The adsorption of proteins to pharmaceutical container surfaces

Burke, Catherine; Steadman, Bryan L.; Volkin, David B.; Tsai, Pei-Kuo; Bruner, Mark W.; Middaugh, C. Russell

doi:10.1016/0378-5173(92)90034-y

Cited by 43 publications

(18 citation statements)

References 6 publications

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“…Another study showed that blood contamination decreases the stability of the CSF proteome (11 ), corroborating our earlier results (21 ). One explanation for the decreased level of the 2 unidentified peaks in the proteome analysis is the possible adsorption to the vial surface, e.g., via hydrophobic or van der Waals interactions (21,33,34 ). Metabolomics revealed increased concentrations of threonic acid after storage at room temperature.…”

Section: Discussionsupporting

confidence: 73%

The Impact of Delayed Storage on the Measured Proteome and Metabolome of Human Cerebrospinal Fluid

et al. 2011

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BACKGROUND Because cerebrospinal fluid (CSF) is in close contact with diseased areas in neurological disorders, it is an important source of material in the search for molecular biomarkers. However, sample handling for CSF collected from patients in a clinical setting might not always be adequate for use in proteomics and metabolomics studies. METHODS We left CSF for 0, 30, and 120 min at room temperature immediately after sample collection and centrifugation/removal of cells. At 2 laboratories CSF proteomes were subjected to tryptic digestion and analyzed by use of nano-liquid chromatography (LC) Orbitrap mass spectrometry (MS) and chipLC quadrupole TOF-MS. Metabolome analysis was performed at 3 laboratories by NMR, GC-MS, and LC-MS. Targeted analyses of cystatin C and albumin were performed by LC–tandem MS in the selected reaction monitoring mode. RESULTS We did not find significant changes in the measured proteome and metabolome of CSF stored at room temperature after centrifugation, except for 2 peptides and 1 metabolite, 2,3,4-trihydroxybutanoic (threonic) acid, of 5780 identified peptides and 93 identified metabolites. A sensitive protein stability marker, cystatin C, was not affected. CONCLUSIONS The measured proteome and metabolome of centrifuged human CSF is stable at room temperature for up to 2 hours. We cannot exclude, however, that changes undetectable with our current methodology, such as denaturation or proteolysis, might occur because of sample handling conditions. The stability we observed gives laboratory personnel at the collection site sufficient time to aliquot samples before freezing and storage at −80 °C.

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Section: Discussionsupporting

confidence: 73%

The Impact of Delayed Storage on the Measured Proteome and Metabolome of Human Cerebrospinal Fluid

et al. 2011

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“…[10][11][12] These factors include heat stress, surface binding, and physical agitation such as stirring, shaking, and vortexing that can generate significant air/solution interfaces. 12,31,32 The interaction of proteins with solid surfaces and/or air/solution interfaces can result in denaturation or unfolding and eventual aggregation of proteins. 12,14,20,[33][34][35][36][37][38][39][40] HPV VLPs possess high surface activity and certain level of hydrophobic surface exposure.…”

Section: Mechanisms Of Hpv Vlp Aggregationmentioning

confidence: 99%

Stabilization of human papillomavirus virus-like particles by non-ionic surfactants

Shi

Sanyal

et al. 2005

Journal of Pharmaceutical Sciences

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112

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“…While the formulation of proteins remains an ongoing challenge, it has become clear that most, if not all, proteins can, in fact, be prepared in a pharmaceutically acceptable form. The most probable mechanisms of degradation of proteins have become increasingly better defined VOLKIN and MIDDAUGH 1992). This has, in turn, led to the identification of both methods of protein preparation and storage, as well as physiologically acceptable excipients that serve as starting points in most formulation efforts.…”

Section: Formulationmentioning

confidence: 99%

“…In the case of oligomeric proteins, subunit dissociation can also occur. Another problem, which sometimes appears, is adsorption of proteins to container surfaces (BURKE et al 1992). This can be either a consequence of one or more of the aforementioned processes or may simply be a reflection of the intrinsic affinity of the amphipathic surface of proteins for a variety of interfaces.…”

Section: Formulationmentioning

confidence: 99%