Decoupling Charge and Side Chain Effects in Hierarchical Organization of Cationic PFX Peptide and Alginate

We have successfully created self-assembled membranes by combining positively charged (Pro-X-(Phe-X)5-Pro) PFX peptides with negatively charged alginate. These PFX/alginate membranes were formed by three different peptides that contain either X = Arginine (R), Histidine (H), or Ornithine (O) as thei...

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Bibliographic Details
Published in:Biomacromolecules 2024-07, Vol.25 (7), p.4168-4176
Main Authors: Yosefi, Gal, Kass, Itamar, Rapaport, Hanna, Bitton, Ronit
Format: Article
Language:English
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Summary:We have successfully created self-assembled membranes by combining positively charged (Pro-X-(Phe-X)5-Pro) PFX peptides with negatively charged alginate. These PFX/alginate membranes were formed by three different peptides that contain either X = Arginine (R), Histidine (H), or Ornithine (O) as their charged amino acid. The assemblies were compared to membranes that were previously reported by us composed of X = lysine (K). This study enabled us to elucidate the impact of amino acids’ specific interactions on membrane formation. SEM, SAXS, and cryo-TEM measurements show that although K, R, H, and O may have a similar net charge, the specific traits of the charged amino acid is an essential factor in determining the hierarchical structure of alginate/PFX self-assembled membranes.
ISSN:1525-7797
1526-4602
1526-4602
DOI:10.1021/acs.biomac.4c00278