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New Journal of Chemistry
Volumn 30, Issue 11, 2006, Pages 1662-1668
Probing specific protein recognition by size-controlled glycosylated cyclodextrin nanoassemblies
Author keywords

[No Author keywords available]
Indexed keywords

CYCLODEXTRIN;
EID: 33750801108     PISSN: 11440546     EISSN: 13699261     Source Type: Journal    
DOI: 10.1039/b608495h     Document Type: Article
Times cited : (42)
References (65)
  • 57
    • 0004273681 scopus 로고
    • Oxford University Press, Oxford, Micelles range from 5 to 10 nm in size and have an internal hydrophobic core which can be described by SAXS. 15c Our TEM investigation shows the presence of nanoparticles of thiohexyl-CD which are aggregates of micelles (25-30 nm) and bigger micellar clusters (the smallest ones have a diameter of 100-200 nm, the biggest ones of 500-600 nm)32
    • R. C. C. New, Liposomes: a practical approach, Oxford University Press, Oxford, 1990
    • (1990) Liposomes: A Practical Approach
    • New, R.C.C.1
  • 58
    • 33750815817 scopus 로고    scopus 로고
    • Vesicles of thiohexadecyl-CD possess a thin layer shell and an aqueous inner core as confirmed by TEM and by elastic light scattering (results not shown)
    • Vesicles of thiohexadecyl-CD possess a thin layer shell and an aqueous inner core as confirmed by TEM and by elastic light scattering (results not shown)
  • 62
    • 0010623278 scopus 로고    scopus 로고
    • Kluwer Academic, Plenum Publishers, New York, The crystal structure of PA-I in the presence of calcium ions has been solved 39,40 as a tetramer containing, for each subunit, four tryptophan (Trp) and three tyrosine (Tyr) residues which adsorb in the UV region (260-295 nm). The PA-I structure shows that Tyr36 participates in the coordination of calcium ions and Tyr98, Tyr105 and Trp42 are located in neighbouring loops. It has been recently shown that the lectin-galactose contact points in the binding sites participate in the coordination of the calcium ion. By exciting at 290 nm the contribution of the Tyr component is minimal and does not obscure the Trp emission spectrum centred at 340 nm
    • J. R. Lakowicz, Priciples of Fluorescence Spectroscopy, Kluwer Academic, Plenum Publishers, New York, 1999
    • (1999) Priciples of Fluorescence Spectroscopy
    • Lakowicz, J.R.1
  • 64
    • 0344440747 scopus 로고    scopus 로고
    • Since fluorescence lifetimes are extremely sensitive to the fluorophore local environment, they, as is known, can depend on the protein stock used for the experiments. The discrepancies between two different stocks of lectin have been tested and e.g. the longer lifetime value for the free lectin changes from 3.1 to 2.5 ns. Anyway, in the presence of SC6CDGal and SC16CDGal, the trend in the decay lifetimes is consistent with that reported in Table 1. Time resolved fluorescence results are in agreement with steady-state fluorescence experiments which confirm the SC6CDGal/lectin interaction by quenching of a peculiar emission band We were unable to use, as conventionally described in the literature, stock buffered solution of protein and CDs. This problem could be probably ascribed to the ionic strength of the buffer which, being between 10 and 100 mM, affects the colloidal stability of CD aggregates by inducing detectable precipitation
    • G. Cioci E. P. Mitchell C. Gautier M. Wimmerová D. Sudakevitz S. Pérez N. Gilboa-Garber A. Imberty FEBS Lett. 2003 555 297
    • (2003) FEBS Lett. , vol.555 , pp. 297
    • Cioci, G.1    Mitchell, E.P.2    Gautier, C.3    Wimmerová, M.4    Sudakevitz, D.5    Pérez, S.6    Gilboa-Garber, N.7    Imberty, A.8

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.