Structure and properties of TentaGel resin beads: Implications for combinatorial library chemistry

Molecular Diversity

Volumn 1, Issue 4, 1996, Pages 223-232

  Quarrell, Rachel ^a   Claridge, Timothy D W ^a   Weaver, George W ^a   Lowe, Gordon ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

31P NMR; Combinatorial libraries; Confocal scanning laser microscope; Spin lattice relaxation; TentaGel resin beads; Trypsin

Indexed keywords

DEUTERIUM; FLUORESCEIN ISOTHIOCYANATE; POLYSTYRENE DERIVATIVE; RESIN; SOLVENT; TENTAGEL RESIN; TRYPSIN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CONFOCAL MICROSCOPY; DIRECTED MOLECULAR EVOLUTION; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARTICLE SIZE; SOLUTION AND SOLUBILITY;

DEUTERIUM; DIRECTED MOLECULAR EVOLUTION; FLUORESCEIN-5-ISOTHIOCYANATE; MAGNETIC RESONANCE SPECTROSCOPY; MICROSCOPY, CONFOCAL; MOLECULAR STRUCTURE; PARTICLE SIZE; POLYSTYRENES; RESINS, SYNTHETIC; SOLUTIONS; SOLVENTS; TRYPSIN;

EID: 0030202292     PISSN: 13811991     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF01715526     Document Type: Article

References (34)

