Response to: "Comment on ‘Production of multivalent protein binders using a self-trimerization collagen-like peptide scaffold’" Min-Yuan Chou 1 Biomedical Engineering Research Laboratories, Industrial Technology Research Institute, Taiwan 1 Correspondence: E-mail: minyuanc@itri.org.tw I am writing in response to the concerns expressed by Dr. Cuestra and colleagues regarding not citing their work in our recently published manuscript. First, I would like to differentiate their work published in The International Journal of Cancer from ours. As found in the first paragraph under the "Discussion" section of our paper, we have pointed out that many researchers used different trimerizing domains, including the C-terminal non-collagenous (NC1) domain of collagens (in the case of Cuestra et al. , the NC1 domain of type XVIII collagen; others were derived from the C-propeptide of fibrillar collagens), to drive the trimerization of its fusion partners (antibody fragments, cytokines, growth factors, et al. ). In contrast, we adopted a novel approach by using a short self-trimerizing collagen-like peptide to fulfill the art. This was based on the finding of our previous work, in which the formation of the triple-helical structure of type XXI collagen is governed by the C-terminal collagenous (COL1) domain and the content of hydroxyproline in
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