C07K1/13

ANTI-HER2 POLYPEPTIDES DERIVATIVES AS NEW DIAGNOSTIC MOLECULAR PROBES

The present invention provides new polypeptide derivatives binding to Human Epidermal Growth Factor Receptor 2 (HER2) and their conjugates thereof, and to their use as a diagnostic agent, particularly for early detection, patient stratification and treatment monitoring of forms of cancer characterized by over-expression of HER2.

ANTI-HER2 POLYPEPTIDES DERIVATIVES AS NEW DIAGNOSTIC MOLECULAR PROBES

The present invention provides new polypeptide derivatives binding to Human Epidermal Growth Factor Receptor 2 (HER2) and their conjugates thereof, and to their use as a diagnostic agent, particularly for early detection, patient stratification and treatment monitoring of forms of cancer characterized by over-expression of HER2.

Antibody Conjugates and Methods of Making and Using the Same

Antibodies that include a sulfatase motif-containing tag in a constant region of an immunoglobulin (Ig) heavy chain polypeptide are disclosed. The sulfatase motif can be converted by a formylglycine-generating enzyme (FGE) to produce a formylglycine (fGly)-modified Ig heavy chain polypeptide. An fGly-modified Ig heavy chain polypeptide of the antibody can be covalently and site-specifically bound to a moiety of interest to provide an antibody conjugate. The disclosure also encompasses methods of production of such tagged Ig heavy chain polypeptides, fGly-modified Ig heavy chain polypeptides, and antibody conjugates, as well as methods of use of same.

Enzymes for trimming of glycoproteins

The invention concerns fusion proteins, wherein two endoglycosidases are fused, possibly via a linker. The fusion enzymes according to the invention have structure (1): EndoX-(L).sub.p-EndoY (1), wherein EndoX is an endoglycosidase, EndoY is an endoglycosidase distinct from EndoX, L is a linker and p is 0 or 1. Such fusion enzymes capable of trimming glycoproteins comprising at least two distinct glycoforms in a single step. The invention further concerns the use of the fusion enzyme according to the invention for trimming glycoproteins. In another aspect, the invention relates to the process of production of the fusion enzyme. In a further aspect, the inventions concerns a process for trimming glycoproteins, comprising trimming the glycoprotein with a fusion enzyme according to the invention, to obtain a trimmed glycoprotein.

Enzymes for trimming of glycoproteins

The invention concerns fusion proteins, wherein two endoglycosidases are fused, possibly via a linker. The fusion enzymes according to the invention have structure (1): EndoX-(L).sub.p-EndoY (1), wherein EndoX is an endoglycosidase, EndoY is an endoglycosidase distinct from EndoX, L is a linker and p is 0 or 1. Such fusion enzymes capable of trimming glycoproteins comprising at least two distinct glycoforms in a single step. The invention further concerns the use of the fusion enzyme according to the invention for trimming glycoproteins. In another aspect, the invention relates to the process of production of the fusion enzyme. In a further aspect, the inventions concerns a process for trimming glycoproteins, comprising trimming the glycoprotein with a fusion enzyme according to the invention, to obtain a trimmed glycoprotein.

18F labeled amino acids, derivatives thereof and method of making same

The present invention provides .sup.18F-labeled amino acids or derivatives thereof having formula (I) and methods of making same, which can be suitable for PET imaging: ##STR00001##

18F labeled amino acids, derivatives thereof and method of making same

The present invention provides .sup.18F-labeled amino acids or derivatives thereof having formula (I) and methods of making same, which can be suitable for PET imaging: ##STR00001##

METHODS FOR RADIOLABELLING GRPR ANTAGONISTS AND THEIR KITS

The present invention relates to methods for radiolabelling GRPR antagonists such as NeoB, and their kits. In particular, the invention to a method for labeling a gastrin-releasing peptide receptor (GRPR) antagonist with a radioactive isotope, preferably .sup.68Ga, .sup.67Ga or .sup.64Cu, said method comprising the steps of: i. providing a first vial comprising said GRPR antagonist in dried form, ii. adding a solution of said radioactive isotope into said first vial, thereby obtaining a solution of said GRPR antagonist with said radioactive isotope, iii. mixing the solution obtained in ii. with at least a buffering agent and incubating it for a sufficient period of time for obtaining said GRPR antagonist labeled with said radioactive isotope, and, iv. optionally, adjusting the pH of the solution.

METHODS FOR RADIOLABELLING GRPR ANTAGONISTS AND THEIR KITS

The present invention relates to methods for radiolabelling GRPR antagonists such as NeoB, and their kits. In particular, the invention to a method for labeling a gastrin-releasing peptide receptor (GRPR) antagonist with a radioactive isotope, preferably .sup.68Ga, .sup.67Ga or .sup.64Cu, said method comprising the steps of: i. providing a first vial comprising said GRPR antagonist in dried form, ii. adding a solution of said radioactive isotope into said first vial, thereby obtaining a solution of said GRPR antagonist with said radioactive isotope, iii. mixing the solution obtained in ii. with at least a buffering agent and incubating it for a sufficient period of time for obtaining said GRPR antagonist labeled with said radioactive isotope, and, iv. optionally, adjusting the pH of the solution.

METHOD FOR IMPROVING TRIBOELECTRIC OUTPUT PERFORMANCE OF PROTEIN FILM BY CHANGING PROTEIN STRUCTURE
20220380559 · 2022-12-01 · ·

The invention discloses a method for improving triboelectric output performance of a protein film by changing a protein structure. Indissolvable protein powder and a trace amount of another protein powder are co-dissolved in a strong alkaline aqueous solution and maintained for a period of time, and then acidifying treatment is performed to achieve neutral condition to allow charge redistribution to induce refolding of the protein, which results in burying of hydrophobic groups of the protein and exposure of charged groups. Therefore, the solubility of the protein is remarkably improved, and a uniform protein solution is formed under a neutral condition. The plant protein structure is changed through a pH cycle process, a surface group exposure condition is adjusted, and the output performance of the plant protein film is greatly improved.