Interactions between PAMAM dendrimers and bovine serum albumin

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1648, Issue 1-2, 2003, Pages 115-126

  Klajnert, Barbara ^a   Stanisławska, Lidia ^a   Bryszewska, Maria ^a   Pałecz, Bartłomiej ^a  

^a UNIVERSITY OF LODZ   (Poland)

Author keywords

ANS; Differential scanning calorimetry; Energy transfer; Fluorescence quenching; Intrinsic fluorescence; PAMAM dendrimer; Red edge excitation shift; Serum albumin; Tryptophan fluorescence

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACRYLIC ACID METHYL ESTER; ALBUMIN; AMINE; DENDRIMER; ETHYLENEDIAMINE; FLUORESCENT DYE; POLYAMIDE; TRYPTOPHAN; BOVINE SERUM ALBUMIN; PAMAM STARBURST; POLYAMINE;

ALBUMIN BLOOD LEVEL; ARTICLE; CATTLE; CONFORMATION; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; EXPERIMENTAL TEST; FLUORESCENCE; INTERMETHOD COMPARISON; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; SURFACE PROPERTY; THERMOSTABILITY; ANIMAL; CHEMISTRY; HEAT; METABOLISM; PH; PROTEIN BINDING; SPECTROFLUOROMETRY;

BOVINAE;

ANIMALS; CATTLE; HEAT; HYDROGEN-ION CONCENTRATION; POLYAMINES; PROTEIN BINDING; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE;

EID: 1242341277     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00117-1     Document Type: Article

References (34)

