Idioma:

Binding assessment of two arachidonic-based synthetic derivatives of adrenalin with β-lactoglobulin: Molecular modeling and chemometrics approach

Gholami, S. ; Bordbar, A.K. ; Akvan, N. ; Parastar, H. ; Fani, N. ; Gretskaya, N.M. ; Bezuglov, V.V. ; Haertlé, T.

Biophysical chemistry, 2015-12, Vol.207, p.97-106 [Periódico revisado por pares]

Netherlands: Elsevier B.V

Texto completo disponível

Citações Citado por

Enviar para

Título:
Binding assessment of two arachidonic-based synthetic derivatives of adrenalin with β-lactoglobulin: Molecular modeling and chemometrics approach
Autor: Gholami, S. ; Bordbar, A.K. ; Akvan, N. ; Parastar, H. ; Fani, N. ; Gretskaya, N.M. ; Bezuglov, V.V. ; Haertlé, T.
Assuntos: Arachidonic Acid - chemistry ; Arachidonic Acids - chemistry ; Arachidonic Acids - metabolism ; Arachidonoyl adrenalin ; Arachidonoyl noradrenalin ; Binding modes ; Binding Sites ; Chemical Sciences ; Chemometrics ; Entropy ; Epinephrine - analogs & derivatives ; Epinephrine - chemistry ; Epinephrine - metabolism ; Hydrogen Bonding ; Lactoglobulins - chemistry ; Lactoglobulins - metabolism ; Molecular docking ; Molecular Docking Simulation ; Molecular dynamics simulation ; Norepinephrine - analogs & derivatives ; Norepinephrine - chemistry ; Norepinephrine - metabolism ; Other ; Principal Component Analysis ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Spectrophotometry, Ultraviolet
É parte de: Biophysical chemistry, 2015-12, Vol.207, p.97-106
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: A computational approach to predict the main binding modes of two adrenalin derivatives, arachidonoyl adrenalin (AA-AD) and arachidonoyl noradrenalin (AA-NOR) with the β-lactoglubuline (BLG) as a nano-milk protein carrier is presented and assessed by comparison to the UV–Vis absorption spectroscopic data using chemometric analysis. Analysis of the spectral data matrices by using the multivariate curve resolution-alternating least squares (MCR-ALS) algorithm led to the pure concentration calculation and spectral profiles resolution of the chemical constituents and the apparent equilibrium constants computation. The negative values of entropy and enthalpy changes for both compound indicated the essential role of hydrogen bonding and van der Waals interactions as main driving forces in stabilizing protein–ligand complex. Computational studies predicted that both derivatives are situated in the calyx pose and remained in that pose during the whole time of simulation with no any significant protein structural changes which pointed that the BLG could be considered as a suitable carrier for these catecholamine compounds. [Display omitted] •Catecholamine derivatives bind to the calyx binding site of BLG.•The binding was proceed via H-bonding, van der Waals and hydrophobic interactions•The order of affinity of BLG-catecholamines complexation is AA-NOR > AA-AD•Simulation results revealed negligible changes in structure and dynamics of BLG.
Editor: Netherlands: Elsevier B.V
Idioma: Inglês

Links

Voltar para lista de resultados

Realização: Logos de Redes Sociais:

Binding assessment of two arachidonic-based synthetic derivatives of adrenalin with β-lactoglobulin: Molecular modeling and chemometrics approach

Gholami, S. ; Bordbar, A.K. ; Akvan, N. ; Parastar, H. ; Fani, N. ; Gretskaya, N.M. ; Bezuglov, V.V. ; Haertlé, T.

Netherlands: Elsevier B.V

Buscando em bases de dados remotas. Favor aguardar.