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Department of Biochemistry

Publications of the Gutte Group

Gutte, B. & Klauser, S. Design of catalytic polypeptides and proteins. Protein Eng. Des. Sel. 31, 457-470 (2018). PMID: 31241746.

Boenzli, E., Robert-Tissot,C., Sabatino, G., Cattori, V., Meli, ML., Gutte, B., Rovero, P., Flynn, N., Hofmann-Lehmann, R. & Lutz, H. In vitro inhibition of feline leukemia virus infection by synthetic peptides derived from the transmembrane domain. Antivir Ther. 16, 905-913 (2011).

Oufir, M., Bisset, LR., Hoffmann, SRK., Xue, G., Klauser, S., Bergamaschi, B., Gervaix, A., Böni, J., Schüpbach, J. & Gutte, B. Artificial 64-residue HIV-1 enhancer-binding peptide is a potent inhibitor of viral replication in HIV-infected cells. Advances in Virol. ID 165871 (2011).

Nikolaev Y, Deillon C, Hoffmann SR, Bigler L, Friess S, Zenobi R, Pervushin K, Hunziker P & Gutte B. The leucine zipper domains of the transcription factors GCN4 and c-Jun have ribonuclease activity. PLoS One. 5(5):e10765 (2010).

Cui, T., Gao, Y., Ang, CX., Puah, CM., Gutte, B. & Lam, Y. Hydrogen peroxide enhances enterokinase-catalysed proteolytic cleavage of fusion protein. Recent Pat. Biotechnol. 2, 189-190 (2008).

Gutte, B. Solid-phase synthesis for a lifetime. Biopolymers. 90, 215 (2008).

Cui, T., Gao, Y., Puah, CM & Gutte, B. Efficient preparation of an acyclic permutant of kalata B1 from a recombinant fusion protein with thioredoxin. J. Biotechnol. 130, 378-384 (2007).

Gutte, B. Robert Bruce Merrifield (1921–2006). Angew Chem Int Ed Engl 45, 5412–3 (2006).       

Liu, N., Caderas, G., Deillon, C., Hoffmann, S., Klauser, S., Cui, T.  Gutte, B. Fusion proteins from artificial and natural structural modules. Curr. Protein Pept. Sci. 2, 107–21 (2001).       

Mittl, P. R., Deillon, C., Sargent, D., Liu, N., Klauser, S., Thomas, R. M., Gutte, B. & Grutter, M. G. The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure. Proc. Natl. Acad. Sci. USA 97, 2562–6 (2000). 

Caderas, G., Klauser, S., Liu, N., Bienz, A. Gutte, B. Inhibition of HIV-1 enhancer-controlled transcription by artificial enhancer-binding peptides derived from bacteriophage 434 repressor. Eur. J. Biochem. 266, 599–607 (1999).       

Liu, N., Deillon, C., Klauser, S., Gutte, B. Thomas, R. M. Synthesis, physicochemical characterization, and crystallization of a putative retro-coiled coil. Protein Sci. 7, 1214–20 (1998).       

Liu, N., Caderas, G., Gutte, B. Thomas, R. M. An artificial HIV enhancer-binding peptide is dimerized by the addition of a leucine zipper. Eur. Biophys. J. 25, 399–403 (1997).       

Stadler, K., Liu, N., Trotman, L., Hiltpold, A., Caderas, G., Klauser, S., Hehlgans, T. Gutte, B. Design, synthesis, and characterization of HIV-1 enhancer-binding polypeptides derived from bacteriophage 434 repressor. Int. J. Pept. Protein Res. 46, 333–40 (1995).       

Hehlgans, T., Stolz, M., Klauser, S., Cui, T., Salgam, P., Verca, S. B., Widmann, M., Leiser, A., Stadler, K.  Gutte, B. The DNA-binding properties of an artificial 42-residue polypeptide derived from a natural repressor. FEBS Lett.. 315, 51–5 (1993).       

Munk, K., Pritzer, E., Kretzschmar, E., Gutte, B., Garten, W. Klenk, H. D. Carbohydrate masking of an antigenic epitope of influenza virus haemagglutinin independent of oligosaccharide size. Glycobiology 2, 233–40 (1992).

Klauser, S., Gantner, D., Salgam, P. Gutte, B. Structure-function studies of designed DDT-binding polypeptides. Biochem. Biophys. Res. Commun. 179, 1212–9 (1991).       
Burgisser, D., Frey, S., Gutte, B.  Klauser, S. Preparation and characterization of polyclonal and monoclonal antibodies against the insecticide DDT. Biochem. Biophys. Res. Commun. 166, 1228–36 (1990).       

Langen, H., Epprecht, T., Linden, M., Hehlgans, T., Gutte, B.  Buser, H. R. Rapid partial degradation of DDT by a cytochrome P-450 model system. Eur. J. Biochem. 182, 727–35 (1989).       

