(Total Views: 409)
Posted On: 06/24/2017 3:59:38 AM
Post# of 72446
below is a post i made on IHUB in reply to an article sox04 posted from the new IPIX website
I believe the below copied excerpt from the article you posted describes what Brilacidin is and why it works in a very easy to understand manner. Totally synthetic, cheap and easy to make, 100 times more potent than the Host Defense Protein it mimics, 1000 times more selective, and one tenth the size. Properties achieved by coarse-grain computer modeling (whatever that is).
"Brilacidin is a small, non-peptidic, fully synthetic mimic of Host Defense Proteins (HDPs), specifically defensins (pdf), that can be developed as systemic or topical agent.
An arylamide foldamer, and unlike most peptidic-based small molecules (e.g., Pexiganan), Brilacidin is not subject to the traditional shortcomings of antimicrobial peptide (AMP)-based compounds, including rapid proteolytic degradation. Instead, by using sophisticated coarse-grain computer modeling that mimicked the behavior of natural defensins (electrostatics, lipophicility, etc.), it was designed (pdfs) to be smaller (one-tenth the size) and then fine-tuned to exhibit enhanced pharmacological properties—more easily and much less expensively synthesized, more stable (a rigid backbone), more potent (by a 100-fold) and more selective (by a 1000-fold)."
I believe the below copied excerpt from the article you posted describes what Brilacidin is and why it works in a very easy to understand manner. Totally synthetic, cheap and easy to make, 100 times more potent than the Host Defense Protein it mimics, 1000 times more selective, and one tenth the size. Properties achieved by coarse-grain computer modeling (whatever that is).
"Brilacidin is a small, non-peptidic, fully synthetic mimic of Host Defense Proteins (HDPs), specifically defensins (pdf), that can be developed as systemic or topical agent.
An arylamide foldamer, and unlike most peptidic-based small molecules (e.g., Pexiganan), Brilacidin is not subject to the traditional shortcomings of antimicrobial peptide (AMP)-based compounds, including rapid proteolytic degradation. Instead, by using sophisticated coarse-grain computer modeling that mimicked the behavior of natural defensins (electrostatics, lipophicility, etc.), it was designed (pdfs) to be smaller (one-tenth the size) and then fine-tuned to exhibit enhanced pharmacological properties—more easily and much less expensively synthesized, more stable (a rigid backbone), more potent (by a 100-fold) and more selective (by a 1000-fold)."
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