2020
DOI: 10.1093/nar/gkz1210
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iFLinkC: an iterative functional linker cloning strategy for the combinatorial assembly and recombination of linker peptides with functional domains

Abstract: Recent years have witnessed increasing efforts to engineer artificial biological functions through recombination of modular-organized toolboxes of protein scaffolds and parts. A critical, yet frequently neglected aspect concerns the identity of peptide linkers or spacers connecting individual domains which remain poorly understood and challenging to assemble. Addressing these limitations, iFlinkC comprises a highly scalable DNA assembly process that facilitates the combinatorial recombination of functional dom… Show more

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Cited by 58 publications
(40 citation statements)
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“…68 Alternatively, proline-rich linkers were beneficial in auto-inhibited biosensors as proline increases the rigidity and thus persistence length of the linkers. 69 Similarly, tandem repeats of small folded domains expand the reach of antibodies more efficiently than flexible linkers. 70…”
Section: Discussionmentioning
confidence: 99%
“…68 Alternatively, proline-rich linkers were beneficial in auto-inhibited biosensors as proline increases the rigidity and thus persistence length of the linkers. 69 Similarly, tandem repeats of small folded domains expand the reach of antibodies more efficiently than flexible linkers. 70…”
Section: Discussionmentioning
confidence: 99%
“…Constructs were cloned into suitable expression vectors for recombinant protein production in E. coli either on their own or as a fusion protein by means of the iFLinkC DNA assembly process. [ 35 ] The complete amino acid sequences of individual expression constructs are outlined in the Supporting Information. Porcine pancreatic α‐Amy was purchased commercially (Catalogue no.…”
Section: Methodsmentioning
confidence: 99%
“…Fusion proteins with multiple or new functions can be encoded by combining open reading frames. The length and amino acid sequence of the linker affects the activity and interaction of domains, so optimisation may be needed; linker libraries and combinatorial approaches are available (Gräwe et al, 2020;G. Li et al, 2016).…”
Section: Variants and Fusion Proteinsmentioning
confidence: 99%