Moser, R., Frey, S., Munger, K., Hehlgans, T., Klauser, S., Langen, H., Winnacker, E. L., Mertz, R. Gutte, B. Expression of the synthetic gene of an artificial DDT-binding polypeptide in Escherichia coli. Protein Eng. 1, 339–43 (1987).       

Aguet, M., Salgam, P., Gutte, B. Arnheiter, H. A crystalline synthetic peptide representing the epitope of a monoclonal antibody raised against synthetic interferon-alpha 1 fragment 111–166. Eur. J. Biochem. 146, 689–91 (1985).       

Arnheiter, H., Ohno, M., Smith, M., Gutte, B.  Zoon, K. C. Orientation of a human leukocyte interferon molecule on its cell surface receptor: carboxyl terminus remains accessible to a monoclonal antibody made against a synthetic interferon fragment. Proc. Natl. Acad. Sci. U S A 80, 2539–43 (1983).       

Arnheiter, H., Thomas, R. M., Leist, T., Fountoulakis, M. & Gutte, B. Physicochemical and antigenic properties of synthetic fragments of human leukocyte interferon. Nature 294, 278–80 (1981).       

Porschke, D.  Gutte, B. Interaction of lac repressor fragment 33--38 (Lys-Thr-Arg-Glu-Lys-Val) with homo-oligonucleotides. FEBS Lett. 127, 63–6 (1981).       

Gutte, B., Schindler, S., Standar, F. Wittschieber, E. Interaction of synthetic NH2-terminal fragments of bacteriophage lambda cro protein with nucleic acids. Biochem. Biophys. Res. Commun. 95, 1071–9 (1980).       

Jaenicke, R., Gutte, B., Glatter, U., Strassburger, W.  Wollmer, A. Conformation of a synthetic 34-residue polypeptide that interacts with nucleic acids. FEBS Lett. 114, 161–4 (1980).       

Gutte, B., Daumigen, M. Wittschieber, E. Design, synthesis and characterisation of a 34-residue polypeptide that interacts with nucleic acids. Nature 281, 650–5 (1979).       

Gutte, B. Effect of various nucleotides on folding and enzymic properties of a synthetic 63-residue analog of ribonuclease A and natural ribonuclease A. Eur. J. Biochem. 92, 403–10 (1978).       

Gutte, B. Synthetic 63-residue RNase A analogs. Simultaneous exchange of asparagine 44 by leucine and of threonine 45 by valine. J. Biol. Chem. 253, 3837–42 (1978).       

Kullmann, W. Gutte, B. Synthesis of an open-chain asymmmetrical cystine peptide corresponding to the sequence A18–21--B19–26 of bovine insulin by solid phase fragment condensation. Int. J. Pept. Protein Res. 12, 17–26 (1978).       

Gutte, B. Study of RNase A mechanism and folding by means of synthetic 63-residue analogs. J. Biol. Chem. 252, 663–70 (1977).       

Klotz, M. Gutte, B. Combination of insulin chains on an anti-insulin antibody-Sepharose column. Nature 262, 791–3 (1976).       

Barwald, K. R., Reid, R. E. Gutte, B. Formation and enzymic properties of dimeric RNase P. FEBS Lett. 60, 423–6 (1975).       

Gutte, B. A synthetic 70-amino acid residue analog of ribonuclease S-protein with enzymic activity. J. Biol. Chem. 250, 889–904 (1975).       

Gutte, B., Lin, M. C., Caldi, D. G. Merrifield, R. B. Reactivation of des(119-, 120-, or 121-124) ribonuclease A by mixture with synthetic COOH-terminal peptides of varying lengths. J. Biol. Chem. 247, 4763–7 (1972).       

Lin, M. C., Gutte, B., Caldi, D. G., Moore, S. Merrifield, R. B. Reactivation of des (119-124) ribonuclease A by mixture with synthetic COOH-terminal peptides; the role of phenylalanine-120. J. Biol. Chem. 247, 4768–74 (1972).       

Gutte, B. Merrifield, R. B. The synthesis of ribonuclease A. J. Biol. Chem. 246, 1922–41 (1971).       

Lin, M. C., Gutte, B., Moore, S. Merrifield, R. B. Regeneration of activity by mixture of ribonuclease enzymically degraded from the COOH terminus and a synthetic COOH-terminal tetradecapeptide. J. Biol. Chem. 245, 5169–70 (1970).       

Gutte, B. Merrifield, R. B. The total synthesis of an enzyme with ribonuclease A activity. J. Am. Chem. Soc 91, 501–2 (1969).       

Zahn, H., Gutte, B. Gattner, H. G. [Reactions of reduced A- and B-chains with insulin]. Diabetologia 4, 118–22 (1968).       

Zahn, H., Gutte, B., Pfeiffer, E. F. Ammon, J. [Resynthesis of insulin from the preoxidized A chain and reduced B chain]. Justus Liebigs Ann. Chem. 691, 225–31 (1966).