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Updated: Mar 17, 2026

Facile Protocol for the Synthesis of Self-assembling Polyamine-based Peptide Amphiphiles PPAs and Related Biomaterials
Published on: June 25, 2018
Conjugation of biogenic and synthetic polyamines with serum proteins: A comprehensive review
P Chanphai1, T J Thomas2, H A Tajmir-Riahi1
1Department of Chemistry, Biochemistry and Physics, University of Québec at Trois-Rivières, C. P. 500, Trois-Rivières, Québec G9A 5H7,Canada.
Abstract:
We have reviewed the conjugation of biogenic polyamines spermine (spm), spermidine (spmd) and synthetic polyamines 3,7,11,15-tetrazaheptadecane.4HCl (BE-333) and 3,7,11,15,19-pentazahenicosane.5HCl (BE-3333) with human serum albumin (HSA), bovine serum albumin (BSA) and milk beta-lactoglobulin (b-LG) in aqueous solution at physiological pH. The results of multiple spectroscopic methods and molecular modeling were analysed here and correlations between polyamine binding mode and protein structural changes were estabilished. Polyamine-protein bindings are mainly via hydrophilic and H-bonding contacts. BSA forms more stable conjugates than HSA and b-LG. Biogenic polyamines form more stable complexes than synthetic polyamines except in the case of b-LG, where the protein shows more hydrophobic character than HSA and BSA. The loading efficacies were 40-52%. Modeling showed the presence of several H-bonding systems, which stabilized polyamine-protein conjugates. Polyamine conjugation induced major alterations of serum protein conformations. The potential application of serum proteins in delivery of polyamines is evaluated here.
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