Identification of cyclized calmodulin antagonists from a phage display random peptide library

Molecular Diversity

Volumn 1, Issue 4, 1996, Pages 259-265

  Pierce, Heather Hanson ^a   Adey, Nils ^b   Kay, Brian K ^a  

^a UNIVERSITY OF NORTH CAROLINA   (United States)

^b Myriad Genetics Laboratories Inc   (United States)

Author keywords

Alanine scanning; Antagonists; Bacteriophage M13; Calmodulin; Conformationally constrained peptides; Mutagenesis; Phage display

Indexed keywords

CALMODULIN; COMPLEMENTARY DNA; CYCLOPEPTIDE; ENZYME INHIBITOR; LIGAND; PEPTIDE LIBRARY; PROTEIN KINASE (CALCIUM,CALMODULIN);

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BACTERIOPHAGE M13; CATTLE; CHEMISTRY; DIRECTED MOLECULAR EVOLUTION; DRUG ANTAGONISM; GENETICS; IN VITRO STUDY; METHODOLOGY; MOLECULAR CLONING; MOUSE; NUCLEOTIDE SEQUENCE;

AMINO ACID SEQUENCE; ANIMALS; BACTERIOPHAGE M13; BASE SEQUENCE; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CALMODULIN; CATTLE; CLONING, MOLECULAR; DIRECTED MOLECULAR EVOLUTION; DNA, COMPLEMENTARY; ENZYME INHIBITORS; LIGANDS; MICE; PEPTIDE LIBRARY; PEPTIDES, CYCLIC;

EID: 0030202121     PISSN: 13811991     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF01715530     Document Type: Article

References (36)

