Avid Bioservices Inc (CDMO)

[biopharm]

Indeed, it has been found
that membranes composed of anionic phospholipids (such as
phosphatidylserine and phosphatidyglycerol) catalyze the
formation of amyloids.
...
...

Sunrise trial with Bavituximab a PS Targeting mab worked as expected ...just as Biogens PS Targeting drug worked as expected ....did some IDMC try to tell Biogen it would fail as the IDMC told Peregrine? Merck knows

Why would multiple Big Pharmas work against not exposing PS Targeting IP?

What illegal intentions would Oncologie Inc have with Ampersand Capital?

Biogen now has a PS Targeting drug, as it breaks the blood brain barrier and IP assets are on the line ...

It has been known for a long time amyloids caused due to flipped PS and Biogen not being requested to prove MOA?


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Formation of amyloid fibers triggered by phosphatidylserine-containing membranes.

Zhao H, et al. Biochemistry. 2004.

Authors
Zhao H1,
Tuominen EK,
Kinnunen PK.

Author information

1
Helsinki Biophysics and Biomembrane Group, Institute of Biomedicine, P.O. Box 63 (Haartmaninkatu 8), University of Helsinki, FIN-00014 Helsinki, Finland.
Citation

Abstract
Protein misfolding has been shown to be the direct cause of a number of highly devastating diseases such as Alzheimer's disease, Parkinson's disease, and Creutzfeldt-Jacob syndrome, affecting the aging population globally. The deposition in tissues of amyloid fibrils is a characteristic of all these diseases, and the mechanisms by which these protein aggregates form continue to be intensively investigated. In only a fraction of cases is an underlying mutation responsible, and accordingly, what initiates amyloid formation in vivo is the major question that is addressed. In this study, we show that membranes containing phosphatidylserine (PS), a negatively charged phospholipid, induce a rapid formation of fibers by a variety of proteins, viz., lysozyme, insulin, glyceraldehyde-3-phosphate dehydrogenase, myoglobin, transthyretin, cytochrome c, histone H1, and alpha-lactalbumin. Congo red staining of these fibers yields the characteristic light green birefringence of amyloid, and fluorescent lipid tracers further reveal them to include phospholipids. Our results suggest that PS as well as other acidic phospholipids could provide the physiological low-pH environment on cellular membranes, enhancing protein fibril formation in vivo. Interestingly, all the proteins mentioned above either are cytotoxic or induce apoptosis. PS-protein interaction could be involved in the mechanism of cytotoxicity of the aggregated protein fibrils, perturbing membrane functions. Importantly, our results suggest that this process induced by acidic phospholipids may provide an unprecedented and generic connection between three current major areas of research: (i) mechanism(s) triggering amyloid formation, (ii) cytotoxicity of amyloidal protein aggregates, and (iii) mechanism(s) of action of cytotoxic proteins.

https://www.ncbi.nlm.nih.gov/m/pubmed/15301528/