Influence of surfactants upon protein/peptide adsorption to glass and polypropylene

Duncan, Michelle R.; Lee, Joanne M.; Warchol, Mark P.

doi:10.1016/0378-5173(94)00402-q

Cited by 77 publications

(57 citation statements)

References 9 publications

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“…It is well established that the driving force in protein adsorption to hydrophobic surfaces includes entropic effects through dehydration of the surface. 44 It was immediately clear from TIRF data that mAb-1 adsorption to hydrophobic surfaces was much reduced compared with (hydrophilic) silica surfaces: approaching 2 mg/m 2 compared with 5.5-12 mg/m 2 , respectively (Fig. 6).…”

Section: Discussionmentioning

confidence: 99%

Adsorption behavior of a human monoclonal antibody at hydrophilic and hydrophobic surfaces

Couston

Skoda

Uddin

et al. 2013

mAbs

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Section: Discussionmentioning

confidence: 99%

Adsorption behavior of a human monoclonal antibody at hydrophilic and hydrophobic surfaces

Couston

Skoda

Uddin

et al. 2013

mAbs

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“…Such adsorptive behavior can lead to distinct losses in the amount of macromolecule available for delivery. 25 Furthermore, the amount of peptide or protein to be incorporated within the system is dependent on the physicochemical properties of the peptide/protein and the production procedures. 26 The design of novel formulations, especially lipid-based nanoscale carriers, seems promising for the disruption of stratum corneum through the nano-bio interaction of colloidal carrier with skin lipids, protection of proteins and peptides from the external environment, and maintenance of long-term activity.…”

Section: Discussionmentioning

confidence: 99%

Effective transcutaneous immunization by antigen-loaded flexible liposome in vivo

Li¹,

Peng²,

Chen³

et al. 2011

IJN

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Background Transcutaneous vaccines have received wide attention due to their easy-to-use, needle-free, noninvasive delivery. However, the novel barrier function of stratum corneum hinders the transport of antigen and adjuvant in transcutaneous immunization. Novel nanoscale delivery systems employing, for example, liposomes and nanoparticles, have been widely investigated to overcome the penetration barrier of stratum corneum for effective transcutaneous immunization. Objective The objective of this study was to prepare two types of flexible liposomes and determine their efficacies for the transcutaneous delivery of antigen and the subsequent immune response induced in vivo. Methods Ovalbumin (OVA) liposome-based transcutaneous vaccines were prepared using reverse-phase evaporation and film-dispersion methods. Particle sizes and antigen encapsulating efficiency were then evaluated. After application to bare mouse skin, topical sites were examined for the presence of fluorescence-labeled liposome. The efficacy of the transcutaneously delivered OVA-loaded flexible liposome in activating the immune responses was investigated by detecting serum immunoglobulin G levels. The influence of an adjuvant, imiquimod, in the transcutaneous immunization was also tested. Results Two flexible liposomes with well-encapsulated OVA were successfully prepared by film-dispersion or reverse-phase evaporation methods. The sizes of the prepared flexible liposomes ranged from 200 to 400 nm. In vivo, the fluorescence-labeled liposome was detected in hair-follicle ducts, indicating that the flexible liposome can penetrate the skin barrier through the hair follicles. Upon transcutaneous administration, the OVA-encapsulated flexible liposome elicited a strong immune response similar to that of positive control (ie, OVA solution administrated by subcutaneous injection with Al(OH) 3 as an adjuvant). Co-administration of imiquimod with the OVA-loaded liposome expressed a significant enhancement on the transcutaneous immune responses. Conclusion Results of this study highlight the nanoscale formulation, flexible liposome, as a promising carrier for the transcutaneous delivery of antigen proteins. Imiquimod was shown to be an effective adjuvant as a transcutaneous immunization enhancer with the potential for transcutaneous vaccine development.

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“…[39][40][41] In addition, surfactants have been successfully used to minimize adsorption to surfaces via competitive binding. 42,43 A review of the current landscape of mAb products marketed in the United States reveals that the majority contain polysorbates. Some specific examples of mAbs formulated with PS80 include adalimumab (Humira Ò ), alemtuzumab (Campath Ò /Lemtrada TM ), rituximab (Rituxan Ò ), and tocilizumab (Actemra Ò ).…”

Section: Discussionmentioning

confidence: 99%

Development of a stable low-dose aglycosylated antibody formulation to minimize protein loss during intravenous administration

Morar-Mitrica

Puri

Sassi

et al. 2015

mAbs

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The physical and chemical integrity of a biopharmaceutical must be maintained not only during long-term storage but also during administration. Specifically for the intravenous (i.v.) delivery of a protein drug, loss of stability can occur when the protein formulation is compounded with i.v. bag diluents, thus modifying the original composition of the drug product. Here we present the challenges associated with the delivery of a low-dose, highly potent monoclonal antibody (mAb) via the i.v. route. Through parallel in-use stability studies and conventional formulation development, a drug product was developed in which adsorptive losses and critical oxidative degradation pathways were effectively controlled. This development approach enabled the i.v. administration of clinical doses in the range of 0.1 to 0.5 mg total protein, while ensuring liquid drug product storage stability under refrigerated conditions.

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Influence of surfactants upon protein/peptide adsorption to glass and polypropylene

Cited by 77 publications

References 9 publications

Adsorption behavior of a human monoclonal antibody at hydrophilic and hydrophobic surfaces

Adsorption behavior of a human monoclonal antibody at hydrophilic and hydrophobic surfaces

Effective transcutaneous immunization by antigen-loaded flexible liposome in vivo

Development of a stable low-dose aglycosylated antibody formulation to minimize protein loss during intravenous administration

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