PUMA
Istituto di Biofisica     
Gabellieri E., Strambini G. B., Shcharbin D., Klajnert B., Bryszewska M. Dendrimer-Protein Interactions Studied by Tryptophan Room Temperature Phosphorescence. In: Biochimica et Biophysica Acta-Proteins and Proteomics, vol. 1764 (11) pp. 1750 - 1756. Elsevier Science, 2006.
 
 
Abstract
(English)
Dendrimers are a relatively new class of materials with unique molecular architectures, which provide promising opportunities for biological applications as DNA carriers and drug delivery systems. Progress in these fields, however, requires knowledge of their potential interactions with biological components at cellular and molecular level. This study utilizes Trp phosphorescence spectroscopy to examine possible perturbations of the protein native fold in solution by neutral, positively and negatively charged fifth generation polyamidoamine (PAMAM) dendrimers. Phosphorescence lifetime measurements, conducted on model proteins varying in the degree of burial of the triplet probe and in quaternary structure, show that dendrimers interact with proteins in solutions forming stable complexes in which the protein structure may be significantly altered, particularly in superficial, flexible regions of the polypeptide. Both electrostatic and non-electrostatic interactions can give rise to stable complexes, whose affinity and limited number of binding sites distinguish them from mere aspecific molecular associations. Of direct relevance for the application of these polymers in the medical field, structural alterations have also been detected in human plasma proteins such as serum albumin and immunoglobulins. The above results suggest that Trp phosphorescence may provide a useful monitor for working out experimental conditions and protocols that help preserve the structural integrity of proteins in the presence of these polymers.
DOI: 10.1016/j.bbapap.2006.09.008
Subject PAMAM dendrimers
Dendrimer-protein interactions
Protein conformation
Room temperature phosphorescence


Icona documento 1) Download Document PDF


Icona documento Open access Icona documento Restricted Icona documento Private

 


Per ulteriori informazioni, contattare: Librarian http://puma.isti.cnr.it

Valid HTML 4.0 Transitional