Adsorption of human insulin and AspB28 insulin on a PTFE-like surface

Mollmann, Susanne H.; Bukrinsky, Jens T.; Frøkjær, Sven; Elofsson, Ulla

doi:10.1016/j.jcis.2005.01.018

Cited by 47 publications

(53 citation statements)

References 59 publications

(77 reference statements)

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“…Here we should note that the association state of insulin, which can be affected by buffer and pH, [26][27][28][29] also, might influence the insulin adsorption. 6 …”

Section: Physicochemical Properties Of the Prepared Membranesmentioning

confidence: 99%

“…Since pain and risk for infection cannot be completely avoided in this method, novel non-invasive insulin delivery techniques such as iontophoresis have been required. [1][2][3][4][5] The adsorption of proteins on biomaterial surfaces has been widely studied, [6][7][8][9][10] and it has been identified to be very complex and can be influenced by a lot of factors such as electrostatic interactions and hydrophilicity/hydrophobicity. Protein adsorption on membranes not only could change the pore size and charge property of the membrane but also could give valuable information for the study of the protein transport mechanism within the membrane.…”

mentioning

confidence: 99%

“…Protein adsorption on membranes not only could change the pore size and charge property of the membrane but also could give valuable information for the study of the protein transport mechanism within the membrane. 6,11,12 There have been, however, few reports on the relationship between insulin adsorption on and transport through a membrane for the drug delivery. It is of great interest to study the insulin adsorption behavior on the charged membranes for the administration of insulin release.…”

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confidence: 99%

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Characterization of Insulin Adsorption Behavior on Amphoteric Charged Membranes

Zhang

Saito

Matsumoto

et al. 2008

Polym J

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With view to develop an amphoteric charged membrane for drug delivery, we have studied the adsorption of insulin on it. In the present study, the amphoteric charged membranes were prepared by pore-surface modification of porous poly(acrylonitrile) (PAN) membranes by grafting with acrylic acid (AAc) and/or N,N-(dimethylamino)propyl acrylamide (DMAPAA). Their surface charge properties and the insulin adsorption behaviors were investigated by zeta potential measurement and UV spectrophotoscopy, respectively, at different pHs. The equilibrium adsorbed amount of insulin correlates well with the charge properties of the membranes and insulin, which indicates that electrostatic interaction played an important role in the insulin adsorption. In addition, adsorption kinetics changed from a Fickian mode to a non-Fickian one when adsorbed amount increased to very high values.KEY WORDS: Insulin / Poly(acrylonitrile) / Amphoteric Charged Membrane / Zeta Potential / Adsorption / Insulin is a polypeptide hormone produced by the pancreatic cells, and regulates carbohydrate homeostasis. Currently, the administration of insulin through parenteral injection (e.g., subcutaneous injection) is the commonest therapy of diabetes. Since pain and risk for infection cannot be completely avoided in this method, novel non-invasive insulin delivery techniques such as iontophoresis have been required.

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“…Here we should note that the association state of insulin, which can be affected by buffer and pH, [26][27][28][29] also, might influence the insulin adsorption. 6 …”

Section: Physicochemical Properties Of the Prepared Membranesmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Characterization of Insulin Adsorption Behavior on Amphoteric Charged Membranes

Zhang

Saito

Matsumoto

et al. 2008

Polym J

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“…Hydrophobic and electrostatic interactions are known to be involved in the mechanism of protein adsorption on interfaces. 24,25) It is therefore probable that hydrophobic interactions are involved in filgrastim adsorption on infusion sets. Figure 5 is a representation of the assumed filgrastim adsorption process on infusion sets.…”

Section: Resultsmentioning

confidence: 99%

Comparison of the Adsorption of Original and Biosimilar Preparations of Filgrastim on Infusion Sets and the Inhibition of Adsorption by Polysorbate 80

