52. Pande J, Szewczyk MM, Grover AK (2010) Phage display: concept, innovations, applications
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53. Kabir S (2002) Immunoglobulin purification by affinity chromatography using protein A
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54. Li R, Dowd V, Stewart DJ, Burton SJ, Lowe CR (1998) Design, synthesis, and application of a
protein A mimetic. Nat Biotechnol 16:190–195
55. Menegatti S, Bobay BG, Ward KL, Islam T, Kish WS, Naik AD, Carbonell RG (2016) Design
of protease-resistant peptide ligands for the purification of antibodies from human plasma.
J Chromatogr A 1445:93–104
56. Tu Z, Xu Y, Fu J, Huang Z, Wang Y, Liu B, Tao Y (2015) Preparation and characterization of
novel IgG affinity resin coupling anti-Fc camelid single-domain antibodies. J Chromatogr B
983–984:26–31
57. Ellington AD, Szostak JW (1990) In vitro selection of RNA molecules that bind specific
ligands. Nature 346:818–822
58. Ghosh G, Huang DB, Huxford T (2004) Molecular mimicry of the NF-kappaB DNA target site
by a selected RNA aptamer. Curr Opin Struct Biol 14:21–27
59. Blank M, Blind M (2005) Aptamers as tools for target validation. Curr Opin Chem Biol
9:336–342
60. Romig TS, Bell C, Drolet DW (1999) Aptamer affinity chromatography: combinatorial
chemistry applied to protein purification. J Chromatogr B 731:275–284
61. Forier C, Boschetti E, Ouhammouch M, Cibiel A, Ducongé F, Nogré M, Tellier M, Bataille D,
Bihoreau N, Santambien P, Chtourou S, Perret G (2017) DNA aptamer affinity ligands
for highly selective purification of human plasma-related proteins from multiple sources.
J Chromatogr 1489:39–50
62. Beloborodov SS, Bao J, Krylova SM, Shala-Lawrence A, Johnson PE, Krylov SN (2018)
Aptamer facilitated purification of functional proteins. J Chromatogr B 1073:201–206
63. Tuerk C, Gold L (1990) Systematic evolution of ligands by exponential enrichment: RNA
ligands to bacteriophage T4 DNA polymerase. Science 249:505–510
64. Lorenz C, von Pelchrzim F, Schroeder R (2006) Genomic systematic evolution of ligands by
exponential enrichment (Genomic SELEX) for the identification of protein-binding RNAs
independent of their expression levels. Nat Protoc 1:2204–2212
65. Peselis A, Serganov A (2014) Structure and function of pseudoknots involved in gene
expression control. Wiley Interdiscip Rev RNA 5:803–822
66. Svoboda P, Di Cara A (2006) Hairpin RNA: a secondary structure of primary importance. Cell
Mol Life Sci 63:901–908
67. Li W, Ma B, Shapiro B (2001) Molecular dynamics simulations of the denaturation and
refolding of an RNA tetraloop. J Biomol Struct Dyn 19:381–396
68. Katahira M, Moriyama K, Kanagawa M, Saeki J, Kim MH, Nagaoka M, Ide M, Uesugi S,
Kono T (1995) RNA quadruplex containing g and a. Nucleic Acids Symp Ser 34:197–198
69. Turner DH, Sugimoto N, Freier SM (1990) Thermodynamics and kinetics of base-pairing of
DNA and RNA self-assembly and helix coil transition. Nucleic acids. Springer-Verlag, Berlin,
pp 201–227
70. Gruenewald B, Nicola CU, Lusitg A, Schwarz G, Klump H (1979) Kinetics of the helix-coil
transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation
measurements. Biophys Chem 9:137–147
71. Rother K, Rother M, Boniecki M, Puton T, Bujnicki JM (2011) RNA and protein 3D structure
modeling: similarities and differences. J Mol Model 17:2325–2336
72. Laing C, Schlick T (2010) Computational approaches to 3D modeling of RNA. J Phys
Condens Matter 22:283101
73. Lorenz R, Wolfinger MT, Tanzer A, Hofacker IL (2016) Predicting RNA secondary structures
from sequence and probing data. Methods 103:86–98
74. Sun LZ, Zhang D, Chen SJ (2017) Theory and modeling of RNA structure and interactions
with metal ions and small molecules. Annu Rev Biophys 46:227–246
Aptamer-Based Affinity Chromatography for Protein Extraction and Purification
133
and future. Biotechnol Adv 28:849–858
53. Kabir S (2002) Immunoglobulin purification by affinity chromatography using protein A
mimetic ligands prepared by combinatorial chemical synthesis. Immunol Invest 31:263–278
54. Li R, Dowd V, Stewart DJ, Burton SJ, Lowe CR (1998) Design, synthesis, and application of a
protein A mimetic. Nat Biotechnol 16:190–195
55. Menegatti S, Bobay BG, Ward KL, Islam T, Kish WS, Naik AD, Carbonell RG (2016) Design
of protease-resistant peptide ligands for the purification of antibodies from human plasma.
