Protein Triad Comprising Genetically Fused Hemoglobin and Human Serum Albumins as an Artificial O2 Carrier Resistant to Haptoglobin Binding

We describe synthesis of a symmetric protein triad comprising a genetically fused recombinant hemoglobin(di-α/Cβ120) center and human serum albumin sides [rHb(di-α/Cβ120)–HSA2]. This trimer is not cleaved at low concentration. It shows adequate resistance to haptoglobin binding as an artificial O2 c...

Full description

Saved in:
Bibliographic Details
Published in:Chemistry letters 2021-12, Vol.50 (12), p.2011-2014
Main Authors: Morita, Yoshitsugu, Shindo, Yuki, Komatsu, Teruyuki
Format: Article
Language:English
Subjects:
Binding
Erythrocytes
Hemoglobin
Inositols
Mutation
Proteins
Serum albumin
Trimers
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:We describe synthesis of a symmetric protein triad comprising a genetically fused recombinant hemoglobin(di-α/Cβ120) center and human serum albumin sides [rHb(di-α/Cβ120)–HSA2]. This trimer is not cleaved at low concentration. It shows adequate resistance to haptoglobin binding as an artificial O2 carrier used as a red blood cell (RBC) substitute. Also, O2 affinity of the trimer was modulated to the appropriate value, similarly to that of RBCs, by complexation of inositol hexaphosphate and a Kβ108 mutation into the Hb core.
ISSN:0366-7022
1348-0715
DOI:10.1246/cl.210549