Interaction of a hydrophobic-functionalized PAMAM dendrimer with bovine serum albumin : thermodynamic and structural changes
The interaction between a hydrophobic-functionalized PAMAM dendrimer (PAMAM-NH2-C12, 25%, G4) and bovine serum albumin (BSA) has been investigated by circular dichroism (CD), UV-vis, and fluorescence spectroscopic methods and molecular modeling. The analysis of the effects of dendrimer complexation...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 30(2014), 19 vom: 20. Mai, Seite 5536-44 |
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| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2014
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Dendrimers PAMAM Starburst Serum Albumin, Bovine 27432CM55Q |
| Zusammenfassung: | The interaction between a hydrophobic-functionalized PAMAM dendrimer (PAMAM-NH2-C12, 25%, G4) and bovine serum albumin (BSA) has been investigated by circular dichroism (CD), UV-vis, and fluorescence spectroscopic methods and molecular modeling. The analysis of the effects of dendrimer complexation on the stability and conformation of BSA indicated that the binding process of the hydrophobic-functionalized dendrimer with BSA induced the relatively large changes in secondary structure of protein. Thermal denaturation of BSA, when carried out in the presence of dendrimer, also indicated that this hydrophobic-functionalized dendrimer acted as a structure destabilizer for BSA. The hydrophobic, electrostatic, and hydrogen bonding forces played important roles in the complex formation. The putative binding site of PAMAM-NH2-C12 (25%) dendrimer on BSA was near to domain I and domain II. The effect of hydrophobic modification on the stability and structure of BSA would find useful information on the cytotoxicity of PAMAM dendrimer |
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| Beschreibung: | Date Completed 15.04.2015 Date Revised 16.11.2017 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la501129y |