The present invention relates to polypeptides which are covalently bound to molecular scaffolds such that two or more peptide loops are subtended between attachment points to the scaffold. In particular, the invention describes peptides which bind to TfR1. The invention also relates to multimeric binding complexes which comprise at least two of said bicyclic peptide ligands. The invention also includes pharmaceutical compositions comprising said peptide ligands and multimeric binding complexes and the use of said peptide ligands, and multimeric binding complexes and pharmaceutical compositions in preventing, suppressing or treating a disease or disorder through TfR1 mediated delivery of a therapeutic agent.

The present invention relates to a method of producing an immunoligand/payload conjugate, which method encompasses conjugating a payload to an immunoligand by means of a sequence-specific transpeptidase, or a catalytic domain thereof (FIG. 6B).

The present disclosure relates to a polypeptide exhibiting granulocyte-colony stimulating factor activity. The polypeptide comprises at least one non-native cysteine residue at a site selected from the group consisting of T.sub.1CP.sub.2 (SEQ ID NO: 25), P.sub.2CL.sub.3 (SEQ ID NO: 26), L.sub.3CG.sub.4 (SEQ ID NO: 27), G.sub.4CP.sub.5 (SEQ ID NO: 28), P.sub.5CA.sub.6 (SEQ ID NO: 29), A.sub.6CS.sub.7 (SEQ ID NO: 30), S.sub.96CP.sub.97 (SEQ ID NO: 31), P.sub.97CE.sub.98 (SEQ ID NO: 32), L.sub.99CG.sub.100 (SEQ ID NO: 33), P.sub.101CT.sub.102 (SEQ ID NO: 34), E.sub.122CE.sub.123 (SEQ ID NO: 35), L.sub.124CG.sub.125 (SEQ ID NO: 36), M.sub.126CA.sub.127 (SEQ ID NO: 37), P.sub.138CA.sub.139 (SEQ ID NO: 39), A.sub.143CF.sub.144 (SEQ ID NO: 40), R.sub.146CR.sub.147 (SEQ ID NO: 41), R.sub.169CH.sub.170 (SEQ ID NO: 42), H.sub.170CL.sub.171 (SEQ ID NO: 43), L.sub.171CA.sub.172 (SEQ ID NO: 44), A.sub.172CQ.sub.173 (SEQ ID NO: 45), and Q.sub.173CP.sub.174 (SEQ ID NO: 46) in an amino acid sequence having at least 90% sequence identity to sequence set forth in SEQ ID NO: 2.

A fusion protein includes a SARS-CoV-2 nucleocapsid N-terminal domain and/or a SARS-CoV-2 nucleocapsid C-terminal domain, wherein the fusion protein lacks the SARS-CoV-2 nucleocapsid aggregation domain.

Disclosed is a method for the preparation of a complex in which a physiologically active polypeptide is covalently bonded to an immunoglobulin constant region via a non-peptidyl linker. The method is characterized by the employment of a reducing agent, by which conventional problems of low production yield and modification of the polypeptide can be overcome. The physiologically active polypeptide-non-peptidyl polymer-immunoglobulin constant region complex can be produced with high purity and yield as well as at low cost. Thus, the method is industrially useful. Moreover, by exhibiting a prolonged action profile, the physiologically active polypeptide-non-peptidyl polymer-immunoglobulin constant region complex can be effectively used for developing long-acting formulations of physiologically active polypeptides which have improved drug compliance.

The present invention relates to a method for prolonging half-life of a protein or a (poly)peptide by replacing one or more amino acid residues of the protein. Further, the present invention is about the protein having a prolonged half-life prepared by the method above.

The present invention relates to a method for prolonging half-life of a protein or a (poly)peptide by replacing one or more amino acid residues of the protein. Further, the present invention is about the protein having a prolonged half-life prepared by the method above.

The present invention relates to a method for prolonging half-life of a protein or a (poly)peptide by replacing one or more amino acid residues of the protein. Further, the present invention is about the protein having a prolonged half-life prepared by the method above.

Disclosed are methods for forming targeted collagen products having an amplified desired characteristic, including the step of adding peptides exhibiting a desired characteristic to collagen to form the targeted collagen product. Further disclosed are methods for forming a targeted collagen product lacking an undesired characteristic, including the step of subtracting peptides exhibiting the undesired characteristic from collagen to form the targeted collagen product. Also disclosed are targeted collagen products formed by the disclosed methods.

The present invention relates to a method for prolonging half-life of a protein or a (poly)peptide by replacing one or more amino acid residues of the protein. Further, the present invention is about the protein having a prolonged half-life prepared by the method above.