J Chromatogr A 1445:93–104
56. Tu Z, Xu Y, Fu J, Huang Z, Wang Y, Liu B, Tao Y (2015) Preparation and characterization of
novel IgG affinity resin coupling anti-Fc camelid single-domain antibodies. J Chromatogr B
983–984:26–31
57. Ellington AD, Szostak JW (1990) In vitro selection of RNA molecules that bind specific
ligands. Nature 346:818–822
58. Ghosh G, Huang DB, Huxford T (2004) Molecular mimicry of the NF-kappaB DNA target site
by a selected RNA aptamer. Curr Opin Struct Biol 14:21–27
59. Blank M, Blind M (2005) Aptamers as tools for target validation. Curr Opin Chem Biol
9:336–342
60. Romig TS, Bell C, Drolet DW (1999) Aptamer affinity chromatography: combinatorial
chemistry applied to protein purification. J Chromatogr B 731:275–284
61. Forier C, Boschetti E, Ouhammouch M, Cibiel A, Ducongé F, Nogré M, Tellier M, Bataille D,
Bihoreau N, Santambien P, Chtourou S, Perret G (2017) DNA aptamer affinity ligands
for highly selective purification of human plasma-related proteins from multiple sources.
J Chromatogr 1489:39–50
62. Beloborodov SS, Bao J, Krylova SM, Shala-Lawrence A, Johnson PE, Krylov SN (2018)
Aptamer facilitated purification of functional proteins. J Chromatogr B 1073:201–206
63. Tuerk C, Gold L (1990) Systematic evolution of ligands by exponential enrichment: RNA
ligands to bacteriophage T4 DNA polymerase. Science 249:505–510
64. Lorenz C, von Pelchrzim F, Schroeder R (2006) Genomic systematic evolution of ligands by
exponential enrichment (Genomic SELEX) for the identification of protein-binding RNAs
independent of their expression levels. Nat Protoc 1:2204–2212
65. Peselis A, Serganov A (2014) Structure and function of pseudoknots involved in gene
expression control. Wiley Interdiscip Rev RNA 5:803–822
66. Svoboda P, Di Cara A (2006) Hairpin RNA: a secondary structure of primary importance. Cell
Mol Life Sci 63:901–908
67. Li W, Ma B, Shapiro B (2001) Molecular dynamics simulations of the denaturation and
refolding of an RNA tetraloop. J Biomol Struct Dyn 19:381–396
68. Katahira M, Moriyama K, Kanagawa M, Saeki J, Kim MH, Nagaoka M, Ide M, Uesugi S,
Kono T (1995) RNA quadruplex containing g and a. Nucleic Acids Symp Ser 34:197–198
69. Turner DH, Sugimoto N, Freier SM (1990) Thermodynamics and kinetics of base-pairing of
DNA and RNA self-assembly and helix coil transition. Nucleic acids. Springer-Verlag, Berlin,
pp 201–227
70. Gruenewald B, Nicola CU, Lusitg A, Schwarz G, Klump H (1979) Kinetics of the helix-coil
transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation
measurements. Biophys Chem 9:137–147
71. Rother K, Rother M, Boniecki M, Puton T, Bujnicki JM (2011) RNA and protein 3D structure
modeling: similarities and differences. J Mol Model 17:2325–2336
72. Laing C, Schlick T (2010) Computational approaches to 3D modeling of RNA. J Phys
Condens Matter 22:283101
73. Lorenz R, Wolfinger MT, Tanzer A, Hofacker IL (2016) Predicting RNA secondary structures
from sequence and probing data. Methods 103:86–98
74. Sun LZ, Zhang D, Chen SJ (2017) Theory and modeling of RNA structure and interactions
with metal ions and small molecules. Annu Rev Biophys 46:227–246
Aptamer-Based Affinity Chromatography for Protein Extraction and Purification
133