Purification of recombinant human interferon-β by immobilized antisense peptides

Scapol, L.; Rappuoli, P.; Viscomi, G. C.

doi:10.1016/0021-9673(92)85553-6

Cited by 31 publications

(15 citation statements)

References 31 publications

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“…The authors believed that this matrix presented an ideal sorbent for isolation of glycoconjugates. Instead of labile and expensive protein molecules, more stable peptides mimicking a protein domain responsible for the formation of specific pair are widely used as highly specific affinity ligands [103,104]. The typical procedure for preparation of peptidyl sorbents includes: (i) peptide synthesis, (ii) its isolation, purification, and analysis, and, finally, (ii) its covalent attachment to the solid support.…”

Section: Surface Modificationmentioning

confidence: 99%

Preparation of methacrylate monoliths

Влах

Tennikova²

2007

J of Separation Science

151

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Rigid macroporous polymers developed in the early 1990s are widely used as efficient stationary phases for all types of chromatographic separations. The main advantages of so-called monolithic supports are their high hydraulic permeability and the dominance of the convection over the diffusion mechanism of mass-exchange under dynamic conditions that allow the separation to be carried out at extremely high flow rates and, consequently, during very short operation times. Among other types of macroporous polymers, the methacrylate-based monolithic materials represent the most popular and successfully explored class of sorbents. This review is an attempt to collect together the contributions of different groups working in the area of monolith preparation. Examples of different methcrylate monomers and crosslinkers, as well as porogenic solvents, including polymer ones, used in monolith preparation are discussed.

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Section: Surface Modificationmentioning

confidence: 99%

Preparation of methacrylate monoliths

Влах

Tennikova²

2007

J of Separation Science

151

View full text Add to dashboard Cite

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“…Therapeutic value of interferons against certain types of tumors such as brain tumors and malignant melanomas caused both increasing interest in these proteins [23] and more focusing on investigations aimed to obtain treated and purified interferons [24]. The purification of human interferons from various sources has been attempted by a variety of methods including metal-chelation, precipitation, cation or anion-exchange, gel filtration, hydrophobic and immunoaffinity chromatography over many years and some protocols have been proposed that yield homogenous protein [25][26][27][28][29].…”

Section: Introductionmentioning

confidence: 99%

Evaluation of human interferon adsorption performance of Cibacron Blue F3GA attached cryogels and interferon purification by using FPLC system

Doğan

Özkara

Sarı

et al. 2012

Journal of Chromatography B

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“…Different from our previous method, a fragment of a native protein, fragment 1-14 of hIFN-β was selected as sense peptide. In 1992, Scapol et al [7] demonstrated the specific recognition between hIFN-β and its corresponding antisense peptides. Three antisense peptides encoded by the antisense strands of DNA corresponding to the 1-14, 42-54 and 103-115 fragments of hIFN-β were applied in the purification of hIFN-β.…”

Section: Design Of Sense Peptide and Antisense Peptidesmentioning

confidence: 98%

“…As such interaction is specific and selective, its application in affinity technology has been widely achieved. For example, antisense peptide-immobilized chromatographic supports have been employed to isolate native proteins like recombinant c-raf protein [5] , the Arg 8 -vasopressin-receptor complex [6] and human interferon-β [7] . Moreover, Davids et al [8] developed antisense peptides as the selective inhibitors of cytokine interleukin I in 1997.…”

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confidence: 99%

Study on peptide-peptide interaction using high-performance affinity chromatography and quartz crystal microbalance biosensor

et al. 2007

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The specific interaction between sense and antisense peptides was studied by high-performance affinity chromatography (HPAC) and quartz crystal microbalance (QCM) biosensor. Fragment 1-14 of human interferon-β (hIFN-β) was chosen as sense peptide and its three antisense peptides (AS-IFN 1, AS-IFN 2, and AS-IFN 3) were designed according to the degeneracy of genetic codes. The affinity column was prepared with sense peptide as ligand and the affinity chromatographic behavior was evaluated. Glu-substituted antisense peptide (AS-IFN 3) showed the strongest binding to immobilized sense peptide at pH 7.5. A quartz crystal microbalance-flow injection analysis (QCM-FIA) system was introduced to investigate the recognition process in real-time. The equilibrium dissociation constants between sense peptide and AS-IFN 1, AS-IFN 2 and AS-IFN 3 measured 2.08×10 −4 , 1.31×10 −4 and 2.22× 10 −5 mol/L, respectively. The mechanism study indicated that the specific recognition between sense peptide and AS-IFN 3 was due to sequence-dependent and multi-modal affinity interaction.antisense peptide, degeneracy, high-performance affinity chromatography, quartz crystal microbalance biosensor, human interferon-β Antisense peptides are the analogical equivalent of antisense oligonucleotides. By definition, a sense peptide is coded by the nucleotide sequence of the sense (positive) strand of DNA. Conversely, an antisense peptide is coded by the nucleotide sequence of the antisense (negative) strand of DNA. Usually the antisense strand of DNA cannot be translated in almost all organisms, but they can be synthesized chemically. As predicted by Mekler [1] and first shown experimentally by Bost et al. [2] , an antisense peptide could interact with the corresponding sense peptide at some degree of selectivity. The interaction between sense and antisense peptides has been reported [3,4] . As such interaction is specific and selective, its application in affinity technology has been widely achieved. For example, antisense peptide-immobilized chromatographic supports have been employed to isolate native proteins like recombinant c-raf protein [5] , the Arg 8 -vasopressin-receptor complex [6] and human interferon-β [7] . Moreover, Davids et al. [8] developed antisense peptides as the selective inhibitors of cytokine interleukin I in 1997. Since then, antisense peptides have been designed and selected as inhibitors of cytokine interleukin-1β [9] , interleukin 18 [10] and β-amyloid peptide 1-40 [11] . In our previous work, the inhibitor of influenza A virus was designed and screened out using antisense peptide based combinatorial peptide libraries [12] .Till now, the mechanism of interactions between sense and antisense peptides has not been clarified. Two main hypotheses have been put forward to explain the specific interactions between sense peptide and antisense peptide. As defined by Heal et al. in 2002 [4] , one

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Purification of recombinant human interferon-β by immobilized antisense peptides

Cited by 31 publications

References 31 publications

Preparation of methacrylate monoliths

Preparation of methacrylate monoliths

Evaluation of human interferon adsorption performance of Cibacron Blue F3GA attached cryogels and interferon purification by using FPLC system

Study on peptide-peptide interaction using high-performance affinity chromatography and quartz crystal microbalance biosensor

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