Gabriele Tuchscherer

Institute of Polymers

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Manfred Mutter

Debiopharm (Switzerland)

M. Mutter

Lehigh University

Pascal Dumy

Institut des Biomolécules Max Mousseron

Christian W. Lehmann

University of Pittsburgh

Marc Mathieu

Inserm

Richard Mimna

University of Lausanne

Daniel Grell

University of Lausanne

Alain Razaname

University of Lausanne

Arunan Chandravarkar

Kerala State Council for Science, Technology and Environment

Patricia Durieux

Syngenta (Switzerland)

Cooperative Institutions

University of Lausanne

École Polytechnique Fédérale de Lausanne

Centre National de la Recherche Scientifique

Novartis (Switzerland)

Heidelberg University

Universitat de Barcelona

University of Basel

Utrecht University

Inserm

University Hospital Heidelberg

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Generation of Monospecific Peptide Antibodies to the DNA Binding Domain of p53

BioTechniques (2000)

Konrad Hüppi Darren W. Henderson David Siwarski Jacob Hochman Michael Bergel

The DNA binding domain (DBD) is the most mutated region of p53 in tumors and has proven to be relatively resistant to the generation of specific antibodies. Template assembled synthetic peptide (TASP) synthesis of a peptide derived from the DBD creates a highly immunogenic molecule without the need for large carriers such as keyhole limpet hemocyanin (KLH). In addition, a rapid means of generating monoclonal antibodies can be achieved through immunization in conjunction with ABL/MYC retrovirus injection into recipient mice. In this paper, we demonstrate that an antibody generated by this means, KH2, reacts specifically with the DBD of p53. To date, this is the first example of a peptide immunogen used successfully in ABL/MYC monoclonal antibody production. KH2 is also the first example of a monospecific antibody that directly binds to and, by definition, assumes the conformation of the DNA binding region of p53.

Immunogen

Keyhole limpet hemocyanin

10.2144/00295rr06

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Citations (1)

Template-assisted protein design: Chimeric TASP by chemoselective ligation

Stefano E. Cervigni Pascal Dumy Pravin T. P. Kaumaya M. Mathieu Origène Nyanguile

This symposium report discusses the recent progress in template-assisted protein de novo design. A no. of chemoselective ligation methods have been evaluated for use in TASP (TASP = template-assembled synthetic proteins) design. Such procedures are currently used to construct chimeric TASP mols. mimicking antigenic, binding and catalytic sites of proteins. [on SciFinder (R)]

Protein design

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Templates in protein de novo design

Journal of Biotechnology (1995)

Gabriele Tuchscherer M. Mutter

Template

Folding (DSP implementation)

Protein design

Protein Engineering

10.1016/0168-1656(95)00010-n

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Citations (47)

Der molekularen Erkennung auf der Spur: die duale Funktion von Pseudoprolinen für das Design von SH3-Liganden

Angewandte Chemie (2001)

Gabriele Tuchscherer Daniel Grell Yoshiro Tatsu Patricia Durieux Jimena Fernández‐Carneado

Pseudoproline (ΨPro) dienen als vielseitige Bausteine, die in der Lage sind, die bioaktive Konformation eines Peptidliganden sowie die für eine Protein-Protein-Wechselwirkung komplementäre Oberflächenstruktur zu induzieren. Diese duale Funktion von ΨPro wurde an prolinreichen Peptiden als effizienten Liganden für SH3-Domänen aufgezeigt (siehe Bild).

10.1002/1521-3757(20010803)113:15<2930::aid-ange2930>3.0.co;2-2

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Neue Proteinmimetika: eingeschlossene Faltungseinheiten (locked-in folds) am Beispiel des ββα-Zinkfingermotivs

Angewandte Chemie (1998)

Gabriele Tuchscherer Christian W. Lehmann Marc Mathieu

Nach dem Prinzip eines molekularen Baukastens werden sekundärstrukturbildende Peptidblöcke über kovalente Bindungen in eine vorgegebene Packungsanordnung zusammengefügt. Die daraus resultierenden „eingeschlossenen Faltungseinheiten”︁ (locked-in folds, LIF; siehe schematische Darstellung) sind chemisch einfach zugänglich und umgehen das bisher ungelöste Faltungsproblem linearer Peptidketten. Mit dieser Strategie können wesentliche strukturelle und funktionelle Merkmale von Zinkfingerproteinen imitiert werden.

10.1002/(sici)1521-3757(19981102)110:21<3160::aid-ange3160>3.0.co;2-j

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Citations (8)

ChemInform Abstract: Template‐Assisted Protein de novo Design

ChemInform (1997)

Gabriele Tuchscherer M. Mutter

Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.

10.1002/chin.199714284

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ChemInform Abstract: Protein Design as a Challenge for Peptide Chemists

ChemInform (1995)

Gabriele Tuchscherer M. Mutter

10.1002/chin.199532291

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Peptide engineering: a trimeric \"locked-in\" zinc finger motif

Barbara Rohwedder Pascal Dumy Manfred Mutter Gabriele Tuchscherer

A symposium report. The concept of template assembled synthetic proteins (TASP) has been evaluated for the locked-in fold derived from the DNA-binding bba zinc finger motif based on the consensus sequence Xaa3-Cys-Xaa2-4-Cys-Xaa12-His-Xaa3-4-His-Xaa4 to mimic some structural and functional features. [on SciFinder (R)]

Structural motif

Motif (music)

Zinc finger nuclease

Sequence motif

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Non-natural architectures in protein design: TASP molecules as receptor mimetics

The FASEB Journal (1997)

M. Mutter Pascal Dumy Patrick Garrouste Christian W. Lehmann Cristina Peggion

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Tailoring the Cis ‐ Trans Isomerization of Amides

Luis Moroder Christian Renner John Lopez Manfred Mutter Gabriele Tuchscherer

This chapter contains sections titled: Introduction Substituted Prolines Hydroxyprolines Mercaptoproline Halogenated Prolines Other Proline Analogs Alkylated Proline Analogs Bridged Bicyclic Proline Analogs Locked Proline Mimetics Pseudoprolines in Chemical Synthesis and Biology From Proline to Pseudoproline Synthesis of Pseudoprolines Pseudoprolines for the Synthesis of Difficult Sequences Pseudoprolines in Bioactive Peptides Pseudoprolines for Enhancing Peptide Cyclization and Turn Induction Pseudoprolines for Modulating Polyproline Helices Pseudoprolines for Modulating Structure and Function of Cyclosporins Pseudoprolines for Targeting Cis Bonds in Peptides and Proteins Conclusions and Perspectives

Polyproline helix

10.1002/9783527609338.ch11

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Citations (10)