12/29/2023 0 Comments Looped domains with protein scaffoldThese proteins are referred to as protein scaffold, alternative protein scaffold, alternative scaffold, non-antibody protein scaffold, or alternative binding proteins (hereinafter, as referred to as ‘protein scaffold’) (Skerra A, FEBS J, 275:2677-2683, 2008 Skerra, Current Opin. In order to solve the above problems, there have been attempts to develop proteins, other than the antibodies, that specifically bind to target molecules, such as antibodies, while solving the problems regarding the antibodies (Review Article: Hey, et al., Trends in Biotech. However, the antibodies have various problems in that they are purely expressed and low in solubility, they should be expressed in an animal cell-expressing cell line, the purification costs are very expensive, and their stabilities are very low in the reducing intracellular environment. As known molecules that specifically bind to target molecules to control the biological activities of the target molecules, antibodies (full-length antibodies or their fragments) have been under leading development. Interactions between biomolecules (for example, protein-protein, protein-nucleic acid interactions) play important roles in various life phenomena such as growth, differentiation and development of cells, intercellular/intracellular signal transductions, and mass transport. Specific information of the domain may be searched on web sites for bioinformatics, such as Prosite (Hulo N., et al., Nucleic Acids Res, 36:D245-249, 2008 Website: ), SMART (Letunic I., et al., Nucleic Acids Res., 34:D257-D260, 2006 Website: ), and representative examples of the domain include immunoglobulin-like, fibronectin II and III, Kringle, etc. At least one identical domain may be distributed in various proteins, and one protein may be composed of various different domains. For the proteins, a domain is referred to a separate functional and/or structural unit. BACKGROUND ARTįrom the analysis of amino acid sequences and secondary and tertiary structures of proteins, a large number of the proteins are composed of separate domains (or modules). Further the present invention provides a method and a composition of Kringle domain variants for prevention, detection, diagnosis, treatment or relieving of diseases or disorders, particularly cancers and other immune-related diseases, and administering an effective amount of Kringle domain variants to animals. Additionally, the present invention relates to a method for preparing multispecific monomers and multivalent monomers by grafting target-binding loops of a Kringle domain variant into other non-binding loops of another Kringle domain variant with the same or different target binding specificity. The present invention relates to a method for constructing a protein scaffold library based on the Kringle domain structure, protein scaffold variants from the Kringle domain library, which bind to various targeted molecules to modulate their biological activities, a method for constructing homo-/hetero-oligomers which allow multi-specificity binding to multiple targets by the tandem assembly monomeric Kringle domain variants. Furthermore, a protein scaffold variant based on the Kringle domain structure that specifically binds to target molecules, DNA encoding the protein scaffold variant, or a method and composition for prevention, detection, diagnosis, treatment or relieving diseases or disorders, particularly cancers and other immune-related diseases, comprising: administering an effective amount of the related molecule to animals, preferably human. Additionally, there is provided a method for preparing multispecific monomers and multivalent monomers by grafting target-binding loops of a Kringle domain variant into non-binding loops of another Kringle domain variant with the same or different target binding specificity. Also, there is provided a method for constructing homo-/hetero-oligomers which allow multi-specificity binding to multiple targets by the tandem assembly monomeric Kringle domain variants using a linker. ![]() There are provided a Kringle domain structure, comprising: inducing artificial mutations at amino acid residues except for conserved amino acid residues that are important to maintain the structural scaffold of a Kringle domain and protein scaffold variants, based on the Kringle domain structure, which modulate the biological activities of a variety of target molecules derived from the protein scaffold library by specifically binding to the target molecules.
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