Interactions between PAMAM dendrimers and bovine serum albumin

• Published in: Biochimica et biophysica acta Vol. 1648; no. 1; pp. 115 - 126
• Main Authors: Klajnert, Barbara, Stanisławska, Lidia, Bryszewska, Maria, Pałecz, Bartłomiej
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 30.05.2003
• Subjects: Animals; ANS; Cattle; Dendrimers; Differential scanning calorimetry; Energy transfer; Fluorescence quenching; Hot Temperature; Hydrogen-Ion Concentration; Intrinsic fluorescence; PAMAM dendrimer; Polyamines - chemistry; Polyamines - metabolism; Protein Binding; Red edge excitation shift; Serum albumin; Serum Albumin, Bovine - chemistry; Serum Albumin, Bovine - metabolism; Spectrometry, Fluorescence; Tryptophan fluorescence; Differential scanning calorimetry; Intrinsic fluorescence; ANS; Tryptophan fluorescence; Serum albumin; PAMAM dendrimer; Red edge excitation shift; Energy transfer; Fluorescence quenching
• ISSN: 1570-9639; 0006-3002; 1878-1454; 1878-2434
• DOI: 10.1016/S1570-9639(03)00117-1

Dendrimers are a new class of polymeric materials. They are globular, highly branched, monodisperse macromolecules. Due to their structure, dendrimers promise to be new, effective biomedical materials as oligonucleotide transfection agents and drug carriers. More information about biological properties of dendrimers is crucial for further investigation of dendrimers in therapeutic applications. In this study the mechanism of interactions between polyamidoamine (PAMAM) dendrimers and bovine serum albumin (BSA) was examined. PAMAM dendrimers are based on an ethylenediamine core and branched units are constructed from both methyl acrylate and ethylenediamine. We used three types of PAMAM dendrimers with different surface groups (–COOH, –NH 2, –OH). As BSA contains two tryptophan residues we were able to evaluate dendrimers influence on protein molecular conformation by measuring the changes in the fluorescence of BSA in the presence of dendrimers. Additionally experiments with a fluorescent probe 1-anilinonaphthalene-8-sulfonic acid (ANS) were carried out. The differential scanning calorimetry (DSC) was chosen to investigate impact on protein thermal stability upon the dendrimers. Our experiments showed that the extent of the interactions between BSA and dendrimers strongly depends on their surface groups and is the biggest for amino-terminated dendrimers.