Molecular imprinted particles for lysozyme purification

Odabaşı, Mehmet; Say, Rıdvan; Deni̇zli̇, Adil

doi:10.1016/j.msec.2006.03.002

Cited by 93 publications

(36 citation statements)

References 29 publications

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“…The conformation of a protein is quite flexible, and while an imprint of the protein is made in one position, it may be difficult for another molecule of the same type to perfectly fit that original shape [2]. In addition, a protein's large molecular size, fragility, and complexity create difficulties in imprinting [17].…”

Section: Discussionmentioning

confidence: 99%

Protein binding to peptide-imprinted porous silica scaffolds

Brown

Puleo

2008

Chemical Engineering Journal

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Of the many types of biomolecules used for molecular imprinting applications, proteins are some of the most useful, yet challenging, templates to work with. One method, termed the 'epitope approach', involves imprinting a short peptide fragment of the protein into the polymer to promote specific adsorption of the entire protein, similar to the way an antigen binds to an antibody via the epitope. Whole lysozyme or the 16 residue lysozyme C peptide was imprinted into porous silica scaffolds using sol-gel processing. After removing template, scaffolds were exposed to lysozyme and/or RNase A, which was used as a competitor molecule of comparable size. When comparing protein-to peptideimprinted scaffolds, similar amounts of lysozyme and RNase were bound from single protein solutions. However, while whole lysozyme-imprinted scaffolds showed about 4:1 preferential binding of lysozyme to RNase, peptide-imprinted scaffolds failed to show statistical significance, even though a slight preferential binding trend was present. These initial studies suggest there is potential for using peptide-imprinting to create specific protein-binding sites on porous inorganic surfaces, although further development of the materials is needed.

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Section: Discussionmentioning

confidence: 99%

Protein binding to peptide-imprinted porous silica scaffolds

Brown

Puleo

2008

Chemical Engineering Journal

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“…4c and d) and the binding parameters are given in Table S3. This revealed a single straight line and implied the presence of homogeneous binding sites in the polymers (33). The equilibrium dissociation constant of insulin (K d ) of insulin binding to MIP2 (3.049 μmol L ) and clearly indicated the formation of uniform recognition sites (34).…”

Section: Binding Isothermsmentioning

confidence: 91%

Biomimetic insulin-imprinted polymer nanoparticles as a potential oral drug delivery system

2017

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In this study, we investigate molecularly imprinted polymers (MIPs), which form a three-dimensional image of the region at and around the active binding sites of pharmaceutically active insulin or are analogous to b cells bound to insulin. This approach was employed to create a welldefined structure within the nanospace cavities that make up functional monomers by cross-linking. The obtained MIPs exhibited a high adsorption capacity for the target insulin, which showed a significantly higher release of insulin in solution at pH 7.4 than at pH 1.2. In vivo studies on diabetic Wistar rats showed that the fast onset within 2 h is similar to subcutaneous injection with a maximum at 4 h, giving an engaged function responsible for the duration of glucose reduction for up to 24 h. These MIPs, prepared as nanosized material, may open a new horizon for oral insulin delivery.

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“…Also, it could be interacted with positively charged Ni(II) metal ions easily via electrostatic interactions. So, the precomplexation step of polymerization procedure is the crucial step, because the selected medium affected the threedimensional structure memory of the molecular imprinted polymers (Peng et al, 2004;Odabasi et al, 2007). In this manner, the shape memory of the MICC worked better at pH 7.4, rather than the other pH values (Striegler, 2004).…”

Section: Adsorption Studiesmentioning

confidence: 99%

Molecularly imprinted composite cryogels for hemoglobin depletion from human blood

Baydemir

Andaç

Perçin

et al. 2014

J of Molecular Recognition

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A molecularly imprinted composite cryogel (MICC) was prepared for depletion of hemoglobin from human blood prior to use in proteome applications. Poly(hydroxyethyl methacrylate) based MICC was prepared with high gel fraction yields up to 90%, and characterized by Fourier transform infrared spectrophotometer, scanning electron microscopy, swelling studies, flow dynamics and surface area measurements. MICC exhibited a high binding capacity and selectivity for hemoglobin in the presence of immunoglobulin G, albumin and myoglobin. MICC column was successfully applied in fast protein liquid chromatography system for selective depletion of hemoglobin for human blood. The depletion ratio was highly increased by embedding microspheres into the cryogel (93.2%). Finally, MICC can be reused many times with no apparent decrease in hemoglobin adsorption capacity.

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Molecular imprinted particles for lysozyme purification

Cited by 93 publications

References 29 publications

Protein binding to peptide-imprinted porous silica scaffolds

Protein binding to peptide-imprinted porous silica scaffolds

Biomimetic insulin-imprinted polymer nanoparticles as a potential oral drug delivery system

Molecularly imprinted composite cryogels for hemoglobin depletion from human blood

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