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
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
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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