1. Merrifield, R.B., Peptide synthesis on a solid polymer, Fed. Proc. Fed. Am. Soc. Exp. Biol., 21 (1962) 412.
2. Furka. A., Sebestyen, F., Asgedom, M. Dibo, G., A general method for rapid synthesis of multicomponent peptide mixtures, Int. J. Pept. Protein Res., 37 (1991) 487-493.
3. Lam, K.S., Salmon, S.E., Hersh, E.M. Hruby, V.J., A new type of synthetic peptide library for identifying ligand-binding activity, Nature, 354 (1991) 82-84.
4. Houghten, R.A., Pinilla, C., Blondelle, S.E., Appel, J.R., Dooley, C.T. Cuervo, J.H., Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery, Nature, 354 (1991) 84-86.
5. Lowe, G., Combinatorial chemistry, Chem. Soc. Rev., 24 (1995) 309-317.
6. Gallop, M.A., Barrett, R.W., Dower, W.J., Fodor, S.P.A. Gordon, E.M., Applications of combinatorial technologies to drug discovery. I. Background and peptide combinatorial libraries, J. Med. Chem., 37 (1994) 1233-1251.
7. Gordon, E.M., Barrett, R.W., Dower, W.J., Fodor, S.A. Gallop, M.A., Applications of combinatorial technologies to drug discovery. II. Combinatorial organic synthesis, library screening strategies and future directions, J. Med. Chem., 37 (1994) 1385-1401.
8. Houghten, R.A., Appel, J.R., Blondelle, S.E., Cuervo, J.H., Dooley, C.T. Pinilla, C., The use of synthetic peptide combinatorial libraries for the identification of bioactive peptides, Biotechniques, 13 (1992) 413-421.
9. a. Rapp, W., Zhang, L. Bayer, E., Continuous-flow peptide synthesis on PSPOE-graft-copolymers, In Epton, R. (Ed.) Innovations and Perspectives in Solid-Phase Synthesis, Oxford, U.K., 1989, pp. 205-210.
10. b. Bayer, E. Rapp, W., Chemistry of Peptides and Proteins, Vol. 3, De Gruyter, Berlin, Germany, 1986, pp. 3-7.
11. Meldal, M., Auzanneau, F.-I., Hindsgaul, O. Palcic, M.M., A PEGA resin for use in the solid-phase chemical-enzymatic synthesis of glycopeptides, J. Chem. Soc. Ser. Chem. Commun., (1994) 1849-1850.
12. Renil, M. Meldal, M., Synthesis and application of a PEGA polymeric support for high capacity continuous-flow solid-phase peptide synthesis, Tetrahedron Lett., 36 (1995) 4647-4650.
13. n' specificities of serine proteinases using combinatorial peptide libraries, and evidence that enzymes can penetrate TentaGel resin beads, In Epton, R. (Ed.) Innovations and Perspectives in Solid-Phase Synthesis: 4th International Symposium, Edinburgh, U.K., 1995, in press.
14. Lowe, G. Quarrell, R., Peptide inhibitors of serine proteinases identified by screening targeted SPCLs of CMTI-I mutants, In Epton, R. (Ed.) Innovations and Perspectives in Solid-Phase Synthesis: 3rd International Symposium, Oxford, U.K., 1993, pp. 377-380.
15. Lichtman, J.W., Confocal microscopy, Sei. Am., August (1994) 30-35.
16. Quarrell, R., The inhibition of serine proteinases, and the development of a combinatorial library approach, Ph.D. Thesis, University of Oxford, Oxford, U.K., 1994, p. 163.
17. Kupryszewski, G., Wilusz, T., Polanowski, A., Rolka, K. Ragnarsson, U., Synthesis of trypsin inhibitor CMTI-I from squash seeds (Cucurbita maxima), Pol. J. Chem., 61 (1987) 789-793.
18. Polanowski, A., Otlewski, J., Wilusz, T., Wilimowska-Pelc, A. Leluk, J., A new family of serine proteinase inhibitors from squash seeds, Biol. Zentralbl., 107 (1988) 45-49.
19. Wieczorek, M., Otlewski, J., Cook, J., Parks, K., Leluk, J., Wilimowska-Pelc, A., Polanowski, A., Wilusz, T. Laskowski, M.J., The squash family of serine proteinase inhibitors. Amino acid sequences and association equilibrium constants for inhibitors from squash, summer squash, zucchini and cucumber seeds, Biochem. Biophys. Res. Commun., 126 (1985) 646-652.
20. Mann, K. Fish, W., Protein polypeptide chain molecular weights by gel chromatography in guanidinium chloride, Methods Enzymol., 26 (1972) 28-42.
21. Roberts, B.L., Markland, W., Ley, A.C., Kent, R.B., White, D.W., Guterman, S.K. Ladner, R.C., Directed evolution of a protein: Selection of potent neutrophil elastase inhibitors displayed on M13 fusion phage, Proc. Natl. Acad. Sci. USA, 89 (1992) 2429-2433.
22. Akiyama, S., Nakasuji, K. Nakagawa, M., Linear conjugated systems bearing some aromatic terminal groups. IV. The syntheses of some diarylacetylenes, Bull. Chem. Soc. Jpn., 44 (1971) 2231-2236.
23. 1H NMR in solid-phase organic synthesis, J. Org. Chem., 59 (1994) 7955-7956.
24. Sucholeiki, I., Polymer-assisted organic synthesis, In Epton, R. (Ed.) Innovations and Perspectives in Solid-Phase Synthesis: 4th International Symposium, Edinburgh, U.K., 1995, in press.
25. 13C NMR relaxation times of a tripeptide methyl ester and its polymer-bound analogues, Macromolecules, 23 (1990) 1937-1940.
26. Dixon, K.R., In Mason, J. (Ed.) Multinuclear NMR, Plenum Press, New York, NY, 1987, pp. 369-402.
27. Vagner, J., Barany, G., Sepetov, N.K., Krchňák, V., Lebl, M. Lam, K.S., Novel methodology for differentiation of 'surface' and 'interior' areas of polyethylene glycol-polystyrene (PEG-PS) supports: Application of 'library' screening procedures, In Epton, P.R. (Ed.) Innovations and Perspectives in Solid-Phase Synthesis: 3rd International Symposium, Oxford, U.K., 1993, pp. 347-352.
28. Blow, D.M., In Boyer, P.D. (Ed.) The Enzymes, Vol. III, Academic Press, New York, NY, 1971, pp. 185-248.
29. Stroud, R.M. Dickerson, R.E., The structure of bovin trypsin: Electron-density maps of the inhibited enzyme at 5 Å and at 2.7 Å resolution, J. Mol. Biol., 83 (1974) 195-208.
30. Bode, W. Schwager, P., The refined crystal structure of bovine β-trypsin at 1.8 Å resolution. II, J. Mol. Biol., 98 (1975) 693-717.
31. Schwert, G.W., J. Biol. Chem., 179 (1949) 655-664.
32. Sarfare, P.S., Kegeles, G. Kwon-Rhee, S.J., Relationship between active sites and polymerization sites in α-chymotrypsin, Biochemistry, 6 (1967) 1389-1393, and references cited therein.
33. Rao, M.S. Kegelas, G., An ultracentrifuge study of the polymerisation of α-chymotrypsin, J. Am. Chem. Soc., 80 (1958) 5724-5729.
34. 13C NMR monitoring of solid-phase glycoside synthesis, In Epton, R. (Ed.) Innovations and Perspectives in Solid-Phase Synthesis: 4th International Symposium, Edinburgh, U.K., 1995, in press.