RT info:eu-repo/semantics/article
T1 A competition between relative stability and binding energy in caffeine phenyl-glucose aggregates: implications in biological mechanisms
A1 Calabrese, Camilla
A1 Camiruaga, Ander
A1 Parra Santamaria, Maider
A1 Evangelisti, Luca
A1 Melandri, Sonia
A1 Maris, Assimo
A1 Usabiaga, Imanol
A1 Fernández, José A.
K1 Caffeine - Physiological effect
K1 Caffeine
K1 Sugar
K1 Azúcar
K1 Analytical chemistry
K1 Spectroscopy
K1 Infrared spectroscopy
K1 Noncovalent interactions
K1 Inorganic chemistry
K1 Organic chemistry
K1 Molecular biology
K1 2301 Química Analítica
K1 2209.21 Espectroscopia
K1 2301.08 Espectroscopia de Infrarrojos
K1 2303 Química Inorgánica
K1 2306 Química Orgánica
K1 2302.21 Biología Molecular
AB Hydrogen bonds and stacking interactions are pivotal in biological mechanisms, although their proper characterisation within a molecular complex remains a difficult task. We used quantum mechanical calculations to characterise the complex between caffeine and phenyl-β-D-glucopyranoside, in which several functional groups of the sugar derivative compete with each other to attract caffeine. Calculations at different levels of theory (M06-2X/6-311++G(d,p) and B3LYP-ED=GD3BJ/def2TZVP) agree to predict several structures similar in stability (relative energy) but with different affinity (binding energy). These computational results were experimentally verified by laser infrared spectroscopy, through which the caffeine·phenyl-β-D-glucopyranoside complex was identified in an isolated environment, produced under supersonic expansion conditions. The experimental observations correlate with the computational results. Caffeine shows intermolecular interaction preferences that combine both hydrogen bonding and stacking interactions. This dual behaviour had already been observed with phenol, and now with phenyl-β-D-glucopyranoside, it is confirmed and maximised. In fact, the size of the complex’s counterparts affects the maximisation of the intermolecular bond strength because of the conformational adaptability given by the stacking interaction. Comparison with the binding of caffeine within the orthosteric site of the A2A adenosine receptor shows that the more strongly bound caffeine·phenyl-β-D-glucopyranoside conformer mimics the interactions occurring within the receptor.
PB MDPI
SN 1422-0067
YR 2023
FD 2023
LK https://uvadoc.uva.es/handle/10324/69344
UL https://uvadoc.uva.es/handle/10324/69344
LA eng
NO International Journal of Molecular Sciences, 2023, Vol. 24, Nº. 5, 4390
NO Producción Científica
DS UVaDOC
RD 14-oct-2024