Document Detail

Albumin binds self-assembling dyes as specific polymolecular ligands.
MedLine Citation:
PMID:  16769109     Owner:  NLM     Status:  MEDLINE    
Self-assembling dyes with a structure related to Congo red (e.g. Evans blue) form polymolecular complexes with albumin. The dyes, which are lacking a self-assembling property (Trypan blue, ANS) bind as single molecules. The supramolecular character of dye ligands bound to albumin was demonstrated by indicating the complexation of dye molecules outnumbering the binding sites in albumin and by measuring the hydrodynamic radius of albumin which is growing upon complexation of self-assembling dye in contrast to dyes lacking this property. The self-assembled character of Congo red was also proved using it as a carrier introducing to albumin the intercalated nonbonding foreign compounds. Supramolecular, ordered character of the dye in the complex with albumin was also revealed by finding that self-assembling dyes become chiral upon complexation. Congo red complexation makes albumin less resistant to low pH as concluded from the facilitated N-F transition, observed in studies based on the measurement of hydrodynamic radius. This particular interference with protein stability and the specific changes in digestion resulted from binding of Congo red suggest that the self-assembled dye penetrates the central crevice of albumin.
Barbara Stopa; Janina Rybarska; Anna Drozd; Leszek Konieczny; Marcin Król; Marek Lisowski; Barbara Piekarska; Irena Roterman; Paweł Spólnik; Grzegorz Zemanek
Related Documents :
19167149 - Equilibrium unfolding of the retinoid x receptor ligand binding domain and characteriza...
9989379 - A dynamical investigation of acrylodan-labeled mutant phosphate binding protein.
23090399 - Structural studies on the folded domain of the human prion protein bound to the fab fra...
2458099 - Analysis of the conformation and ligand-binding properties of the activation segment of...
2437979 - Dye affinity chromatography of ricin subunits.
23991039 - A human antibody to the cd4 binding site of gp120 capable of highly potent but sporadic...
3003349 - [3h]tryptamine autoradiography in rat brain and choroid plexus reveals two distinct sites.
10491089 - Inhibitor peptide snp-1 binds to a soluble form of bst-1/cd157 at a 2:2 stoichiometry.
18855709 - Glycopeptide dendrimers for biomedical applications.
Publication Detail:
Type:  In Vitro; Journal Article     Date:  2006-05-12
Journal Detail:
Title:  International journal of biological macromolecules     Volume:  40     ISSN:  0141-8130     ISO Abbreviation:  Int. J. Biol. Macromol.     Publication Date:  2006 Dec 
Date Detail:
Created Date:  2007-01-09     Completed Date:  2007-01-31     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7909578     Medline TA:  Int J Biol Macromol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1-8     Citation Subset:  IM    
Chair of Medical Biochemistry, Medical College, Jagiellonian University, Kopernika 7, 31-034 Kraków, Poland.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Binding Sites
Circular Dichroism
Coloring Agents / chemistry,  metabolism*
Congo Red / chemistry,  metabolism
Evans Blue / chemistry,  metabolism
Hydrogen-Ion Concentration
Macromolecular Substances
Models, Molecular
Molecular Structure
Protein Binding
Serum Albumin, Bovine / metabolism*
Reg. No./Substance:
0/Coloring Agents; 0/Ligands; 0/Macromolecular Substances; 0/Serum Albumin, Bovine; 314-13-6/Evans Blue; 573-58-0/Congo Red

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Differential sensitivity of flounder (Platichthys flesus) in response to oestrogenic chemical exposu...
Next Document:  Gene delivery to differentiated neurotypic cells with RGD and HIV Tat peptide functionalized polymer...