Abstract: A molecular tool for use in a method of providing a molecule that is capable of binding a target molecule based on a set of polypeptides. A polypeptide having a sequence selected from SEQ ID NOs 1-32. The polypeptide may be used in a method of screening for a ligand-polypeptide conjugate capable of binding a target molecule for the ligand. A ligand-polypeptide conjugate, useful e.g. in therapy.

Abstract: A molecular tool for use in a method of providing a molecule that is capable of binding a target molecule based on a set of polypeptides. A polypeptide having a sequence selected from SEQ ID NOs 1-32. The polypeptide may be used in a method of screening for a ligand-polypeptide conjugate capable of binding a target molecule for the ligand. A ligand-polypeptide conjugate, useful e.g. in therapy.

Abstract: Isolated polypeptides comprising one or more of SEQ ID NOs 3-18, which show a specific binding for C-reactive protein (CRP). A library of isolated polypeptides comprising the polypeptides of SEQ ID NOs 3-18 is disclosed, as are compositions comprising such polypeptides.

Abstract: A method for determining the presence of a compound in a liquid solution, by admixing the liquid solution with a plurality of nanoparticles; providing conditions effective to cause aggregation of the nanoparticles in the liquid solution in the absence of said compound in the liquid solution; and observing a detectable signal reflecting the amount of aggregation of nanoparticles in the liquid solution, wherein the presence of the compound in the liquid solution results in a detectable signal reflecting a reduced amount of aggregation of nanoparticles in the liquid solution, in comparison to the amount of aggregation of nanoparticles obtained in the liquid solution in the absence of the compound therein. A nanoparticle, a composition, a kit and a for multi-well plate for use in the method are also disclosed. In some embodiments the association is cation-, anion and/or PH induced e.g. by using helix-loop-helix polypeptides as first and second molecules attached to the nanoparticles.

Abstract: A polypeptide dimer is provided wherein both protomers have a sequence according to SEQ ID NO: 1 and at least one phosphocholine derivative is attached to the polypeptide. The polypeptide shows a specific binding for C-reactive protein (CRP). The utilization of the polypeptide in assays for determining the concentration of CRP is described. The purification of CRP, and compositions comprising the CRP also are provided.

Abstract: A polypeptide dimer is provided wherein both protomers have a sequence according to SEQ ID NO: 1 and at least one phosphocholine derivative is attached to the polypeptide. The polypeptide shows a specific binding for C-reactive protein (CRP). The utilization of the polypeptide in assays for determining the concentration of CRP is described. The purification of CRP, and compositions comprising the CRP also are provided.

Abstract: At least one embodiment of the present invention relates to new peptides designed based on the sequence of human lactoferrin and to use thereof, in particular for treatment and/or prevention of infections, inflammations, tumours, pain, wounds and/or scars.

Abstract: The present invention relates to the use of specific synthetic sensor molecules for the discrimination of proteins and protein domains involved in autoimmunity. More specifically, in one embodiment, the invention relates to the detection of antibodies which bind to specific domains of the Ro52 protein. In another embodiment, the invention relates to the use of specific synthetic sensor molecules to identify domains of the Ro52 protein with different antibody specificities. The invention also includes a method for assessing the risk that a fetus will develop congenital heart block. The invention enables the evaluation and differential diagnosis of a range of autoimmune disorders, allowing appropriate treatment or more generally medical intervention decisions to be made.

Abstract: The invention relates to new peptides formed of at least seven subsequent amino acids of the amino acids in position 12-40, counted from the N-terminal end, in the sequence constituting human lactoferrin, and preferably modifications thereof. The invention also relates to medicinal products comprising such peptides, especially intended for treatment and prevention of infections, inflammations and tumours. Furthermore, the invention relates to food stuff, e.g. infant formula food, comprising the above mentioned peptides.

Abstract: Novel peptide having a sequence according to SEQ. ID. No. 1, SEQ. ID. No. 2 and/or SEQ. ID. No. 3 are disclosed and also polypeptide scaffold consisting of a four helix bundle formed of two dimerized helix-loop-helix motifs, said helix-loop-helix motifs having sequences according to SEQ. ID. No. 1, SEQ. ID. No. 2 and/or SEQ. ID. No. 3 which may comprise a fluorescent probe at the side chain of Lys15 and a ligand with affinity for a target molecule at the side chain of Lys8 or Lys34. Also disclosed are polypeptide scaffolds for use in biosensing applications with or without the polypeptide scaffold anchored to a solid surface.

