Hemoglobin(βC93A)–Albumin Cluster: Mutation of Cysteine‐β93 to Alanine Allows Moderate Reduction of O2 Affinity by Inositol Hexaphosphate

Covalent wrapping of recombinant human hemoglobin (Cys‐β93→Ala) variant rHb(βC93A) by human serum albumin (HSA) yielded the rHb(βC93A)‐HSA3 cluster as an artificial O2 carrier as a red blood cell substitute. Complexation of inositol hexaphosphate to the central rHb(βC93A) core reduced the O2 affinit...

Full description

Saved in:
Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2019-07, Vol.20 (13), p.1684-1687
Main Authors: Morita, Yoshitsugu, Igarashi, Keisuke, Funaki, Ryosuke, Komatsu, Teruyuki
Format: Article
Language:English
Subjects:
Affinity
Alanine
Albumin
Clusters
Crosslinking
Erythrocytes
heme proteins
Hemoglobin
Human serum albumin
Inositol
Mutation
oxygen carriers
protein modifications
red blood cell substitutes
Reduction
Serum albumin
site-directed mutagenesis
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Covalent wrapping of recombinant human hemoglobin (Cys‐β93→Ala) variant rHb(βC93A) by human serum albumin (HSA) yielded the rHb(βC93A)‐HSA3 cluster as an artificial O2 carrier as a red blood cell substitute. Complexation of inositol hexaphosphate to the central rHb(βC93A) core reduced the O2 affinity moderately, in much the same way as that of naked hemoglobin. This reduction might be attributable to the inert, small Ala‐β93 residue, which cannot be reacted with the bulky maleimide crosslinker. Accepting substitutes: A core–shell protein cluster comprising a recombinant human hemoglobin variant (rHb(βC93A)) at the center and human serum albumin (HSA) at the exterior is synthesized as an artificial O2 carrier to act as a substitute for red blood cells. The rHb(βC93A)‐HSA3 cluster shows controllable O2 affinity by complexation of the allosteric effector inositol hexaphosphate.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201900079