An α-chain modification rivals the effect of fetal hemoglobin in retarding the rate of sickle cell fiber formation

Eli H. Worth, Mark K. Fugate, Kimberly C. Grasty, Patrick J. Loll, Marilyn F. Bishop, Frank A. Ferrone · 2023

Read An α-chain modification rivals the effect of fetal hemoglobin in retarding the rate of sickle cell fiber formation by Eli H. Worth, Mark K. Fugate, Kimberly C. Grasty, Patrick J. Loll, Marilyn F. Bishop, Frank A. Ferrone (2023) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-10713580.txt.

Description

Six researchers led by Eli Worth studied how to slow the stiff fiber growth that harms red blood cells in sickle cell disease. The disease stems from a fault in one hemoglobin chain. The fetal form of hemoglobin blocks fiber growth, so most work tries to switch that form back on or mimic it.

The team instead changed a single site on the other chain, the alpha chain. That change slowed fiber growth as well as fetal hemoglobin did. Because it works on its own path, it could pair with other treatments to boost their effect. The authors present it as a new tool in the search for stronger sickle cell therapies.

Catalog record

CREATOREli H. Worth, Mark K. Fugate, Kimberly C. Grasty, Patrick J. Loll, Marilyn F. Bishop, Frank A. Ferrone
YEAR2023
COLLECTIONPAPERS
FORMATTXT
FILE SIZE24 KB
VERSION1.0
LICENSECC BY 4.0
RIGHTSCC BY
SOURCEEurope PMC

Source: https://europepmc.org/articles/PMC10713580

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