Changing stroke rehab and research worldwide now.Time is Brain! trillions and trillions of neurons that DIE each day because there are NO effective hyperacute therapies besides tPA(only 12% effective). I have 523 posts on hyperacute therapy, enough for researchers to spend decades proving them out. These are my personal ideas and blog on stroke rehabilitation and stroke research. Do not attempt any of these without checking with your medical provider. Unless you join me in agitating, when you need these therapies they won't be there.

What this blog is for:

My blog is not to help survivors recover, it is to have the 10 million yearly stroke survivors light fires underneath their doctors, stroke hospitals and stroke researchers to get stroke solved. 100% recovery. The stroke medical world is completely failing at that goal, they don't even have it as a goal. Shortly after getting out of the hospital and getting NO information on the process or protocols of stroke rehabilitation and recovery I started searching on the internet and found that no other survivor received useful information. This is an attempt to cover all stroke rehabilitation information that should be readily available to survivors so they can talk with informed knowledge to their medical staff. It lays out what needs to be done to get stroke survivors closer to 100% recovery. It's quite disgusting that this information is not available from every stroke association and doctors group.

Thursday, January 19, 2017

Effect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bFGF release

Earlier research suggests that bFGF is useful for stroke. What the fuck will your doctor do with this new information to help your recovery?  Or will s/he continue to sit on their asses doing nothing with new research? Call the hospital president if such incompetency is displayed. Oops, once again telling Drs. and PhDs what needs to be done, thinking that my stroke-addled brain knows more about this stuff than they do.

Potential Usefulness of Basic Fibroblast Growth Factor as a Treatment for Stroke

written in 1999

 

The possible delivery mechanism here:

Effect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bFGF release

Authors Liu YF, Zhang L, Wei W
Received 12 October 2016
Accepted for publication 2 January 2017
Published 18 January 2017 Volume 2017:12 Pages 659—670
DOI https://doi.org/10.2147/IJN.S124523
Checked for plagiarism Yes
Review by Single-blind
Peer reviewers approved by Dr Chang Liu
Peer reviewer comments 2
Editor who approved publication: Dr Lei Yang
Yanfei Liu, Ling Zhang, Wei Wei

Key Laboratory of Cell Engineering of Guizhou Province, Affiliated Hospital of Zunyi Medical College, Zunyi, Guizhou, People’s Republic of China

Abstract:
Peptide self-assembly is one of the promising bottom-up approaches for creating synthetic supermolecular architectures. Noncovalent interactions such as hydrophobic packing, electrostatic interaction, and polypeptide chain entropy (ΔSC) are the most relevant factors that affect the folding and self-assembly of peptides and the stability of supermolecular structures. The GVGV tetrapeptide is an abundant repeat in elastin, an extracellular matrix protein. In this study, four GVGV-containing peptides were designed with the aim of understanding the effects of these weak interactions on peptide self-assembly. Transmission electron microscopy, circular dichroism spectroscopy, dynamic light scattering measurements, and rheometry assays were used to study the structural features of the peptides. Because self-assembling peptides with different amino acid sequences may significantly affect protein release, basic fibroblast growth factor (bFGF) was used as a model molecule and encapsulated within the P2 (RLDLGVGVRLDLGVGV) hydrogel to study the release kinetics. The results showed that the balance among hydrophobic effects, electrostatic interactions, and chain entropy determined the molecular state and self-assembly of the peptide. Moreover, encapsulation of bFGF within the P2 hydrogel allowed its sustained release without causing changes in the secondary structure. The release profiles could be tuned by adjusting the P2 hydrogel concentration. Cell Counting Kit-8 and Western blot assays demonstrated that the encapsulated and released bFGFs were biologically active and capable of promoting the proliferation of murine fibroblast NIH-3T3 cells, most likely due to the activation of downstream signaling pathways.

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