Tange

Matsumoto

Yoshida

et al. 2017

CHEMICAL & PHARMACEUTICAL BULLETIN

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The purpose of the study was to evaluate the adsorption of filgrastim on infusion sets (comprising infusion bag, line and filter) and to compare the adsorption of the original filgrastim preparation with biosimilar preparations using HPLC. The inhibitory effect of polysorbate 80 on this adsorption was also evaluated. Filgrastim was mixed with isotonic sodium chloride solution or 5% (w/v) glucose solution in the infusion fluid. Filgrastim adsorption on infusion sets was observed with all preparations and with both types of infusion solution. The adsorption ratio was about 30% in all circumstances. Filgrastim adsorption on all parts of the infusion set (bag, line and filter) was dramatically decreased by the addition of polysorbate 80 solution at concentrations at or over its critical micelle concentration (CMC). The filgrastim adsorption ratio was highest at a solution pH of 5.65, which is the isoelectric point (pI) of filgrastim. This study showed that the degree of filgrastim adsorption on infusion sets is similar for original and biosimilar preparations, but that the addition of polysorbate 80 to the infusion solution at concentrations at or above its CMC is effective in preventing filgrastim adsorption. The addition of a total-vitamin preparation with a polysorbate 80 concentration over its CMC may be an effective way of preventing filgrastim adsorption on infusion sets. Key words filgrastim; adsorption; infusion set; polysorbate 80The Japanese government now actively promotes the use of generic drugs in order to reduce national medical expenditure.1) As part of the drive to reduce health costs, biosimilar preparations are also beginning to be used in clinical practice in place of original biologicals. However, there are growing concerns about switching from the original preparation to biosimilar preparations in clinical practice.2) In contrast to generic preparations, it is widely considered to be impossible to make biosimilar preparations with identical biophysical properties to the original preparations. The uptake of biosimilar preparations has not been as rapid as the change to generic preparations as switching to a biosimilar preparation does not result in as much cost savings as switching to a generic preparation, bio-pharmaceuticals also being covered by high-cost illness insurance.Filgrastim is a granulocyte colony-stimulating factor used to treat neutropenia. Generally, filgrastim is administered subcutaneously but in patients with a known bleeding disorder, intravenous infusions may be required. In previous reports, original and biosimilar preparations of filgrastim have been shown to have similar clinical effects. [3][4][5] In previous reports, it has been demonstrated that protein preparations, such as insulin, adsorb to infusion sets, 6-8) and filgrastim adsorption on infusion sets has also been reported.9-13) Thus, it is possible that the actual dose of filgrastim infused will be smaller than the theoretical dose predicted. Yagi and Kawa have also found that differences in flow rate affect the ...

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“…The insulin monomer, which exposes lateral hydrophobic residues, interacts more readily with hydrophobic surfaces, which leads to its denaturation [31][32][33][34]. Modification of critical amino acids in the B-chain, either decreases (Asp28 and/or Pro29, [35,36]) or increases (Glu13Gln, [37,38]) the stability of the oligomeric forms. In the case of protein mixtures, a situation often encountered is the kinetic competition between several proteins on the material surfaces, which results in the 'Vroman' effect [39].…”

Section: 3mentioning

confidence: 99%

Protein conformational changes induced by adsorption onto material surfaces: an important issue for biomedical applications of material science

Ballet¹,

Boulangé²,

Bréchet³

et al. 2010

Bulletin of the Polish Academy of Sciences: Technical Sciences

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Abstract. Protein adsorption on solid surfaces is a widespread phenomenon of large biological and biotechnological significance. Conformational changes are likely to accompany protein adsorption, but are difficult to evidence directly. Nevertheless they have important consequences, since the partial unfolding of protein domains can expose hitherto hidden amino acids. This remodeling of the protein surface can trigger the activation of molecular complexes such as the blood coagulation cascade or the innate immune complement system. In the case of extracellular matrix, it can also change the way cells interact with the material surfaces and result in modified cell behavior. In this review, we present direct and indirect evidences that support the view that some proteins change their conformation upon adsorption. We also show that both physical and chemical methods are needed to study the extent and kinetics of protein conformational changes. In particular, AFM techniques and cryo-electron microscopy provide useful and complementary information. We then review the chemical and topological features of both proteins and material surfaces in relation with protein adsorption. Mutating key amino acids in proteins changes their stability and this is related to material-induced conformational changes, as shown for instance with insulin. In addition, combinatorial methods should provide valuable information about peptide or antibody adsorption on well-defined material surfaces. These techniques could be combined with molecular modeling methods to decipher the rules governing conformational changes associated with protein adsorption.

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Adsorption of human insulin and AspB28 insulin on a PTFE-like surface

Cited by 47 publications

References 59 publications

Characterization of Insulin Adsorption Behavior on Amphoteric Charged Membranes

Characterization of Insulin Adsorption Behavior on Amphoteric Charged Membranes

Comparison of the Adsorption of Original and Biosimilar Preparations of Filgrastim on Infusion Sets and the Inhibition of Adsorption by Polysorbate 80

Protein conformational changes induced by adsorption onto material surfaces: an important issue for biomedical applications of material science

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