Hemoglobin Variants as Targets for Stabilizing Drugs
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F10974938%3A_____%2F25%3A25_88_36" target="_blank" >RIV/10974938:_____/25:25_88_36 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.3390/molecules30020385" target="_blank" >https://doi.org/10.3390/molecules30020385</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/molecules30020385" target="_blank" >10.3390/molecules30020385</a>
Alternative languages
Result language
angličtina
Original language name
Hemoglobin Variants as Targets for Stabilizing Drugs
Original language description
Hemoglobin is an oxygen-transport protein in red blood cells that interacts with multiple ligands, e.g., oxygen, carbon dioxide, carbon monoxide, and nitric oxide. Genetic variations in hemoglobin chains, such as those underlying sickle cell disease and thalassemias, present substantial clinical challenges. Here, we review the progress in research, including the use of allosteric modulators, pharmacological chaperones, and antioxidant treatments, which has begun to improve hemoglobin stability and oxygen affinity. According to UniProt (as of 7 August 2024), 819 variants of the alpha-hemoglobin subunit and 771 variants of the beta-hemoglobin subunit have been documented, with over 116 classified as unstable. These data demonstrate the urgent need to develop variant-specific stabilizing options. Beyond small-molecule drugs/binders, novel protein-based strategies-such as engineered hemoglobin-binding proteins (including falcilysin, llama-derived nanobodies, and alpha-hemoglobin-stabilizing proteins)-offer promising new options. As our understanding of hemoglobin's structural and functional diversity grows, so does the potential for genotype-driven approaches. Continued research into hemoglobin stabilization and ligand-binding modification may yield more precise, effective treatments and pave the way toward effective strategies for hemoglobinopathies.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics
Result continuities
Project
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Continuities
R - Projekt Ramcoveho programu EK
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Molecules
ISSN
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e-ISSN
1420-3049
Volume of the periodical
30
Issue of the periodical within the volume
2
Country of publishing house
CH - SWITZERLAND
Number of pages
34
Pages from-to
385 (1-34)
UT code for WoS article
001404360600001
EID of the result in the Scopus database
2-s2.0-85216224909