In vivo tumor targeting and imaging with engineered trivalent antibody fragments containing collagen-derived sequences.

ABSTRACT: There is an urgent need to develop new and effective agents for cancer targeting. In this work, a multivalent antibody is characterized in vivo in living animals. The antibody, termed "trimerbody", comprises a single-chain antibody (scFv) fragment connected to the N-terminal trimerization subdomain of collagen XVIII NC1 by a flexible linker. As indicated by computer graphic modeling, the trimerbody has a tripod-shaped structure with three highly flexible scFv heads radially outward oriented. Trimerbodies are trimeric in solution and exhibited multivalent binding, which provides them with at least a 100-fold increase in functional affinity than the monovalent scFv. Our results also demonstrate the feasibility of producing functional bispecific trimerbodies, which concurrently bind two diffe

SUBMITTER: Cuesta AM 

PROVIDER: S-EPMC2670539 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature