First-pass extracted concept

Viresolve® Pro membrane

Candidate: toolkit item1 source documents7 linked claims
Live refresh every 5sNext refresh in 5s

Aliases

Viresolve® Pro

Extracted Explainers

What the tool is doing

Viresolve® Pro is the virus removal membrane studied in this paper. The abstract describes it as a highly asymmetric, highly selective membrane used during biopharmaceutical processing.

Source 1DOIPubMed

Resources required

Its use occurs in virus removal filtration workflows for plasma- or mammalian cell-derived biopharmaceuticals. The paper specifically studies its behavior under fouling by human serum immunoglobulin G.

Source 1DOIPubMed

What problem it solves

It is used to remove viruses during downstream processing of biopharmaceutical products.

Source 1DOIPubMed

What it does not solve

The abstract indicates that it does not inherently prevent protein fouling, which can reduce flux, capacity, and virus retention.

Source 1DOIPubMed

Evidence Snippets

We use focused ion beam (FIB) milling and scanning electron microscopy (SEM) to directly evaluate changes in 3D pore structure in a Viresolve® Pro membrane due to fouling by human serum immunoglobulin G.
Evidence 1Source 1DOIPubMedprovenance

Supporting Sources

Linked Claims

Claim 1capture location shiftsupports2025Source 1DOIPubMed

For a membrane fouled to 90% flux decline, simulations show nanoparticle capture shifts upstream by about 0.4 µm away from the filter exit.

Quoted textsource-backed
Simulations show an upstream shift in the location of nanoparticle capture (away from the filter exit) by about 0.4 µm for the membrane fouled to 90% flux decline.
Claim 2mechanistic explanationsupports2025Source 1DOIPubMed

The upstream shift in nanoparticle capture is attributed to pore constriction from protein deposition, which redistributes flow paths within the membrane.

Quoted textsource-backed
This is due to pore constriction from protein deposition, highlighting how fouling redistributes flow paths within the membrane.
Claim 3method capabilitysupports2025Source 1DOIPubMed

FIB-SEM can directly evaluate changes in 3D pore structure in a Viresolve® Pro membrane caused by human serum immunoglobulin G fouling.

Quoted textsource-backed
We use focused ion beam (FIB) milling and scanning electron microscopy (SEM) to directly evaluate changes in 3D pore structure in a Viresolve® Pro membrane due to fouling by human serum immunoglobulin G.
Claim 4model agreementsupports2025Source 1DOIPubMed

Flow and particle-transport simulations in the protein-fouled membrane agree well with independent experimental measurements of permeability and particle-capture location.

Quoted textsource-backed
Model simulations of flow and particle transport in the protein-fouled membrane are in good agreement with independent experimental measurements of the permeability and location of particle capture.
Claim 5performance impactsupports2025Source 1DOIPubMed

Protein fouling significantly reduces filtrate flux, capacity, and virus retention in virus removal filtration of plasma- or mammalian cell-derived biopharmaceuticals.

Quoted textsource-backed
Protein fouling can significantly reduce the filtrate flux, capacity, and virus retention during processing of plasma- or mammalian cell-derived biopharmaceuticals through virus removal filters.
Claim 6structural changesupports2025Source 1DOIPubMed

After fouling to 90% flux decline, porosity in the size-selective region near the exit of the Viresolve® Pro membrane decreases by approximately 40%.

Quoted textsource-backed
Protein fouling causes a significant reduction in the membrane porosity, which decreases by approximately 40% in the size-selective region near the exit of the highly asymmetric Viresolve® Pro membrane after the filter is fouled to 90% flux decline.
Claim 7structural changesupports2025Source 1DOIPubMed

Protein fouling reduces the number of small pores in the Viresolve® Pro membrane by more than a factor of two.

Quoted textsource-backed
There is a corresponding reduction in the number of small pores by more than a factor of two.