Abstract: A polypeptide dimer is provided wherein both protomers have a sequence according to SEQ ID NO: 1 and at least one phosphocholine derivative is attached to the polypeptide. The polypeptide shows a specific binding for C-reactive protein (CRP). The utilization of the polypeptide in assays for determining the concentration of CRP is described. The purification of CRP, and compositions comprising the CRP also are provided.

Abstract: Novel peptide having a sequence according to SEQ. ID. No. 1, SEQ. ID. No. 2 and/or SEQ. ID. No. 3 are disclosed and also polypeptide scaffold consisting of a four helix bundle formed of two dimerized helix-loop-helix motifs, said helix-loop-helix motifs having sequences according to SEQ. ID. No. 1, SEQ. ID. No. 2 and/or SEQ. ID. No. 3 which may comprise a fluorescent probe at the side chain of Lys15 and a ligand with affinity for a target molecule at the side chain of Lys8 or Lys34. Also disclosed are polypeptide scaffolds for use in biosensing applications with or without the polypeptide scaffold anchored to a solid surface.

Abstract: A catalytically active peptide comprising an imidazole function in position i flanked by at least one functional group to be amidated in position i+3+4k, where k is an integer equal to or higher than ?1 or in position i?4?4n, wherein n is an integer equal to or higher than 0, characterized in that it also comprises at least one activating group in position i+4+4n or i?3?4n, respectively, wherein n is as above.

Abstract: Disclosed are novel polypeptides of a four helix bundle formed of two dimerized helix-loop-helix motifs, wherein either both have a sequence according to SEQ. ID No. 1, SEQ. ID No. 2, SEQ. ID No. 3, SEQ. ID No. 4, SEQ. ID No. 5, or SEQ. ID No. 7, or one has a sequence according to SEQ. ID No. 6, and the other one has a sequence according to SEQ. ID No. 1, SEQ. ID No. 2, SEQ. ID No. 3, SEQ. ID No. 4, SEQ. ID No. 5 or SEQ. ID No. 7.

Abstract: The invention relates to new peptides formed of at least seven subsequent amino acids of the amino acids in position 12-40, counted from the N-terminal end, in the sequence constituting human lactoferrin, and preferably modifications thereof. The invention also relates to medicinal products comprising such peptides, especially intended for treatment and prevention of infections, inflammations and tumours. Furthermore, the invention relates to food stuff, e.g. infant formula food, comprising the above mentioned peptides.

Abstract: A catalytically active peptide comprising an imidazole function in position i flanked by at least one functional group to be amidated in position i+3+4k, where k is an integer equal to or higher than ?1 or in position i?4?4n, wherein n is an integer equal to or higher than 0, characterized in that it also comprises at least one activating group in position i+4+4n or i?3?4n, respectively, wherein n is as above.

Abstract: A catalytically active peptide comprising an imidazole function in position i flanked by at least one functional group to be amidated in position i+3+4k, where k is an integer equal to or higher than ?1 or in position i?4?4n, wherein n is an integer equal to or higher than 0, characterized in that it also comprises at least one activating group in position i+4+4n or i?3?4n, respectively, wherein n is as above.

Abstract: The invention relates to new peptides formed of at least seven subsequent amino acids of the amino acids in position 12-40, counted from the N-terminal end, in the sequence constituting human lactoferrin, and preferably modifications thereof. The invention also relates to medicinal products comprising such peptides, especially intended for treatment and prevention of infections, inflammations and tumours. Furthermore, the invention relates to food stuff, e.g. infant formula food, comprising the above mentioned peptides.

Abstract: A method for site-selective acyl transfer in amidation of folded polypeptides and proteins based on the use of a chemical structure element comprising an imidazole function, such as histidine, in position i flanked by at least one functional group to be amidated, such as lysinc, in position i+3+4k. where K is an integer equal to or higher than ?1, or in position i?4?4n, wherein n is an integer equal to or higher than 0, and at least one activating group, such as serine, in position i+4+4n or i?3?4n, respectively.

Abstract: An apparatus for determining a drug dosage is disclosed comprising: an input interface for receiving data on at least one patient's biochemical profile, and data on at least one specific property of the drug; and processing means having a simulation module for simulating the effect of a certain dosage based on the received data, and an evaluation module for determining, based on a simulation on at least one dosage, a drug dosage for the at least one patient in question. A corresponding method is also disclosed. Hereby, a dosage may be personalized on the basis of the condition and state of each patient, leading to a more effective dosage. This leads to a better and less hazardous treatment of the patient, as well as decreased health related costs in the society. Further, the strain on the environment could be reduced.