Pieris Ag

Technische Universitat Munchen

Technische Universitaet Muenchen

Pieris Pharmaceuticals Gmbh

Xl-protein Gmbh

Evonik Degussa Gmbh

Evonik Operations Gmbh

Other

Biotechnologicky Ustav Av Cr, V.v.i.

Pieris Proteolab Ag

Technische Universitaet Meunchen

Arne Skerra

Steffen Schlehuber

Martin Huelsmeyer

Andreas Hohlbaum

Gabriele Matschiner

Martin Schlapschy

Thomas Haas

Kristian Hobolt Jensen

Uli Binder

Steffen Schaffer

Jan Christoph Pfeffer

Eric Boudreau

Frank Schmidt

Michaela Gebauer

Gerald Beste

Thomas Stibora

Volker Morath

Richard Jones

Ian Kimber

Rebecca Dearman

Dominik Hinz

Sabine Rauth

Hyun-jin Kim

Mirja Wessel

Wolfgang Kroutil

Markus Pötter

Cyril Barinka

Jakub Ptacek

Andre Schiefner

Alexandra Lerchner

Antonia Richter

Winfried Meining

Evelyn Eggenstein

Ina Theobald

Andreas Eichinger

Harald Jakob

Rachida Siham Bel Aiba

Hans-Georg Joerg Hennemann

Stefan Achatz

Stefan Trentmann

Hendrik Gille

Volker Sieber

Hans-Juergen Christian

Christoph Schorsch

Daniel Fischer

Katrin Grammann

Kai Doderer

Hyun-Jin Kim

Claudia Rollmann

Eva-Maria Eckl

Jasmin Corthals

Martin Vogt

Friedrich-Christian Deuschle

André Schiefner

Lukas Eisoldt

Silvana Roeder

Michael Muller

Michael Schemann

Julia Martin

Thomas Berger

Martin Pöhlchen

Johann H Sattler

Katharina Christin Tauber

Broder Rühmann

Broder Ruehmann

Christian Rausch

Ludwig Kirmair

Amber Nasreen

Richard C Jones

Markus PÖTTER

Michael MÜLLER

The present invention relates to a cluster of differentiation 98 heavy chain (CD98hc)-specific binding protein, wherein the CD98hc-specific binding protein is a lipocalin 2 (Lcn2)-derived binding protein and binds to CD98hc with a Kof 200 nM or lower.

High affinity anticalins directed against human CD98hc

The present invention relates to a novel library for the generation of muteins and to novel muteins derived from human lipocalin 2 (Lcn2, hNGAL) and related proteins that bind a given target with detectable affinity. The invention also relates to corresponding nucleic acid molecules encoding such a mutein and to a method for their generation. The invention further relates to a method for producing such a mutein. For example, such muteins may serve to bind and deplete pathological forms of natural biomolecules such as the amyloid beta peptide in Alzheimer's disease or may target the fibronectin extra-domain B, which is associated with tumor neovasculature.

Muteins of human lipocalin 2 (Lcn2, hNGAL) with affinity for a given target

The present invention relates to a prostate-specific membrane antigen (PSMA)-specific binding protein, wherein the PSMA-specific binding protein is a lipocalin 2 (Lcn2)-derived binding protein and binds to PSMA with a Kof 10 nM or lower. The present invention also relates to a nucleic acid molecule encoding the PSMA-specific binding protein of the invention, a vector comprising said nucleic acid molecule of the invention and a host cell transformed with the vector. Furthermore, the invention relates to a method of producing the PSMA-specific binding protein of the invention, the method comprising culturing the host cell of the invention under suitable conditions and isolating the PSMA-specific binding protein produced. The present invention further relates to a protein conjugate comprising the PSMA-specific binding protein of the invention, or the PSMA-specific binding protein produced by the method of the invention. In addition, the present invention relates to a pharmaceutical or diagnostic composition; to the PSMA-specific binding protein of the invention, the nucleic acid molecule of the invention, the vector of the invention, the host cell of the invention or the PSMA-specific binding protein produced by the method of the invention, for use in therapy and/or diagnosis, and in particular for use in the therapy and/or diagnosis of tumors, Crohn's disease and/or neurological diseases.

PSMA-specific binding proteins

The present invention relates to a nucleic acid molecule comprising a low repetitive nucleotide sequence encoding a proline/alanine-rich amino acid repeat sequence. The encoded polypeptide comprises a repetitive amino acid sequence that forms a random coil. The nucleic acid molecule comprising said low repetitive nucleotide sequences can further comprise a nucleotide sequence encoding a biologically or pharmacologically active protein. Further, the present invention provides for selection means and methods to identify said nucleic acid molecule comprising said low repetitive nucleotide sequence. The present invention also relates to a method for preparing said nucleic acid molecules. Also provided herein are methods for preparing the encoded polypeptide or drug conjugates with the encoded polypeptide using the herein provided nucleic acid molecules. The drug conjugate may comprise a biologically or pharmacologically active protein or a small molecule drug. Also provided herein are vectors and hosts comprising such nucleic acid molecules.

