A novel artificial loop scaffold for the noncovalent constraint of peptides

Chemistry and Biology

Volumn 7, Issue 7, 2000, Pages 515-527

  Gururaja, Tarikere L ^a   Narasimhamurthy, Shanaiah ^b   Payan, Donald G ^a   Anderson, Dc ^a  

^a RIGEL PHARMACEUTICALS INC   (United States)

^b UNIVERSITY AT BUFFALO   (United States)

Author keywords

Peptide dimerizer; Protein folding; Protein minidomain

Indexed keywords

ANIMALIA; HORDEUM VULGARE SUBSP. VULGARE;

EID: 0033912828     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(00)00137-X     Document Type: Article

References (53)

1. Goodman M., Reisine T.et al. Topochemical design of bioactive peptides and peptidomimetics. Bioorg. Khim. 18:1992;1375-1393.
2. Cunningham B.C., Wells J.A. Minimized proteins. Curr. Opin. Struct. Biol. 7:1997;457-462.
3. Souroujon M.C., Mochly-Rosen D. Peptide modulators of protein-protein interactions in intracellular signaling. Nat. Biotechnol. 16:1998;919-924.
4. Goldberg A.L., Akopian T.N., Kisselev A.F., Lee D.H., Rohrwild M. New insights into the mechanisms and importance of the proteasome in intracellular protein degradation. Biol. Chem. 378:1997;131-140.
5. Hilt W., Wolf D.H. Proteasomes. destruction as a programme Trends. Biochem. Sci. 21:1996;96-102.
6. Lee D.H., Goldberg A.L. Proteasome inhibitors. valuable new tools for cell biologists Trends Cell Biol. 8:1998;397-402.
7. Belich M.P., Trowsdale J. Proteasome and class I antigen processing and presentation. Mol. Biol. Rep. 21:1995;53-56.
8. Meister A. On the discovery of glutathione. Trends Biol. Sci. 13:1988;185-188.
9. Uhlig S., Wendel A. The physiological consequences of glutathione variations. Life Sci. 51:1992;1083-1094.
10. Derman A.I., Prinz W.A., Belin D., Beckwith J. Mutations that allow disulfide bond formation in the cytoplasm of E. coli. Science. 262:1993;1744-1747.
11. Colas P., Cohen B., Jessen T., Grishina I., McCoy J., Brent R. Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2. Nature. 380:1996;548-550.
12. Abedi M., Caponigro G., Kamb A. Green fluorescent protein as a scaffold for intracellular presentation of peptides. Nucleic Acids Res. 26:1998;623-630.
13. Scott C., Abel-Santos E., Wall M., Wahnon D., Benkovic S. Production of cyclic peptides and proteins in vivo. Proc. Natl Acad. Sci. USA. 96:1999;13638-13643.
14. Bodenmuller H., Schilling W., Zachmann B., Schaller H. The neuropeptide head activator loses its biological activity by dimerization. EMBO J. 5:1986;1825-1829.
15. McPhalen C.A., James M.N. Crystal and molecular structure of the serine proteinase inhibitor CI-2. Biochemistry. 26:1987;261-269.
16. Leatherbarrow R.J., Salacinski H.J. Design of a small peptide-based proteinase inhibitor by modeling the active-site region of barley chymotrypsin inhibitor 2. Biochemistry. 30:1991;10717-10721.
17. Struthers M., Cheng R., Imperiali B. Design of a monomeric 23-residue polypeptide with defined tertiary structure. Science. 271:1996;342-345.
18. Braisted A., Wells J. Minimizing a binding domain from protein A. Proc. Natl Acad. Sci. USA. 93:1996;5688-5692.
19. McKnight C., Doering D., Matsudaira P., Kim P. A thermostable 35-residue subdomain within villin headpiece. J. Mol. Biol. 12:1996;126-134.
20. Dahiyat B., Mayo S. De novo protein design. fully automated sequence selection Science. 278:1997;82-87.
21. Spector S., Young P., Raleigh D.P. Native-like structure and stability in a truncation mutant of a protein minidomain. the peripheral subunit-binding domain Biochemistry. 38:1999;4128-4136.
22. Englander S.W., Mayne L., Bai Y., Sosnick T.R. Hydrogen exchange. the modern legacy of Linderstrom-Lang Protein Sci. 6:1997;1101-1109.
23. Woodward C. Advances in protein hydrogen exchange by mass spectrometry. J. Am. Soc. Mass Spectrom. 10:1999;672-674.
24. Chung E.D., Robinson C.et al. Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry. Protein Sci. 6:1997;1316-1324.
25. Smith D.L., Deng Y., Zhang Z. Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry. J. Mass Spectrom. 32:1997;135-146.
26. Bai Y., Milne J., Mayne L., Englander S. Primary structure effects on peptide group hydrogen exchange. Proteins Struct. Funct. Genet. 67:1993;75-86.