1. Kay, B.K., Biologically displayed random pepiides as reagents in mapping protein-protein interactions, Perspect. Drug Discov. Design, 2 (1995) 251-268.
2. Cwirla, S.E., Peters, E.A., Barrett, R.W. Dower, W.J., Peptides on phage: A vast library of peptides for identifying ligands, Proc. Natl. Acad. Sci. USA, 87 (1990) 6378-6382.
3. Kay, B.K., Adey, N.B., He, Y.S., Manfredi, J.P., Mataragnon, A.H. Fowlkes, D.M., An M13 phage library displaying random 38-amino-acid peptides as a source of novel sequences with affinity to selected targets, Gene, 128 (1993) 59-65.
4. Motti, C, Nuzzo, M., Meola, A., Galfre, G., Felici, F., Cortese, R., Nicosia, A. Monaci, P., Recognition by human sera and immunogenicily of HBsAg mimotopes selected from an M13 phage display library, Gene, 146 (1994) 191-198.
5. Scott, J.K. Smith, G.P., Searching for peptide ligands with an epitope library, Science, 249 (1990) 386-390.
6. Koivunen, E., Wang, B. Ruoslahti, E., Isolation of a highly specific ligand for the alpha-5 beta-1 integrin from a phage display library, J. Cell Biol., 124 (1994) 373-380.
7. Dedman, J.R., Kaetzel, M.A., Chan, H.C., Nelson, D.J. Jamieson, G.J., Selection of targeted biological modifiers from a bacteriophage library of random pepiides. The identification of novel calmodulin-regulatory peptides, J. Biol. Chem., 268 (1993) 23025-23030.
8. Sparks, A.B., Quilliam, L.A.. Thorn, J.M., Der, C.J. Kay, B.K., Identification and characterization of Src SH3 ligands from phage-displayed random peptide libraries, J. Biol. Chem., 269 (1994) 23853-23856.
9. Munier, H., Blanco, F.J., Precheur, B., Diesis, E., Nieto, IL., Craescu, C.T. Barzu, O., Characterization of a synthetic calmodulin-binding peptide derived from Bacillus anthracis adenylate cyclase, J. Biol. Chem., 268 (1993) 1695-1701.
10. Newsholme, P., Angelos, K.L. Walsh, D.A., High- and intermediate-affinity calmodulin-binding domains of the alpha- and beta-subunits of phosphorylase kinase and their potential role in phosphorylalion-dependunl activation of she holoenzyme, J. Biol. Chem., 267 (1992) 810-818.
11. Payne, M.E., Fong, Y.L., Ono, T., Colbran, R.J., Kemp, B.E., Soderling, T.R. Means, A.R., Calciumcallmodulin-dependent protein kinase II. Characterization of distinct calmodulin binding and inhibitory domains, J. Biol. Chem., 263 (15) (1988) 7190-7195.
12. Means, A.R., Bagchi, I.C., VanBerkum, M.F. Kemp, B.E., Regulation of smooth-muscle myosin light-chain kinase by calmodulin. [Review], Adv. Exp. Med. Biol., 304 (1991) 11-24.
13. O'Neil, K.T. DeGrado, W.F., How calmodulin binds its targets: Sequence-independent recognition of amphiphilic alpha-helices [Review], Trends Biochem. Sci., 15 (1990) 59-64.
14. Chapman, E.R., Alexander, K., Vorherr, T., Carafoli, E. Storm, D.R., Fluorescence energy-transfer analysis of calmodulin-peptide complexes, Biochemistry, 31 (1992) 12819-12825.
15. Ikura, M., Clore, G.M., Gronenborn, A.M., Zhu, G., Klee, C.B. Bax, A., Solution structure of a calmodulin-target peptide complex by multidimensional NMR, Science, 256 (1992) 632-638.
16. Meador, WE., Means, A.R. Quiocho, F.A., Target enzyme recognition by calmodulin: 2.4 Å Structure of a calmodulin-peptide complex, Science, 257 (1992) 1251-1255.
17. Roth, S.M., Schneider, D.M., Strobel, L.A., Van, B.M., Means, A.R. Wand, A.J., Characterization of the secondary structure of calmodulin in complex with a calmodulin-binding domain peptide, Biochemistry, 31 (1992) 1443-1451.
18. Ohya, Y. Botstein, D., Diverse essential functions revealed by complementing yeast calmodulin mutants, Science, 263 (1994) 963-966.
19. VanBerkum, M.F. Means, A.R., Three amino acid substitutions in domain I of calmodulin prevent the activation of chicken smooth-muscle myosin light-chain kinase, J. Biol. Chem., 266 (1991) 21488-21495.
20. Adey, N.B. Kay, B.K., Identification of calmodulin-binding peptide consensus sequences from a phage-displayed random peptide library, Gene, 169 (1996) 133-134.
21. Koivunen, E., Wang, B. Ruoslahti, E., Phage libraries displaying cyclic peptides with different ring sizes: Ligand specificities of the RGD-directed integrais, Biotechnology, 13 (1995) 265-270.
22. O'Neil, K.T., Hoess, R.H., Jackson, S.A., Ramachandran, N.S., Mousa, S.A. DeGrado, W.F., Identification of novel peptide antagonists for GPIIb/IIIa from a conformationally constrained phage peptide library, Proteins, 14 (1992) 509-515.
23. Malencik, D.A. Anderson, S.R., Binding of simple peptides, hormones, and neurotransmitters by calmodulin, Biochemistry, 21 (1982) 3480-3486.
24. Adey, N.B., Sparks, A.B. Beasley, J.R., Construction of phage random peptide libraries, In Kay, B.K., Winter, J. McCafferty, J. (Eds.) Phage Display of Peptides and Protein Domains: A Laboratory Manual, Academic Press, San Diego, CA, in press.
25. Fowlkes, D.M., Adams, M.D., Fowler, V.A. Kay, B.K., Multipurpose vectors for peptide expression on the M13 viral surface, Biotechniques, 13 (1992) 422-428.
26. Sparks, A.B., Adey, N.B., Quilliam, L.A., Thorn, J.M. Kay, B.K., Screening phage-displayed random peptide libraries for SH3 ligands, Methods Enzymol., 255 (1995) 498-509.
27. Sparks, A.B., Hoffman, N.G., McConnell, S.J., Fowlkes, D.M. Kay, B.K., Cloning of ligand targets: Systematic isolation of SH3 domain-containing proteins, Nat. Biotechnol., 14 (1996) 741-744.
28. Apel, E.D., Byford, M.F., Au, D., Walsh, K.A. Storm, D.R., Identification of the protein kinase C phosphorylalion site in neuromodulin, Biochemistry, 29 (1990) 2330-2335.
29. Baudier, J.. Deloulme, J.C., Van, D.A., Black, D. Matthes, H.W, Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17). Identification of a consensus amino acid sequence between neurogranin and neuromodulin (GAP43) that corresponds to the protein kinase C phosphorylation site and the calmodulin-binding domain, J. Biol. Chem., 266 (1991) 229-237.
30. Urbauer, J.L., Short, J.H., Dow, L.K. Wand, A.J., Structural analysis of a novel interaction by calmodulin: High-affinity binding of a peptide in the absence of calcium, Biochemistry, 34 (1995) 8099-8109.
31. James, P., Vorherr, T. Carafoli, E., Calmodulin-binding domains: Just two faced or multi-faceted?, Trends Biochem. Sci., 20 (1995) 38-42.
32. 2+-calmodulin, Nat. Struct. Biol., 1 (1994) 795-801.
33. Giebel, L.B., Cass, R.T., Milligan, D.L., Young, D.C., Arze, R. Johnson, C.R., Screening of cyclic peptide phage libraries identifies ligands that bind Streptavidin with high affinities, Biochemistry, 34 (1995) 15430-15435.
34. Koivunen, E., Gay, D.A. Ruoslahti, E., Selection of peptides binding to the alpha-5 beta-1 integrin from phage display library, J. Biol. Chem., 268 (1993) 20205-20210.
35. McLafferty, M.A., Kent, R.B., Ladner, R.C. Markland, W., M13 bacteriophage displaying disulfide-constrained microproteins, Gene, 128 (1993) 29-36.
36. Clore, G.M., Bax, A., Ikura, M. Gronenborn, A.M., Structure of calmodulin-target peptide complexes, Curr. Opin. Struct. Biol., 3 (1993) 838-845.