Particle formation during peristaltic pumping of therapeutic proteins: Hofmeister anions effectShow others and affiliations
2025 (English)In: Journal of Pharmaceutical Sciences, ISSN 0022-3549, E-ISSN 1520-6017, Vol. 114, no 4, article id 103700Article in journal (Refereed) Published
Abstract [en]
This study reveals specific ion effects on particle formation during peristaltic pumping of a monoclonal Antibody (Antibody A). For this purpose, three anions in the direct Hofmeister series were selected, ranging from the kosmotropic SO42- to the more neutral Cl- and the chaotropic SCN-. Protein particle formation during peristaltic pumping is described primarily as a surface-driven mechanism. Therefore, the effect of the anions was hypothesised to affect the particle formation with the smallest amount of protein adsorbing and the least particles formed in the presence of SCN-, followed by the highest in SO42-. The alternative hypothesis was that most protein particles would be formed in SCN- due to the lower intrinsic stability of Antibody A. On the other hand, if none of the factors dominates the particle formation, it would not necessarily follow the Hofmeister series linearly. This was shown to be the case as significantly more particles were formed in the presence of NaCl, which could be explained by the interplay of the protein’s intrinsic, colloidal, and interfacial stability. Antibody A had the highest protein adsorption in NaCl and the lowest colloidal stability compared to Na2SO4 or NaSCN, which led to the highest amount of subvisual particles formed during pumping.
Place, publisher, year, edition, pages
Elsevier B.V. , 2025. Vol. 114, no 4, article id 103700
Keywords [en]
Adsorption; Anions; Antibodies, Monoclonal; Colloids; Particle Size; Protein Stability; Sodium Chloride; Sulfates; Thiocyanates; ammonium sulfate; anion; dimeticone; histidine; monoclonal antibody; peptides and proteins; silicone; sodium chloride; sodium sulfate; monoclonal antibody; sulfate; thiocyanate sodium; thiocyanic acid derivative; adsorption; Article; colloid; differential scanning calorimetry; dispersity; drug stability; hofmeister series; micro flow imaging; osmolality; particle size; photon correlation spectroscopy; physical parameters; protein aggregation; protein protein interaction; quartz crystal microbalance; thermostability; ultraviolet radiation; chemistry; particle size; protein stability
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:ri:diva-78377DOI: 10.1016/j.xphs.2025.103700Scopus ID: 2-s2.0-85218989769OAI: oai:DiVA.org:ri-78377DiVA, id: diva2:1999451
Note
This research was funded by theSwedish Governmental Agency for Innovation Systems (VINNOVA)Research Council through the competence centre NextBioForm undergrant number 2018−04730.
2025-09-192025-09-192025-09-23Bibliographically approved