Fluorescent supramolecular fibers and sheets built from doubly hexa-His tagged mCherry proteins conjugated by divalent metal cations.

Doubly His-tagged mCherry red fluorescent proteins are observed to form fibers and sheets at neutral pH in the presence of no more than equimolar amounts of Zn or Ni. These architectures, on the order of 10 μm in extent, are detected with scanning transmission electron microscopy imaging. Far ultraviolet circular dichroism spectroscopy attests to the preservation of the native secondary structure of mCherry, while the emission spectrum reveals the maintenance of the chemical environment of the fluorophore site.

Purification of Human Immunoglobulin G with Bathophenanthroline-Zn, -Fe, or -Cu Complexes.

Background/objectives: Pharmaceutical companies are aware of the ongoing effort to satisfy the increasing global demand for therapeutic-grade monoclonal antibodies (mAbs), an especially difficult challenge for poor and developing countries. We present a simple, economical, single-step purification approach at neutral pH for polyclonal human IgG (hIgG), which does not require any expensive ligands, chromatography columns, polymers, or membranes.

Methods/results: Instead, porous precipitates of commercial, recyclable aromatic [bathophenanthroline:cation] complexes were found to efficiently capture impurity proteins from CHO cells or lysate while maintaining the majority of the highly concentrated hIgG (5-15 mg/mL) in the supernatant.

Purification of a Fc-Fusion Protein with [Bathophenathroline:metal] Complexes.

In this study, we assess an alternative Fc-fusion protein purification method that does not rely on chromatographic media or ligands. Recombinant human acetylcholinesterase, fused to the Fc domain of human IgG1 (henceforth, AChE-Fc), was purified with precipitated aromatic complexes composed of the bathophenanthroline (henceforth, batho) chelator with either Zn or Cu ions (i.e.

The [(bathophenanthroline):Fe] complex as an aromatic non-polymeric medium for purification of human lactoferrin.

We describe a non-chromatographic, ligand-free platform for the efficient purification of recombinant human lactoferrin (LF). The platform consists of a [metal:chelator] complex precipitate in the presence of osmotically active polyethylene glycol 6000 (PEG-6000). Purification is achieved in three stages.

Conjugated Nonionic Detergent Micelles: An Efficient Purification Platform for Dimeric Human Immunoglobulin A.

The SARS-COV-2 virus is a deadly agent of inflammatory respiratory disease. Since 2020, studies have focused on developing new therapies based on galactose-rich IgA antibodies. Clinical surveys have also revealed that galactose-deficient IgA1 polymerizes in serum, producing IgA nephropathy, which is a common cause of kidney failure in young adults.

Efficient separation of IgG from IgM antibodies via conjugated surfactant micelles.

Immunoglobulin-G (IgG) (∼150 kDa) antibodies confer longer term immunity against bacterial or viral infections than the heavier IgM's (∼900 kDa), which are generally detectable in blood circulation in response to more recently acquired infections. There may be, however, a time overlap, which is problematic for diagnostic purposes, in the interests of which it is essential to separate IgM's from IgG's. We describe a purification platform, functioning at pH 6.