[PDF]    http://dx.doi.org/10.3952/lithjphys.44105

Open access article / Atviros prieigos straipsnis

Lith. J. Phys. 44, 41–47 (2004)


SPECTROSCOPIC STUDIES OF SELF-ASSEMBLED TPPS4 NANOSTRUCTURES IN AQUEOUS SOLUTIONS: THE ROLE OF SERUM ALBUMIN AND pH
J. Valančiūnaitė, J. Žerebcova, S. Bagdonas, G. Streckytė, and R. Rotomskis
Laser Research Centre, Vilnius University, Saulėtekio 9, LT-10222 Vilnius, Lithuania

Received 18 November 2003

The interaction of meso-tetra(4-sulphonatophenyl) porphyrin (TPPS4) with bovine serum albumin (BSA) in acid medium was investigated using optical absorption spectroscopy. Changes in the absorption spectra indicate that a mechanism of interaction between TPPS4 and BSA is in a complex manner dependent on: (a) the ratio between monomeric and aggregated species in a homogenous solution of TPPS4, (b) the molar ratio of the TPPS4–BSA mixture, and (c) the initial state of protein solution. When different forms of TPPS4 exist in solution, small relative concentrations of BSA favour J-aggregation; however, higher concentrations may lead to the disruption of J-aggregates. If J-aggregates are preformed in the solution, adding of protein does not disrupt these aggregates.
Keywords: absorption spectroscopy, TPPS4, J-aggregates, self-assembling, albumin, pH
PACS: 33.20.Kf, 33.20.Lg


SAVITVARKIŲ TPPS4 NANODARINIŲ SPEKTROSKOPINIAI TYRIMAI: SĄVEIKOS SU ALBUMINU IR APLINKOS pH ĮTAKA
J. Valančiūnaitė, J. Žerebcova, S. Bagdonas, G. Streckytė, R. Rotomskis
Vilniaus universitetas, Vilnius, Lietuva

Vandeninėse rūgštinėse terpėse tetrapirolinis junginys mezotetra(4-sulfonatofenil)porfinas (TPPS4) virsta jonine forma, kuri sudaro savitvarkius organizuotus mezodarinius – J agregatus. Nuostoviosios sugerties spektroskopijos būdu tirtos tų agregatų susidarymo ypatybės jaučio serumo albumino įvairios koncentracijos ir skirtingo rūgštingumo tirpaluose. Nustatyta, kad vienodos TPPS4 koncentracijos tirpaluose, priklausomai nuo terpės pH bei baltymo koncentracijos, susidaro skirtingas J agregatų kiekis. Porfirino joninės formos pusiausvirines sąveikas baltyminiuose tirpaluose lemia konkurencinis mechanizmas. Nedidelės baltymo koncentracijos skatino J agregatų susidarymą, tuo tarpu didesnės turėjo priešingą poveikį. Baltymas neturėjo įtakos jau susidariusių J agregatų patvarumui.


References / Nuorodos

[1] S.B. Brown and M. Shillcock, Biochem. J. 153, 278–285 (1976),
http://dx.doi.org/10.1042/bj1530279
[2] K. Uehara, Y. Hioki, and M. Mimuro, Photochem. Photobiol. 58, 127–132 (1993),
http://dx.doi.org/10.1111/j.1751-1097.1993.tb04913.x
[3] C. Tanielian and G. Heinrich, Photochem. Photobiol. 61, 131–135 (1995),
http://dx.doi.org/10.1111/j.1751-1097.1995.tb03950.x
[4] R.F. Khairutdinov and N. Serpone, J. Phys. Chem. 99, 11952–11958 (1995),
http://dx.doi.org/10.1021/j100031a024
[5] D. Frolov, S. Bagdonas, L. Kelbauskas, W. Dietel, G. Streckytė, and R. Rotomskis, Lithuanian J. Phys. 41, 484–494 (2001)
[6] D. Frolov, S. Bagdonas, R. Rotomskis, and V. Gulbinas, Lithuanian J. Phys. 40, 228–231 (2000)
[7] L. Kelbauskas, S. Bagdonas, W. Dietel, and R. Rotomskis, J. Lumin. 101, 253–262 (2003),
http://dx.doi.org/10.1016/S0022-2313(02)00547-1
[8] M.A. El-Far and N.R. Pimstone, Cancer Res. 46, 4390–4395 (1986),
http://aacrjournals.org/cancerres/article/46/9/4390/491045/Selective-in-Vivo-Tumor-Localization-of
[9] M.A. El-Far, N.A. El-Hamil, and M. Ghoneim, Biochim. 70, 1379–1384 (1988),
http://dx.doi.org/10.1016/0300-9084(88)90010-7
[10] V.E. Yushmanov, T.T. Tominaga, I.E. Borissevitch, H. Imasato, and M. Tabak, Magn. Reson. Imaging 14, 255–261 (1996),
http://dx.doi.org/10.1016/0730-725X(95)02103-Z
[11] J. Davila and A. Harriman, Photochem. Photobiol. 51, 9–19 (1990),
http://dx.doi.org/10.1111/j.1751-1097.1990.tb01678.x
[12] O. Ohno, Y. Kaizu, and H. Kobayashi, J. Chem. Phys. 99, 4128–4139 (1993),
http://dx.doi.org/10.1063/1.466109
[13] D.L. Akins, H.-R. Zhu, and C. Guo, J. Phys. Chem. 98, 3612–3618 (1994),
http://dx.doi.org/10.1021/j100065a012
[14] N.C. Maiti, S. Mazumdar, and N. Periasamy, J. Phys. Chem. B 102, 1528–1538 (1998),
http://dx.doi.org/10.1021/jp9723372
[15] S.M. Andrare and S.M.B. Costa, Biophys. J. 82, 1607–1619 (2002),
http://dx.doi.org/10.1016/S0006-3495(02)75512-4
[16] K. Berg and J. Moan, Int. J. Cancer 59, 814–822 (1994),
http://dx.doi.org/10.1002/ijc.2910590618
[17] S. Bagdonas and R. Rotomskis, Lithuanian J. Phys. 38, 75–78 (1998)
[18] A. Renault, P.-F. Lenne, C. Zakri, A. Aradian, C. Venien-Bruyan, and F. Amblard, Biophys. J. 76, 1580–1590 (1999),
http://dx.doi.org/10.1016/S0006-3495(99)77317-0
[19] M.J. Geisowand and G.H. Beaven, Biochem. J. 163, 477–484 (1977),
http://dx.doi.org/10.1042/bj1630477
[20] M.Y. Khan, Biochem. J. 236, 307–310 (1986),
http://dx.doi.org/10.1042/bj2360307
[21] W.F. Harrington, P. Johnson, and R.H. Ottewill, Biochem. J. 62, 569–582 (1956),
http://dx.doi.org/10.1042/bj0620569
[22] I.E. Borissevitch, T.T. Tominaga, H. Imasato, and M. Tabak, J. Lumin. 69, 65–76 (1996),
http://dx.doi.org/10.1016/0022-2313(96)00037-3