Details zur Publikation

Kategorie Textpublikation
Referenztyp Zeitschriften
DOI 10.1016/j.jcis.2016.01.032
Titel (primär) Exploring 3D structural influences of aliphatic and aromatic chemicals on α-cyclodextrin binding
Autor Linden, L.; Goss, K.-U.; Endo, S.
Quelle Journal of Colloid and Interface Science
Erscheinungsjahr 2016
Department AUC
Band/Volume 468
Seite von 42
Seite bis 50
Sprache englisch
Keywords α-Cyclodextrin (CD); Steric effect; Binding constant; Inclusion complex; Cyclodextrin water partitioning; Solute 3D structure
UFZ Querschnittsthemen RU3;
Abstract Binding of solutes to macromolecules is often influenced by steric effects caused by the 3D structures of both binding partners. In this study, the 1:1 α-cyclodextrin (αCD) binding constants (Ka1) for 70 organic chemicals were determined to explore the solute-structural effects on the αCD binding. Ka1 was measured using a three-part partitioning system with either a headspace or a passive sampler serving as the reference phase. The Ka1 values ranged from 1.08 to 4.97 log units. The results show that longer linear aliphatic chemicals form more stable complexes than shorter ones, and that the position of the functional group has a strong influence on Ka1, even stronger than the type of the functional group. Comparison of linear and variously branched aliphatic chemicals indicates that having a sterically unhindered alkyl chain is favorable for binding. These results suggest that only one alkyl chain can enter the binding cavity. Relatively small aromatic chemicals such as 1,3-dichlorobenzene bind to αCD well, while larger ones like tetrachlorobenzene and 3-ring aromatic chemicals show only a weak interaction with αCD, which can be explained by cavity exclusion. The findings of this study help interpret cyclodextrin binding data and facilitate the understanding of binding processes to macromolecules.
dauerhafte UFZ-Verlinkung
Linden, L., Goss, K.-U., Endo, S. (2016):
Exploring 3D structural influences of aliphatic and aromatic chemicals on α-cyclodextrin binding
J. Colloid Interface Sci. 468 , 42 - 50 10.1016/j.jcis.2016.01.032