Complix Nv

Lonza Biologics Plc

Complix Sa

Lonza Biologies Plc

Algonomics N.v.

Johan Desmet

Ignace Lasters

Maria Henderikx

Stefan Loverix

Dominique Vlieghe

Philippe Stas

Carlo Boutton

Klaartje Somers

Anita Wehnert

Mark Vaeck

Philippe Alard

Geert Meersseman

Sabrina Deroo

Jan Spriet

Nathalie Boutonnet

Jurgen Pletinckx

Krista De Clercq

Jürgen Debaveye

Maria Paulina Henderikx

The invention provides single-chain Alphabody library comprising at least 100 different-sequence single-chain Alphabody polypeptides, wherein said Alphabody polypeptides differ from each other in at least one of a defined set of 5 to 20 variegated amino acid residue positions, and wherein at least 70% but not all of said variegated amino acid residue positions are located either in the loop, helix surface or linker region of the Alphabody. The invention further provides methods for use of the Alphabody libraries and Alphabodies obtainable by the methods of the invention.

Alphabody libraries and methods for producing the same

Provided herein are polypeptides that are capable of crossing the cellular membrane and entering into the intracellular environment, which polypeptides are suitable for use in prophylactic, therapeutic or diagnostic applications as well as in screening and detection. Nucleic acids encoding such polypeptides; methods for preparing such polypeptides, host cells expressing or capable of expressing such polypeptides, compositions, and in particular pharmaceutical compositions, that comprise such polypeptides, in particular for prophylactic, therapeutic or diagnostic purposes are also provided.

Polypeptides capable of cellular internalization

The application provides Alphabodies that specifically bind to IL-23, as well as to polypeptides that comprise or essentially consist of such Alphabodies. Also provided herein are nucleic acids encoding such Alphabodies; to methods for preparing such Alphabodies and polypeptides; and in particular to pharmaceutical compositions, that comprise such Alphabodies, polypeptides, nucleic acids and/or host cells.

Polypeptides specifically binding to IL-23

The present invention is related to a non-natural, thermodynamically stable, proteinaceous scaffold consisting of three non-covalently associated peptides, wherein each peptide sequence comprises less than fifty amino acid residues and wherein at least 50% of the said residues are substitutable amino acids into at least ten different amino acid residue types. The present invention is further related to a non-natural, triple-stranded, parallel alpha-helical coiled coil scaffold wherein each of the three constituting peptide sequences comprise between 2 and 7 consecutive heptad repeats of the formula cxxcxxx (SEQ ID NO: 10), wherein at least 70% of the core c-residues are isoleucines, wherein all non-core x-residues are alanines, and wherein the constituting peptide sequences remain associated under physical conditions that are significantly different from physiological conditions.

Non-natural proteinaceous scaffold made of three non-covalently associated peptides

The present invention provides methods for generating information related to the molecular structure of a biomolecule.

Method for generating information related to the molecular structure of a biomolecule

The present invention is related to a quantitative structure-based affinity scoring method for peptide/protein complexes. More specifically, the present invention comprises a method that operates on the basis of a highly specific force field function (e.g. CHARMM) that is applied to all-atom structural representations of peptide/receptor complexes. Peptide side-chain contributions to total affinity are scored after detailed rotameric sampling followed by controlled energy refinement. The method of the invention further comprises a de novo approach to estimate dehydration energies from the simulation of individual amino acids in a solvent box filled with explicit water molecules and applying the same force field function as used to evaluate peptide/receptor complex interactions.

Method for affinity scoring of peptide/protein complexes

The invention provides methods and apparatus for analyzing a protein structure by

Apparatus and method for structure-based prediction of amino acid sequences

The present invention relates to a method for structure-based prediction of properties of peptides and peptide analogs in complex with major histocompatibility (MHC) class I and class II molecules. The properties mainly relate to the three-dimensional structure of an MHC/peptide complex and the binding affinity of a peptide for an MHC receptor. The invention further relates to a computer program and a device therefor. The invention further relates to data produced by a method of the invention. The invention further relates to peptides and peptide analogs predicted to bind to target-MHC molecules. The present invention thus relates to the field of immunology, with possible applications in manufacture of vaccinates, de-immunization of proteins, and manufacture of therapeutic agents, especially immunotherapeutic agents.

Method, computing routine, device for predicting properties of MHC/peptide complexes, and data and peptides produced therefrom

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Kortrijk, Belgium

Johan Desmet