assn. 87:34-41; 1988.
27. Szabo, P.; Weksler, M. E. Is thymosin α1 a thymic hormone? Clinical Immun. and Immunopathology. 65:195-200; 1992.
28. Toniolo, C.; Bonora, G. M.; Heimer, E. P.; Felix, A. M. Structure, solubility, and reactivity of peptides. Int. J. of Biol. Macromol. 30:232-239; 1987.
29. Wang, Z.; Jones, D. J.; Rizo, J.; Gierash, L. M. Membranebound conformation of a signal peptide: a transferred nuclear Overhauser effect analysis. Biochemistry. 32:13991-13999; 1993.
30. Waldmann, T. A. The multisubunit IL-2 receptor. Ann. Rev. of Biochemistry. 58:875-911; 1989.
31. White, A.; Goldstein, A. L. The endocrine role of the thymus and its hormone thymosin in the regulation of the growth and maturation of host immunological competence. Adv. Metab. Dis. 8:359-374; 1975.