2016
DOI: 10.1016/j.chroma.2016.10.017
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Tryptophan tags and de novo designed complementary affinity ligands for the expression and purification of recombinant proteins

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Cited by 10 publications
(6 citation statements)
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“…In the years that thereafter, this Ugi-modification approach opens a new window to the combinatorial synthesis of pseudobiospecific ligands modified sepharose-supports for purification of diverse kinds of proteins, caused to several reports based on the same methodology . The synthetic ligands have been employed efficiently for mimic Protein G for the purification of mammalian immunoglobulins 72 , mimicking the third domain of Protein G (domain III) and isolate highly pure IgG and Fab fragments from mammalian and yeast cell extracts 73 , purification of recombinant human erythropoietin (rHuEPO) 74 , interacting with glycan moieties on glycoproteins 75 , purification of green fluorescent protein (GFP) or GFP fusion proteins 76 , and expression and purification of fusion proteins through “tag–receptor” affinity pair 77 . (Scheme )…”
Section: Covalent Functionalization Through Multicomponent Reactionsmentioning
confidence: 99%
“…In the years that thereafter, this Ugi-modification approach opens a new window to the combinatorial synthesis of pseudobiospecific ligands modified sepharose-supports for purification of diverse kinds of proteins, caused to several reports based on the same methodology . The synthetic ligands have been employed efficiently for mimic Protein G for the purification of mammalian immunoglobulins 72 , mimicking the third domain of Protein G (domain III) and isolate highly pure IgG and Fab fragments from mammalian and yeast cell extracts 73 , purification of recombinant human erythropoietin (rHuEPO) 74 , interacting with glycan moieties on glycoproteins 75 , purification of green fluorescent protein (GFP) or GFP fusion proteins 76 , and expression and purification of fusion proteins through “tag–receptor” affinity pair 77 . (Scheme )…”
Section: Covalent Functionalization Through Multicomponent Reactionsmentioning
confidence: 99%
“…Recently, new strategies have been developed to purify arginine-rich peptides, namely the Argi system based on the AR aptamer selected to capture Arg-based tags (K D ~ 10 −7 M) ( Table 1 and Table 2 ) [48] . The properties of several tryptophan (Trp)-based tags have also been screened for single-step purification through the development of complementary affinity ligands [49] . Pina et al [49] demonstrated that two new hexapeptide tag variants ( Table 1 ) – (NW)3 and (WF)3 – fulfill the characteristics needed for a good affinity tag and showed that their system based in “tag-receptor” affinity pairs (K D ~ 10 −7 M) works similarly to other commonly used affinity-based purification systems.…”
Section: Protein Purification/immobilization Tagsmentioning
confidence: 99%
“…The properties of several tryptophan (Trp)-based tags have also been screened for single-step purification through the development of complementary affinity ligands [49] . Pina et al [49] demonstrated that two new hexapeptide tag variants ( Table 1 ) – (NW)3 and (WF)3 – fulfill the characteristics needed for a good affinity tag and showed that their system based in “tag-receptor” affinity pairs (K D ~ 10 −7 M) works similarly to other commonly used affinity-based purification systems. Therefore, these pairs can be potentially used for protein immobilization as well.…”
Section: Protein Purification/immobilization Tagsmentioning
confidence: 99%
“…C-C and C-N bond-forming U-4CR can constitute a scaffold providing enormous molecular diversity. U-4CR protocol has been utilized in various fields of chemistry including separation science where it has been employed mainly in affinity chromatography [26][27][28][29][30][31][32][33][34][35][36][37][38][39]. Surprisingly, up to the present time, its adoption in other chromatographic modes has been rather scarce.…”
Section: Introductionmentioning
confidence: 99%