4 results about "Paratope" patented technology

A method for selecting camelid nanobodies from an array library collected from B cells of a camelid animal immunized with an antigen is provided. The method comprises (a) (i)phenylalanine (F) at position 42 (IMGT number), and (ii)a short hinge, and (iii)two or more cysteines in the nanobody sequence, and (iv)glutamine (Q) at position 123 (IMGT number), and (v)a low immunogenicity index, and (vi)a non-conventional VHH derived from germline IGHV3, or valine (V) included at position 42 (IMGT number), and (vii)a non-conventional VHH derived from germline IGHV4, or isoleucine (I) included at position 42 (IMGT number), and (viii)histidine (H), aspartic acid (D), or glutamic acid (E) in the CDR region, and (ix)histidine (H), aspartic acid (D), or glutamic acid (E) in the top 3 amino acid residues of the nanobody sequence, the FR2 region, or the top 16 amino acid residues of the FR3 region, and (x)tyrosine (Y) at position 42 (IMGT number), and a nanobody having a cyclic concave paratope structure arrangement, or (xi)phenylalanine (F) at position 42 (IMGT number), and a nanobody having a convex paratope structure arrangement, identifying a camelid nanobody having at least one of the features, and (b)measuring one or more biological activities of the nanobody identified in step (a).

Provided is a method of selecting a camelid nanobody from a library of camelid nanobody sequences collected from B cells from a camelid immunized with an antigen. The method comprises: (a) identifying a camelid nanobody that has at least one of the following features (i) a phenylalanine (F) at position 42 (IMGT numbering); (ii) a short hinge; (iii) two or more cysteines in the nanobody sequence; (iv) a glutamine (Q) at position 123 (IMGT numbering); (v) low immunogenicity metric; (vi) non-classic VHH derived from germline IGHV3 or a valine (V) at position 42 (IMGT numbering); (vii) non-classic VHH derived from germline IGHV4 or an isoleucine (I) at position 42 (IMGT numbering); (viii) a histidine (H), aspartic acid (D) or glutamic acid (E) in the CDR region; (ix) a histidine (H), aspartic acid (D) or glutamic acid (E) in the first three amino acid residues, the FR2 region, or the first sixteen amino acid residues of the FR3 region of the nanobody sequence; (x) a tyrosine (Y) at position 42 (IMGT numbering), and the nanobody having a loop, concave paratope structure configuration; or (xi) a phenylalanine (F) at position 42 (IMGT numbering), and the nanobody having a convex paratope structure configuration; and (b) measuring one or more biological activities of the nanobody identified in step (a).

The present invention relates to T cell engager masking molecules, and methods related thereto, that contribute to reduce the severity of cytokine release syndrome, wherein said molecules comprise (i.) a binding peptide which is deprived of an isomerization site and which binds to a T-cell engaging paratope of a bispecific T cell engager molecule (TCE), (ii.) a linker, and (iii.) a half-life extending polymer.

This disclosure provides an antibody design method based on flow matching and graph neural networks. The method comprises the following steps: Step 1, input parsing and initial antibody structure construction; Step 2, antigen epitope surface modeling; Step 3, local generation of binding regions based on flow matching; Step 4, global propagation of a surface-enhanced message encoder; Step 5, sequence-structure joint convergence generation, ultimately outputting a full-atom 3D antibody structure and paratope residue sequences. The above process achieves more accurate interface modeling and structure generation by constructing a flow matching generation process in the binding region and utilizing a global geometric message passing mechanism driven by antigen surface point clouds; simultaneously, by restricting flow matching computation to local regions, the computational overhead of generating large molecular structures is effectively reduced.