1. Tomalia D.A., Baker H., Dewald J.R., Hall M., Kallos G., Martin S., Roeck J., Ryder J., Smith P. A new class of polymers: starburst-dendritic macromolecules. Polym. J. 17:1985;117-132.
2. Zanini D., Roy R. Practical synthesis of Starburst PAMAM α-thiosialodendrimers for probing multivalent carbohydrate-lectin binding properties. J. Org. Chem. 63:1998;3486-3491.
3. Zhuo R.X., Du B., Lu Z.R. In vitro release of 5-fluorouracil with cyclic core dendritic polymer. J. Control. Release. 57:1999;249-257.
4. Roberts J.C., Adams Y.E., Tomalia D., Mercer-Smith J.A., Lavallee D.K. Using starburst dendrimers as linker molecules to radiolabel antibodies. Bioconjug. Chem. 2:1990;305-308.
5. Barth R.F., Adams D.M., Soloway A.H., Alam F., Darby M.V. Boronated starburst dendrimer-monoclonal antibody immunoconjugates: evaluation as a potential delivery system for neutron capture therapy. Bioconjug. Chem. 5:1994;58-66.
6. Twyman L.J., Beezer A.E., Esfand R., Hardy M.J., Mitchell J.C. The synthesis of water soluble dendrimers, and their application as possible drug delivery systems. Tetrahedron Lett. 40:1999;1743-1746.
7. Kojima C., Kono K., Maruyama K., Takagishi T. Synthesis of polyamidoamine dendrimers having poly(ethylene glycol) grafts and their ability to encapsulate anticancer drugs. Bioconjug. Chem. 11:2000;910-917.
8. Liu M., Kono K., Fréchet J.M.J. Water-soluble dendritic unimolecular micelles: their potential as drug delivery agents. J. Control. Release. 65:2000;121-131.
9. Liu M., Fréchet J.M.J. Preparation of water-soluble dendritic unimolecular micelles as potential drug delivery agents. Polym. Mater. Sci. Eng. 80:1999;167-168.
10. Bhattacharya A.A., Curry S., Franks N.P. Binding of the general anesthetics propofol and halothane to human serum albumin. J. Biol. Chem. 275:2000;38731-38738.
11. Peters T.J. All About Albumin, Biochemistry, Genetics and Medical Applications. 1996;Academic Press, San Diego.
12. Bos O.J., Labro J.F., Fischer M.J.E., Witling J., Janssen L.H.M. The molecular mechanism of the neutral-to-base transition of human serum albumin. J. Biol. Chem. 264:1989;953-959.
13. Carter D.C., Ho X.J. Structure of serum albumins. Adv. Protein Chem. 45:1994;153-203.
14. Demchenko A.P. Site-selective excitation: a new dimension in protein and membrane spectroscopy. Trends Biochem. Sci. 13:1988;374-377.
15. de Oliveira A.H.C., Giglio J.R., Andriao-Escarso S.H., Ward R.J. The effect of resonance energy homotransfer on the intrinsic tryptophan fluorescence emission of the bothropstoxin-I dimer. Biochem. Biophys. Res. Commun. 284:2001;1011-1015.
16. Eftink M.R. Fluorescence quenching reactions: probing biological macromolecular structures. Dewey T.G. Biophysical and Biochemical Aspects of Fluorescence Spectroscopy. 1991;1-41 Plenum, New York.
17. 2+-induced interaction between albumin and anionic polyelectrolytes. Biomacromolecules. 2:2001;270-277.
18. b transitions of tryptophan: applications of theory and experimental observation to fluorescence of proteins. Methods Enzymol. 237:1997;113-150.
19. Lapshina E.A., Zavodnik I.B. Microcalorimetric and fluorescent studies of pH-induced transitions in erythrocyte membranes. Biol. Membr. 7:1994;155-163.
20. Burstein E.A. Equilibrium dynamics of native protein structure. (in Russian) USSR Acad. Sci. Pushchino. 1977;60-72.
21. Milhem O.M., Myles C., McKeown N.B., Attwood D., D'Emanuele A. Polyamidoamine Starburst dendrimers as solubility enhancers. Int. J. Pharm. 197:2000;239-241.
22. Roberts J.C., Bhalgat M.K., Zera R.T. Preliminary biological evaluation of polyaminoamine (PAMAM) Starburst™ dendrimers. J. Biomed. Mater. Res. 30:1996;53-65.
23. 125I-labelled polyamidoamine dendrimers in vivo. J. Control. Release. 65:2000;133-148.
24. Caminati G., Turro N.J., Tomalia D.A. Photophysical investigation of starburst dendrimers and their interactions with anionic and cationic surfactants. J. Am. Chem. Soc. 112:1990;8515-8522.
25. Wells M., Crooks R.M. Interactions between organized, surface-cofined monolayers and vapour-phase probe molecules. Preparation and properties of chemically sensitive dendrimer surfaces. J. Am. Chem. Soc. 118:1996;3988-3989.
26. Komath S.S., Swamy M.J. Fluorescence quenching, time-resolved fluorescence and chemical modification studies on the tryptophan residues of snake gourd (Trichosanthes anguina) seed lectin. J. Photochem. Photobiol., B Biol. 50:1999;108-118.
27. B. Klajnert, M. Bryszewska, Interactions of tryptophan and ANS with PAMAM dendrimers, Cell. Mol. Biol. Lett. (in press).
28. Putman F.W. The Plasma Proteins. 1960;Academic Press, New York.
29. Era S., Itoh K.B., Sogami M., Kuwata K., Iwama T., Yamada H., Watari H. Structural transition of bovine plasma albumin in the alkaline region - the N-B transition. Int. J. Pept. Protein Res. 35:1990;1-11.
30. Bos O.J., Labro J.F., Fischer M.J., Wilting J., Janssen L.H. The molecular mechanism of the neutral-to-base transition of human serum albumin. Acid/base titration and proton nuclear magnetic resonance studies on a large peptic and a large tryptic fragment of albumin. J. Biol. Chem. 264:1989;953-959.
31. France R.M., Grossman S.H. Acrylamide quenching of apo- and holo-α-lactalbumin in guanidine hydrochloride. Biochem. Biophys. Res. Commun. 269:2000;709-712.
32. Ercelen S., Kazan D., Erarslan A., Demchenko A.P. On the excited-state energy transfer between tryptophan residues in proteins: the case of penicillin acylase. Biophys. Chemist. 90:2001;203-217.
33. Slavik J. Anilinonaphthalene sulfonate as a probe of membrane composition and function. Biochim. Biophys. Acta. 694:1982;1-25.
34. Schönbrunn E., Eschenburg S., Luger K., Kabsch W., Amrhein N. Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA. Proc. Natl. Acad. Sci. U. S. A. 97:2000;6345-6349.