27. Gariani T., Leatherbarrow R. Stability of protease inhibitors based on the Bowman-Birk reactive site loop to hydrolysis by proteases. J. Peptide Res. 49:1997;467-475.
28. Bloemendal M., Johnson W.C. Structural information on proteins from circular dichroism spectroscopy possibilities and limitations. Pharm. Biotechnol. 7:1995;65-100.
29. Woody R.W. Circular dichroism. Methods Enzymol. 246:1995;34-71.
30. Greenfield N. Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal. Biochem. 235:1996;1-10.
31. Greenfield N., Fasman G. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry. 8:1969;4108-4116.
32. Perczel A., Hollosi M., Sandor P., Fasman G.D. The evaluation of type I and type II β-turn mixtures. Circular dichroism, NMR and molecular dynamics studies. Int. J. Peptide Prot. Res. 41:1993;223-236.
33. Johnson W.C. Protein secondary structure and circular dichroism. a practical guide Proteins Struct. Funct. Genet. 7:1990;205-214.
34. 1H NMR spectra of proteins via double quantum filtering. Biochem. Biophys. Res. Comm. 117:1983;479-485.
35. HNα for identification of helical secondary structure. J. Mol. Biol. 180:1984;741-751.
36. Gururaja T.L., Levine J.H., Tran D.T., Naganagowda G.A., Ramalingam K., Levine M.J. Candidacidal activity prompted by N-terminus histatin-like domain of human salivary mucin (MUC7). Biochem. Biophys. Acta. 1431:1999;107-119.
37. Brahms S., Brahms J. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138:1980;149-178.
38. Martsev S.P., Vlasov A.P., Arosio P. Distinct stability of recombinant L and H subunits of human ferritin. calorimetric and ANS binding studies Protein Eng. 11:1998;377-381.
39. Vanhoof G., Goossens F., De Meester I., Hendriks D., Scharpe S. Proline motifs in peptides and their biological processing. FASEB J. 9:1995;736-744.
40. Imperiali B., Ottesen J. Design strategies for the construction of independently folded polypeptide motifs. Biopolymers. 47:1998;23-29.
41. Murray M., Niyogi S.et al. Structure-function analysis of a conserved aromatic cluster in the N-terminal domain of human epidermal growth factor. Protein Eng. 11:1998;1041-1050.
42. Javitch J., Ballesteros J., Weinstein H., Chen J. A cluster of aromatic residues in the sixth membrane-spanning segment of the dopamine D2 receptor is accessible in the binding-site crevice. Biochemistry. 37:1998;998-1006.
43. Frank B., Buckley D., McKnight C. Hydrophobic core mutations in the mini-protein HP35: a key phenylalanine specifies the 3D fold. Protein Sci. 7(suppl 1):1998;264S.
44. Fields G., Noble R. Solid phase peptide synthesis utilizing 9-fluorenylmethoxy-carbonyl amino acids. Int. J. Pept. Protein Res. 35:1990;161-214.
45. Hudson D. Methological implications of simultaneous solid-phase peptide synthesis. I. Comparison of different coupling procedures. J. Org. Chem. 53:1988;617-624.
46. Kaiser E., Colescott R., Bossinger C., Cook P. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal. Biochem. 34:1970;595-598.
47. Knorr R., Trazeciak A., Bannworth W. New coupling reagents in peptide chemistry. Tetrahedron Lett. 30:1989;1927-1930.
48. Carpino L.A. 1-Hydroxy-7-azabenzotriazole. An efficient peptide coupling additive. J. Am. Chem. Soc. 115:1993;4397-4398.
49. Zhang L. Epton R. Innovation and perspectives in solid phase synthesis. 3rd International Symposium. 1994;711 Mayflower Scientific Ltd, Birmingham.
50. Wade J., Bedford J., Sheppard R., Tregear G. DBU as an N alpha-deprotecting reagent for the fluorenylmethoxycarbonyl group in continuous flow solid-phase peptide synthesis. Peptide Res. 4:1991;194-199.
51. Castro B., Dormoy J.R., Evin G., Selve C. Peptide coupling reagents. N-[Oxytris(dimethylamino)phosphonium]benzotriazole hexafluorophosphate. Tetrahedron Lett. 14:1975;1219-1222.
52. Gururaja T.L., Levine M.J. Solid-phase synthesis and characterization of human salivary statherin. a tyrosine-rich phosphoprotein inhibitor of calcium phosphate precipitation Peptide Res. 9:1996;283-289.
53. Bohm G., Muhr R., Jaenicke R. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 5:1992;191-195.