 |
PDBsum entry 6kye
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxygen transport
|
PDB id
|
|
|
|
6kye
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
(+ 0 more)
140 a.a.
|
|
|
|
|
|
|
|
|
|
|
(+ 0 more)
146 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Genetically engineered haemoglobin wrapped covalently with human serum albumins as an artificial o2 carrier.
|
|
|
Authors
|
|
R.Funaki,
W.Okamoto,
C.Endo,
Y.Morita,
K.Kihira,
T.Komatsu.
|
|
|
Ref.
|
|
J Mater Chem B, 2020,
8,
1139-1145.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
We describe the synthesis and O2 affinity of genetically engineered
human adult haemoglobin (rHbA) wrapped covalently with recombinant human serum
albumins (rHSAs) as an artificial O2 carrier used for a completely
synthetic red blood cell (RBC) substitute. Wild-type rHbA [rHbA(wt)] expressed
in yeast species Pichia pastoris shows an identical amino acid sequence and
three-dimensional structure to those of native HbA. It is particularly
interesting that two orientations of the prosthetic haem group in rHbA(wt) were
aligned by gentle heating in the natural form. Covalent wrapping of rHbA(wt)
with three rHSAs conferred a core-shell structured haemoglobin-albumin cluster:
rHbA(wt)-rHSA3. Three variant clusters containing an rHbA mutant core
were also created: Leu-β28 → Phe, Leu-β28 → Trp, and Leu-β28 →
Tyr/His-β63 → Gln. Replacement of Leu-β28 with Trp decreased the distal
space in the haem pocket, thereby yielding a cluster with moderately low
O2 affinity which is nearly the same as that of human RBC.
|
|
|
|
|
|
|
