Adsorption of a Formulated Protein on a Drug Delivery Device Surface

Tzannis, Stelios T.; Hrushesky, William J. M.; Wood, Patricia A.; Przybycien, Todd M.

doi:10.1006/jcis.1997.4841

Cited by 59 publications

(43 citation statements)

References 52 publications

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“…If an adsorbed protein were denatured by its interaction with the surface, then displaced at the surface by another protein and so on, a pool of inactive protein in solution would be generated if the protein could not properly refold after it left the surface. In this way, the surface would serve as a catalyst for denaturing a protein solution (Tzannis et al, 1996(Tzannis et al, , 1997.…”

Section: Reversibility and Exchangeabilitymentioning

confidence: 99%

Adsorption of poly(ethylene glycol)‐modified ribonuclease A to a poly(lactide‐co‐glycolide) surface

Daly¹,

Przybycien²,

Tilton³

2005

Biotech & Bioengineering

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Protein adsorption is a source of variability in the release profiles of therapeutic proteins from biodegradable microspheres. We employ optical reflectometry and total internal reflection fluorescence to explore the extent and kinetics of ribonuclease A (RNase A) adsorption to spin-cast films of poly(lactide-co-glycolide) (PLG) and, in particular, to determine how covalent grafting of polyethylene glycol (PEG) to RNase A affects adsorption. Adsorption kinetics on PLG surfaces are surface-limited for RNase A but transport-limited for unconjugated PEG homopolymers and for PEG-modified RNase A, indicating that PEG anchors the conjugates to the surface during the transport-limited regime. PEG modification of RNase A decreases the total number of adsorbed molecules per unit area but increases the areal surface coverage because the grafted PEG chains exclude additional surface area. Total internal reflection fluorescence-based exchange measurements show that there is no exchange between adsorbed and solution-phase protein molecules. This indicates an unusually tenacious adsorption. Streaming current measurements indicate that the zeta potential of the PLG surface becomes increasingly negative as the film is exposed to water for several weeks, as expected. Aging of the PLG surface results in increased adsorption of unmodified RNase A but decreased adsorption of unconjugated PEG homopolymers and of PEG-RNase A conjugates, relative to the extent of adsorption on freshly prepared PLG surfaces. Adsorption results correlate well with an increase in the rate, total extent and preservation of bioactivity of RNase A released from PLG microspheres for the PEG-modified version of RNase A.

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Section: Reversibility and Exchangeabilitymentioning

confidence: 99%

Adsorption of poly(ethylene glycol)‐modified ribonuclease A to a poly(lactide‐co‐glycolide) surface

Daly¹,

Przybycien²,

Tilton³

2005

Biotech & Bioengineering

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“…These methods include, but are not limited to, solitary use or combinations of factor analysis (FA) (16 -20), singular value decomposition (SVD) (21,22), Fourier self-deconvolution (FSD; or resolution enhancement) (14,(23)(24)(25)(26), second derivative (SD) band identification and fitting (27)(28)(29), and the development of spectral correlation coefficients (30,31). Recent reviews of these techniques by Pelton and McLean (32) and Jackson and Mantsch (33) are instructive.…”

Section: Fourier-transformed Infrared (Ftir)mentioning

confidence: 99%

A Holistic Approach for Protein Secondary Structure Estimation from Infrared Spectra in H2O Solutions

Vedantham

Sparks

Sane

et al. 2000

Analytical Biochemistry

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113

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“…Tzannis et al have reported that the biological activity of the delivered protein was dramatically reduced by approximately 90% after a 24-h infusion program. Examination of the secondary and tertiary structure of both adsorbed and delivered protein indicated that transient surface association of IL-2 with the catheter tubing resulted in profound, irreversible structural changes that were responsible for the bioactivity losses (7).…”

Section: Introductionmentioning

confidence: 99%

Role of a Novel Excipient Poly(Ethylene Glycol)-b-Poly(L-Histidine) in Retention of Physical Stability of Insulin in Aqueous Solutions

Taluja

Bae

2007

Pharm Res

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Adsorption of a Formulated Protein on a Drug Delivery Device Surface

Cited by 59 publications

References 52 publications

Adsorption of poly(ethylene glycol)‐modified ribonuclease A to a poly(lactide‐co‐glycolide) surface

Adsorption of poly(ethylene glycol)‐modified ribonuclease A to a poly(lactide‐co‐glycolide) surface

A Holistic Approach for Protein Secondary Structure Estimation from Infrared Spectra in H2O Solutions

Role of a Novel Excipient Poly(Ethylene Glycol)-b-Poly(L-Histidine) in Retention of Physical Stability of Insulin in Aqueous Solutions

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