Alizarin interaction with sickle hemoglobin: elucidation of their anti-sickling properties by multi-spectroscopic and molecular modeling techniques.
Adult
Anthraquinones
/ chemistry
Cell Death
/ drug effects
Cellulose
/ analogs & derivatives
Circular Dichroism
Erythrocytes
/ metabolism
Hemoglobin, Sickle
/ chemistry
Humans
Hydrogen Bonding
Ligands
Models, Molecular
Molecular Dynamics Simulation
Osmotic Fragility
Polymerization
Protein Structure, Secondary
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
Spectrum Analysis
Thermodynamics
Young Adult
CD
Hb S polymerization inhibition
Sickle hemoglobin
alizarin
fluorescence
molecular modeling
spectroscopy
Journal
Journal of biomolecular structure & dynamics
ISSN: 1538-0254
Titre abrégé: J Biomol Struct Dyn
Pays: England
ID NLM: 8404176
Informations de publication
Date de publication:
10 2019
10 2019
Historique:
pubmed:
19
12
2018
medline:
28
7
2020
entrez:
19
12
2018
Statut:
ppublish
Résumé
Polymerization of hemoglobin S is a major cause of morbidity and mortality in sickle cell disease, which leads to sickling and destruction of red blood cell. Alizarin, a bioactive compound from
Identifiants
pubmed: 30558488
doi: 10.1080/07391102.2018.1557557
doi:
Substances chimiques
Anthraquinones
0
Hemoglobin, Sickle
0
Ligands
0
acetylcellulose
3J2P07GVB6
alizarin
60MEW57T9G
Cellulose
9004-34-6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM