Interaction of brassinolide with essential amino acid residues: a theoretical approach.
The interaction of the most active natural brassinosteroid, brassinolide, with the twenty natural amino acids is studied applying the multiple minima hypersurface method to model the molecular interactions explicitly. The resulting thermodynamic data gives useful information about the amino acids with the greatest association for brassinolide and the stabilities of such complexes. Density functional theory (DFT) optimizations were further carried out to test the performance of semiempirical calculations. Additional calculations with a more accurate DFT method were performed to explore the formation of this type of molecular complexes. The semiempirical geometries and stability order of these complexes are in good agreement with the DFT calculations. Each group of amino acids possesses a preferential zone of interaction with brassinolide, forming the polar-charged amino acids the most stable complexes. This study could contribute to future investigations of the interaction of brassinosteroids with the receptor protein in plants.
Morera-Boado
Cercis
C
Laboratorio de Química Computacional y Teórica, Facultad de Química, Universidad de la Habana, 10400 Habana, Cuba. cercis@fq.uh.cu
Mora-Diez
Nelaine
N
Montero-Cabrera
Luis A
LA
Alonso-Becerra
Esther
E
González-Jonte
Raul H
RH
de la Vega
Jose M García
JM
D000601:Amino Acids, Essential / Q000737:chemistry*; D060406:Brassinosteroids; D002777:Cholestanols / Q000737:chemistry*; D008958:Models, Molecular; D013260:Steroids, Heterocyclic / Q000737:chemistry*; D013816:Thermodynamics
D000601:Amino Acids, Essential; D060406:Brassinosteroids; D002777:Cholestanols; D013260:Steroids, Heterocyclic; C023623:brassinolide