Synthetic peptides containing a conserved sequence motif of the Id protein family modulate vascular smooth muscle cell phenotype

Bioorganic and Medicinal Chemistry Letters

Volumn 19, Issue 22, 2009, Pages 6298-6302

  Pellegrino, Sara ^a   Ferri, Nicola ^a   Colombo, Noemi ^b   Cremona, Edoardo ^a   Corsini, Alberto ^a   Fanelli, Roberto ^a,b   Gelmi, Maria Luisa ^a   Cabrele, Chiara ^b,c  

^a UNIVERSITY OF MILAN   (Italy)

^b UNIVERSITY OF REGENSBURG   (Germany)

^c RUHR UNIVERSITY BOCHUM   (Germany)

Author keywords

Helix loop helix; Id proteins; Peptide dimerization; Peptide mimic; Protein domain recognition; Smooth muscle cell; Solid phase peptide synthesis

Indexed keywords

ALPHA ACTIN; INHIBITOR OF DIFFERENTIATION PROTEIN; SYNTHETIC PEPTIDE;

ARTICLE; CELL GROWTH; CELL MIGRATION; CELL PROLIFERATION; DOWN REGULATION; NUCLEOTIDE SEQUENCE; PHENOTYPE; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN MOTIF; SMOOTH MUSCLE FIBER; VASCULAR LESION; VASCULAR SMOOTH MUSCLE;

ACTINS; AMINO ACID MOTIFS; AORTA, THORACIC; CALCIUM-BINDING PROTEINS; CELL DIFFERENTIATION; CELL PROLIFERATION; CONSERVED SEQUENCE; ENDOTHELIUM, VASCULAR; INHIBITOR OF DIFFERENTIATION PROTEINS; MUSCLE, SMOOTH, VASCULAR; MYOCYTES, SMOOTH MUSCLE; NUCLEAR PROTEINS; PEPTIDES; PHENOTYPE; PROTEIN BINDING; REPRESSOR PROTEINS;

EID: 71049156752     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2009.09.105     Document Type: Article

References (35)

1. Ross R. N. Eng. J. Med. 340 (1999) 115
2. Hansson G.K., Robertson A.K., and Söderberg-Nauclér C. Annu. Rev. Pathol. 1 (2006) 297
3. Kumar M.S., Hendrix J.A., Johnson A.D., and Owens G.K. Circ. Res. 92 (2003) 840
4. Matsumura M.E., Lobe D.R., and McNamara C.A. J. Biol. Chem. 277 (2002) 7293
5. Neuhold L.A., and Wold B. Cell 74 (1993) 1033
6. O'Toole P.J., Inoue T., Emerson L., Morrison I.E., Mackie A.R., Cherry R.J., and Norton J.D. J. Biol. Chem. 278 (2003) 45770
7. Lasorella A., Uo T., and Iavarone A. Oncogene 20 (2001) 8326
8. Fong S., Debs R.J., and Desprez P.Y. Trends Mol. Med. 10 (2004) 387
9. Henke E., Perk J., Vider J., de Candia P., Chin Y., Solit D.B., Ponomarev V., Cartegni L., Manova K., Rosen N., and Benezra R. Nat. Biotechnol. 26 (2008) 91
10. Ciarapica R., Annibali D., Raimondi L., Savino M., Nasi S., and Rota R. Oncogene 28 (2009) 1881
11. Fairman R., Beran-Steed R.K., Anthony-Cahill S.J., Lear J.D., Stafford III W.F., DeGrado W.F., Benfield P.A., and Brenner S.L. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 10429
12. Kiewitz S.D., and Cabrele C. Biopolymers (Pept. Sci.) 80 (2005) 762
13. Liu J., Shi W., and Warburton D. Biochem. Biophys. Res. Commun. 273 (2000) 1042
14. Svobodova J., and Cabrele C. ChemBioChem 7 (2006) 1164
15. Wibley J., Deed R., Jasiok M., Douglas K., and Norton J. Biochim. Biophys. Acta 1294 (1996) 138
16. Colombo N., and Cabrele C.J. Pept. Sci. 12 (2006) 550
17. Kiewitz S.D., Kakizawa T., Kiso Y., and Cabrele C.J. Pept. Sci. 14 (2008) 1209
18. Fairman R., Beran-Steed R.K., and Handel T.M. Protein Sci. 6 (1997) 175
19. Sauve S., Tremblay L., and Lavigne P. J. Mol. Biol. 342 (2004) 813
20. Chavali G.B., Vijayalakshmi C., and Salunke D.M. Proteins 42 (2001) 471
21. Aggarwal S., Singh P., Topaloglu O., Isaacs J.T., and Denmeade1 S.R. Cancer Res. 66 (2006) 9171
22. Aggarwal S., Janssen S., Wadkins R.M., Harden J.L., and Denmeade1 S.R. Biomaterials 26 (2005) 6077
23. Cwirla S.E., Balasubramanian P., Duffin D.J., Wagstrom C.R., Gates C.M., Singer S.C., Davis A.M., Tansik R.L., Mattheakis L.C., Boytos C.M., Schatz P.J., Baccanari D.P., Wrighton N.C., Barrett R.W., and Dower W.J. Science 276 (1997) 1696
24. Wrighton N.C., Balasubramanian P., Barbone F.P., Kashyap A.K., Farrell F.X., Jolliffe L.K., Barrett R.W., and Dower W.J. Nat. Biotechnol. 15 (1997) 1261
25. Cabrele C., Clerici F., Gandolfi R., Gelmi M.L., Molinari F., and Pellegrino S. Tetrahedron 62 (2006) 3502
26. Caputo F., Clerici F., Gelmi M.L., Pellegrino S., and Pilati T. Tetrahedron: Asymmetry 17 (2006) 61
27. Ferri N., Granata A., Pirola C., Torti F., Pfister P.J., Dorent R., and Corsini A. Mol. Pharmacol. 74 (2008) 144
28. The Cpg-crosslinked peptide constructs were found to be stable in the cell medium containing 10% FCS, as shown by analytical HPLC and MALDI-ToF-MS controls at different times over a period of three days (Fig. S2 of Supplementary data).
29. It might be reasoned that the moderate activity of constructs 2, 3, 3a, and 3b might reflect an unfavorable steric clash between the N,N-linked peptide arms. Further studies are necessary to evaluate the structural properties of the Cpg-containing peptides.
30. Barone M.V., Pepperkok R., Peverali F.A., and Philipson L. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 4985
31. Chaloin L., Vidal P., Heitz A., van Mau N., Mery J., Divita G., and Heitz F. Biochemistry 36 (1997) 11179
32. Lundberg P., Magzoub M., Lindberg M., Hällbrink M., Jarvet J., Eriksson L.E.G., Langel U., and Gräslund A. Biochem. Biophys. Res. Commun. 299 (2002) 85
33. The Id1 HLH domain contains no native tryptophan residues. In order to prepare an analog suitable for fluorescence measurements, we synthesized Id1 HLH peptides containing tryptophan at different positions and evaluated the tolerance of the substitution by comparing the CD spectra of the native and modified sequences (Snyder, A. T. J. Master Thesis, University of Regensburg, Germany, October 2004).
34. Hill A.V. J. Physiol. 40 (1910) iv
35. We additionally recorded the fluorescence titration curve of the W/I-94 Id1 HLH analog with 3a-scr. Contrarily to 3a, 3a-scr gave a point data set characterized by remarkable dispersion a by a slow linear decrease in tryptophan intensity, probably due to unspecific interactions (Fig. S5 of Supplementary data).