Comment on "Production of multivalent protein binders using a self-trimerization collagen-like peptide scaffold" Ángel M. Cuesta, David Sánchez-Martín, Laura Sanz and Luis Álvarez-Vallina 1 Molecular Immunology Unit, Hospital Universitario Puerta de Hierro, Madrid, Spain 1 Correspondence: E-mail: lalvarezv.hpth@salud.madrid.org The recently published manuscript by Fan et al. (1) describes the generation of multivalent antibody fragments using collagen sequence-based peptides to drive multimerization. In 2006, our group reported in The International Journal of Cancer that fusion of the N-terminal association subdomain (50 residues) of murine collagen XVIII NC1, responsible for noncovalent trimerization of collagen XVIII alpha chains, to the C-terminus of a single-chain variable fragment (scFv) confers their natural trimeric state to the fused antibody (2) . The homo-trimeric molecules were isolated in functional active form from the cell culture supernatant of gene-modified human cells and showed high stability in the presence of relevant proteinases (2) . The scFv used recognizes an angiogenesis-associated laminin epitope (3) and inhibits tumor angiogenesis and growth in vivo (4) . We demonstrated that trimeric scFv-NC1 bound to laminin, and was more effective in blocking capillary morphogenesis in vitro, and in preventing tumor growth in vivo than its monomeric version (2) . Given the wide
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Comment on "Production of multivalent protein binders using a self-trimerization collagen-like peptide scaffold"
Cuesta, Ángel M.; Sánchez-Martín, David; Sanz, Laura; Álvarez-Vallina, Luis
Follow The FASEB Journal
, Volume 22 (10): 3417
Fed of American Socs for Experimental Biology – Oct 1, 2008
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