Conjugation of biogenic and synthetic polyamines with serum proteins: A comprehensive review

P. Chanphai, T. J. Thomas, H. A. Tajmir-Riahi

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)515-522
Number of pages8
JournalInternational Journal of Biological Macromolecules
StatePublished - Nov 1 2016

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Economics and Econometrics
  • Energy(all)


  • Conjugation
  • Drug delivery
  • Modeling
  • Polyamine
  • Serum protein


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