Cargando…
Metal-catalyzed oxidation of human serum albumin does not alter the interactive binding to the two principal drug binding sites
It is well known that various physiological factors such as pH, endogenous substances or post-translational modifications can affect the conformational state of human serum albumin (HSA). In a previous study, we reported that both pH- and long chain fatty acid-induced conformational changes can alte...
Autores principales: | Yamasaki, Keishi, Nishi, Koji, Anraku, Makoto, Taguchi, Kazuaki, Maruyama, Toru, Otagiri, Masaki |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5986994/ https://www.ncbi.nlm.nih.gov/pubmed/29872747 http://dx.doi.org/10.1016/j.bbrep.2018.05.002 |
Ejemplares similares
-
Long chain fatty acids alter the interactive binding of ligands to the two principal drug binding sites of human serum albumin
por: Yamasaki, Keishi, et al.
Publicado: (2017) -
Differential Effects of Methoxy Group on the Interaction of Curcuminoids with Two Major Ligand Binding Sites of Human Serum Albumin
por: Sato, Hiroki, et al.
Publicado: (2014) -
Analysis of the Binding of Aripiprazole to Human Serum
Albumin: The Importance of a Chloro-Group in the Chemical Structure
por: Sakurama, Keiki, et al.
Publicado: (2018) -
Comparison of the Pharmacokinetic Properties of Hemoglobin-Based Oxygen Carriers
por: Taguchi, Kazuaki, et al.
Publicado: (2017) -
Influence of Molecular Structure on O(2)-Binding Properties and Blood Circulation of Hemoglobin‒Albumin Clusters
por: Yamada, Kana, et al.
Publicado: (2016)