Measurements of water sorption enthalpy on polymer surfaces and its effect on protein adsorption

Kim, Joonyeong; Qian, Wei; Al‐Saigh, Zeki Y.

doi:10.1016/j.susc.2010.11.011

Cited by 15 publications

(4 citation statements)

References 54 publications

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“…Studies have shown that water molecules bound to PEG are structurally distinct from bulk water and partly responsible for the low protein adsorption on surfaces grafted with PEG. 32 This particular organization of water molecules could explain the decrease in γ S T observed after an increase in RH %. Water sorption isotherms also showed that 1:1 B-PEG:HPβCD particles are able to retain more water than the 1:1 L-PEG:HPβCD particles, resulting in a hysteresis loop in the isotherm for the B-PEG-based particles.…”

Section: Discussionmentioning

confidence: 95%

“…Additionally, for these particles, an increase in the RH from 0 to 40% decreased γ S T significantly, which should be beneficial for particle aerosolization. Studies have shown that water molecules bound to PEG are structurally distinct from bulk water and partly responsible for the low protein adsorption on surfaces grafted with PEG . This particular organization of water molecules could explain the decrease in γ S T observed after an increase in RH %.…”

Section: Discussionmentioning

confidence: 99%

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Evaluation of HPβCD–PEG Microparticles for Salmon Calcitonin Administration via Pulmonary Delivery

et al. 2011

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For therapeutic peptides, the lung represents an attractive, noninvasive route into the bloodstream. To achieve optimal bioavailability and control their fast rate of absorption, peptides can be protected by coprocessing with polymers such as polyethylene glycol (PEG). Here, we formulated and characterized salmon calcitonin (sCT)-loaded microparticles using linear or branched PEG (L-PEG or B-PEG) and hydroxypropyl-beta-cyclodextrin (HPβCD) for pulmonary administration. Mixtures of sCT, L-PEG or B-PEG and HPβCD were co-spray dried. Based on the particle properties, the best PEG:HPβCD ratio was 1:1 w:w for both PEGs. In the sCT-loaded particles, the L-PEG was more crystalline than B-PEG. Thus, L-PEG-based particles had lower surface free energy and better aerodynamic behavior than B-PEG-based particles. However, B-PEG-based particles provided better protection against chemical degradation of sCT. A decrease in sCT permeability, measured across Calu-3 bronchial epithelial monolayers, occurred when the PEG and HPβCD concentrations were both 1.6 wt %. This was attributed to an increase in buffer viscosity, caused by the two excipients. sCT pharmacokinetic profiles in Wistar rats were evaluated using a 2-compartment model after iv injection or lung insufflation. The maximal sCT plasma concentration was reached within 3 min following nebulization of sCT solution. L-PEG and B-PEG-based microparticles were able to increase T(max) to 20 ± 1 min and 18 ± 8 min, respectively. Furthermore, sCT absolute bioavailability after L-PEG-based microparticle aerosolization at 100 μg/kg was 2.3 times greater than for the nebulized sCT solution.

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Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Evaluation of HPβCD–PEG Microparticles for Salmon Calcitonin Administration via Pulmonary Delivery

et al. 2011

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“…Kawaguchi et al studied the adsorption of proteins onto the N -isopropylacrylamide (NIPA) gel at 298 and 313 Kthat is, below and above the LCSTand found that the adsorption amount of proteins at 313 K was larger than that at 298 K, because the protein adsorption by the NIPA gel was mainly driven by the hydrophobic interaction between them. In general, the protein adsorption onto a solid surface is determined mainly by the electrostatic and hydrophobic interactions between them and the structural stability of the protein molecule, and it is well-known that the protein desorption from the solid surface is very difficult to realize. − However, they also reported that the protein desorption from the NIPA gel can be realized only by increasing temperature from 298 K to 313 K after the proteins were adsorbed onto the gel at 298 K. To our knowledge, this is the first report on the adsorption and desorption of protein using the NIPA-based material. Although some other research groups have also conducted the protein adsorption experiments using the NIPA-based materials, − there have been no reports on protein desorption only by temperature control, except for the above-mentioned study.…”

Section: Introductionmentioning

confidence: 88%

Temperature-Swing Adsorption of Proteins in Water Using Cationic Copolymer-Grafted Silica Particles

Morisada

Namazuda

Suzuki

et al. 2011

Ind. Eng. Chem. Res.

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We have prepared silica particles grafted with poly(N-isopropylacrylamide) (PNIPA) copolymers as adsorbent for the temperature-swing adsorption of bovine serum albumin (BSA) in water, where vinylbenzyl trimethylammonium chloride (VBTA), 2-(dimethylamino)ethyl methacrylate (DMAEMA), or N,N-dimethylacrylamide (DMAA) was employed as a comonomer. The surface potentials of PNIPA-grafted and P(NIPA-co-DMAA)-grafted silica particles in water at 298 and 313 K were negative, while those of P(NIPA-co-VBTA)-grafted silica particle were positive, because VBTA is a quaternary ammonium salt and positively charged in aqueous solutions. As for the P(NIPA-co-DMAEMA)-grafted silica particle, the surface potential changed from positive to near zero with increasing temperature from 298 K to 313 K. This may be because the coil-to-globule transition of grafted copolymers leads to the dehydration and deprotonation of DMAEMA group, which is a tertiary amine and can be positively charged only in the aqueous phase. Although PNIPA-grafted and P(NIPA-co-DMAA)-grafted silica particles failed to adsorb BSA, P(NIPAco-VBTA)-grafted and P(NIPA-co-DMAEMA)-grafted silica particles adsorbed BSA, indicating that BSA is adsorbed by the electrostatic attraction between the negatively charged BSA and the positively charged copolymers on the silica surface. Moreover, P(NIPA-co-VBTA)-grafted and P(NIPA-co-DMAEMA)-grafted silica particles repeatedly adsorbed BSA at 298 K and desorbed some of the preadsorbed BSA at 313 K via the temperature-swing operation. This BSA desorption may result from the decrease in the number of the positively charged groups accessible to BSA due to the coil-to-globule transition of the grafted copolymers with increasing temperature.

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“…Intermediate water is freezable and interacts moderately with the macromolecular interface and other water molecules and affects various interactions, including cargo delivery profile, adsorption-desorption of proteins, and cell adhesion behavior. 15,16 Free water, on the other hand, refers to the water layer with minimal interaction with the macromolecular interface, predominantly featuring water-water and water-solute hydrogen bonding interactions. This proportion of water possesses the highest crystallization ability and mobility.…”

Section: Introductionmentioning

confidence: 99%

An investigation of water status in gelatin methacrylate hydrogels by means of water relaxometry and differential scanning calorimetry

Chang,

Dargaville,

Momot

et al. 2024

J. Mater. Chem. B

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Measurements of water sorption enthalpy on polymer surfaces and its effect on protein adsorption

Cited by 15 publications

References 54 publications

Evaluation of HPβCD–PEG Microparticles for Salmon Calcitonin Administration via Pulmonary Delivery

Evaluation of HPβCD–PEG Microparticles for Salmon Calcitonin Administration via Pulmonary Delivery

Temperature-Swing Adsorption of Proteins in Water Using Cationic Copolymer-Grafted Silica Particles

An investigation of water status in gelatin methacrylate hydrogels by means of water relaxometry and differential scanning calorimetry

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