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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Chanphai, P. Thomas, T. J. Tajmir-Riahi, H. A. |
| Description | Country affiliation: Canada Author Affiliation: Chanphai P ( Department of Chemistry, Biochemistry and Physics, University of Québec at Trois-Rivières, C. P. 500, Trois-Rivières, Québec G9A 5H7,Canada.); Thomas TJ ( Department of Medicine, Rutgers Robert Wood Johnson Medical School, Rutgers Cancer Institute of New Jersey, New Brunswick, NJ 08901, USA.); Tajmir-Riahi HA ( Department of Chemistry, Biochemistry and Physics, University of Québec at Trois-Rivières, C. P. 500, Trois-Rivières, Québec G9A 5H7,Canada. Electronic address: tajmirri@uqtr.ca.) |
| 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. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Journal | International Journal of Biological Macromolecules |
| Volume Number | 92 |
| e-ISSN | 18790003 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-11-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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