Abstract: 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.

Abstract: 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.

Abstract: The present invention relates to single-chain proteins of the formula HRS1-L1-HRS2-L2-HRS3, wherein HRS1, HRS2 and HRS3 are heptad repeat sequences and L1 and L2 are structurally flexible linker sequences, and wherein HRS1, HRS2 and HRS3 form a thermodynamically stable triple-stranded, antiparallel, alpha-helical coiled coil structure in aqueous solution. The invention also relates to amino acid sequence variants, conditions and methods to obtain such proteins and variants, and usages thereof, especially their usage as scaffolds and as therapeutic products.

Abstract: 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.

Abstract: 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, nucleicacids and/or host cells.

Abstract: The application provides polypeptides comprising or essentially consisting of at least one Alphabody, wherein said Alphabody is capable of internalization into a cell and specifically binds to an intracellular target molecule. The application further provides nucleic acids encoding such polypeptides; methods for preparing such polypeptides; host cells expressing or capable of expressing such polypeptides; compositions, and in particular to pharmaceutical compositions, that comprise such polypeptides, nucleic acids and/or host cells; and uses of such polypeptides, nucleic acids, host cells and/or compositions, in particular for prophylactic, therapeutic or diagnostic purposes.

Abstract: The present invention relates to HIV-1 gp41-binding single-chain 3-stranded alpha-helical coiled coil molecules, denoted “Alphabodies”, nucleic acids encoding said Alphabodies, host cells comprising said nucleic acids, as well as pharmaceutical compositions comprising said Alphabodies, and methods for the treatment, prevention and diagnosis of HIV infection using said Alphabodies.

Abstract: The present invention relates to single-chain proteins of the formula HRS1-L1-HRS2-L2-HRS3, wherein HRS1, HRS2 and HRS3 are heptad repeat sequences and L1 and L2 are structurally flexible linker sequences, and wherein HRS1, HRS2 and HRS3 form a thermodynamically stable triple-stranded, antiparallel, alpha-helical coiled coil structure in aqueous solution. The invention also relates to amino acid sequence variants, conditions and methods to obtain such proteins and variants, and us ages thereof, especially their usage as scaffolds and as therapeutic products.

Abstract: 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, wherein at least 50% of the core residues are isoleucines, wherein all non-core residues are alanines, and wherein the constituting peptide sequences remain associated under physical conditions that are significantly different from physiological conditions.