Influence of the separation of the charged groups and aromatic ring on interaction of tyrosine and phenylalanine analogues and derivatives with beta-cyclodextrin.
Interactions of tyrosine and phenylalanine analogues with beta-cyclodextrin have been examined in terms of structural features of the ligand such as the separation of the charged amino group and aromatic ring, the presence of additional functional group attached to the amino or phenyl ring, and the presence of a charge on amino or carboxyl group, and steric effects using steady-state and time-resolved fluorescence spectroscopy and microcalorimetry. The studied aromatic amino acids possess low binding constant to beta-cyclodextrin, diversified with respect to the presence or absence of a substituent in para position of the phenyl ring. However, calculated, based on the global analysis of the fluorescence intensity decays, binding constants do not allow to estimate unequivocally the influence of the distance between the charged groups and phenol/phenyl ring on the inclusion complex stability because of their low diversification.
Mrozek
Justyna
J
Faculty of Chemistry, University of Gdańsk, Sobieskiego 18, 80-952 Gdańsk, Poland.
Banecki
Bogdan
B
Karolczak
Jerzy
J
Wiczk
Wiesław
W
D002151:Calorimetry; D006863:Hydrogen-Ion Concentration; D015394:Molecular Structure; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D055672:Static Electricity; D013816:Thermodynamics; D013997:Time Factors; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000737:chemistry*; D047392:beta-Cyclodextrins / Q000737:chemistry*
D047392:beta-Cyclodextrins; D014443:Tyrosine; D010649:Phenylalanine