Nucleic acids encoding repetitive amino acid sequences rich in proline and alanine residues that have low repetitive nucleotide sequences

There is provided a microbial cell expressing a mutant AlkB enzyme, the mutant AlkB enzyme comprising at least one point mutation in the wild type sequence of AlkB, wherein the point mutation is at amino acid position V129 and/or T136 of the wild type AlkB enzyme. There is also provided a method for producing omega-hydroxy carboxylic acid and/or ester thereof using this cell.

Microorganism expressing mutant AlkB enzyme and use to prepare omega-hydroxy carboxylic acid and/or ester

A method is useful for the biocatalytic synthesis of proteinogenic L-amino acids, such as L-alanine, L-valine, L-methionine, L-leucine, L-isoleucine or L-phenylalanine from a respective aldehyde and carbon dioxide. In particular, the method is useful for the biocatalytic synthesis of L-methionine from 3-methylthio-propanal ('methional') and carbon dioxide.

Process for producing L-methionine from methional

The present invention relates to a biosynthetic random coil polypeptide or a biosynthetic random coil polypeptide segment or biosynthetic conjugate, in which the biosynthetic random coil polypeptide, the biosynthetic random coil polypeptide segment, or the biosynthetic conjugate comprises an amino acid sequence consisting solely of proline and alanine amino acid residues, wherein the amino acid sequence consists of at least about 50 proline (Pro) and alanine (Ala) amino acid residues. The at least about 50 proline (Pro) and alanine (Ala) amino acid residues may be (a) fconstituent(s) of a heterologous polypeptide or an heterologous polypeptide construct. Also uses and methods of use of these biosynthetic random coil polypeptides or polypeptide segments or conjugates are described.

Biosynthetic proline/alanine random coil polypeptides and their uses

The invention relates to an enzymatic method for producing 2-hydroxy-4-methylmercaptobutanoic acid from 3-methylthio-propanal (3-methylmercaptopropanal (MMP) or 'methional') and carbon dioxide.

Enzymatic method for producing 2-hydroxy-4-methylmercaptobutanoic acid (MHA)

The present disclosure relates to a collection of novel muteins derived from human &#x3b1;1m (or a1m) polypeptide or a functional homologue thereof. The disclosure further refers to a &#x3b1;1m mutein capable of specifically binding to one or more targets other than a target to which wild-type &#x3b1;1m binds. The disclosure also relates to a method for producing such collection of muteins and a method for isolating a mutein capable of binding one or more such non-natural targets of wild-type &#x3b1;1m polypeptide. These aspects are made possible due to, e.g, the structural elucidation of &#x3b1;1m disclosed herein by the present inventors, an appreciation of ligand-binding sights thereof and, hence, an understanding of which amino acid positions are most suitable for mutagenesis for re-engineering specificity and affinity for any given target while maintaining the secondary and/or tertiary structure of a1m.

Muteins of a1m lipocalin and method of production therefor

Muteins of human lipocalin 2 (Lcn2,hNGAL) with affinity for a given target

The present invention relates to a biosynthetic random coil polypeptide or a biosynthetic random coil polypeptide segment or biosynthetic conjugate, in which the biosynthetic random coil polypeptide, the biosynthetic random coil polypeptide segment, or the biosynthetic conjugate comprises an amino acid sequence consisting solely of proline and alanine amino acid residues, wherein the amino acid sequence consists of at least about 50 proline (Pro) and alanine (Ala) amino acid residues. The at least about 50 proline (Pro) and alanine (Ala) amino acid residues may be (a) constituent(s) of a heterologous polypeptide or an heterologous polypeptide construct. Also uses and methods of use of these biosynthetic random coil polypeptides or polypeptide segments or conjugates are described.

The present invention relates to novel muteins derived from human tear lipocalin. The invention also refers to a corresponding nucleic acid molecule encoding such a mutein and to a method for its generation. The invention further refers to a method for producing such a mutein. Finally, the invention is directed to a pharmaceutical composition comprising such a lipocalin mutein as well as to various uses of the mutein.

Muteins of tear lipocalin and methods for obtaining the same

A process for producing alanine, including culturing a cell under aerobic conditions in an aqueous phase in the presence of an inorganic nitrogen source, and then contacting the aqueous phase and the cell cultured in the aqueous phase with a hydrophobic organic phase. The cell is a prokaryotic or a lower eukaryotic cell and expresses a recombinant alanine dehydrogenase.

Method for aerobically producing alanine or a compound produced using alanine

The present disclosure relates to a collection of novel muteins derived from human &#x3b1;1m (or a1m) polypeptide or a functional homolog thereof. The disclosure further refers to a &#x3b1;1m mutein capable of specifically binding to one or more targets other than a target to which wild-type &#x3b1;1m binds. The disclosure also relates to a method for producing such collection of muteins and a method for isolating a mutein capable of binding one or more such non-natural targets of wild-type &#x3b1;1m polypeptide. These aspects are made possible due to, e.g, the structural elucidation of &#x3b1;1m disclosed herein by the present inventors, an appreciation of ligand-binding sights thereof and, hence, an understanding of which amino acid positions are most suitable for mutagenesis for re-engineering specificity and affinity for any given target while maintaining the secondary and/or tertiary structure of a1m.

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Arne Skerra