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Interaction of polyamidoamine (PAMAM) succinamic acid dendrimers generation 4 with human serum albumin

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Title: Interaction of polyamidoamine (PAMAM) succinamic acid dendrimers generation 4 with human serum albumin
Authors: Sekowski, Szymon1 sekowski100@vp.pl, Buczkowski, Adam2, Palecz, Bartlomiej2, Gabryelak, Teresa1
Source: Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy. Oct2011, Vol. 81 Issue 1, p706-710. 5p.
Subjects: Polyamines, Carboxylic acids, Dendrimers, Serum albumin, Fluorescence spectroscopy, Circular dichroism, Protein structure, Calorimetry
Abstract: Abstract: Dendrimers, a relatively new group of highly branched three dimensional polymers, are intensively investigated to use them in biomedical and physicochemical sciences. Their specific architecture gives them the ability to interact with many different types of molecules. In our studies the interaction between PAMAM succinamic acid dendrimers generation 4 (PAMAM-SAH G4) and human serum albumin (HSA) was examined. Experiments showed that a single molecule of a HSA can bind approximately 6 particles of dendrimers. The fluorescence studies demonstrated that dendrimers lead to a decrease in protein fluorescence but changes in fluorescence anisotropy were not observed. Alterations in the spectrum of circular dichroism indicated changes in the secondary protein structure. The results clearly show that this generation of dendrimers possesses a strong ability to interact with human serum albumin. [Copyright &y& Elsevier]
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Database: Engineering Source
Description
Abstract:Abstract: Dendrimers, a relatively new group of highly branched three dimensional polymers, are intensively investigated to use them in biomedical and physicochemical sciences. Their specific architecture gives them the ability to interact with many different types of molecules. In our studies the interaction between PAMAM succinamic acid dendrimers generation 4 (PAMAM-SAH G4) and human serum albumin (HSA) was examined. Experiments showed that a single molecule of a HSA can bind approximately 6 particles of dendrimers. The fluorescence studies demonstrated that dendrimers lead to a decrease in protein fluorescence but changes in fluorescence anisotropy were not observed. Alterations in the spectrum of circular dichroism indicated changes in the secondary protein structure. The results clearly show that this generation of dendrimers possesses a strong ability to interact with human serum albumin. [Copyright &y& Elsevier]
ISSN:13861425
DOI:10.1016/j.saa.2011.07.009