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Related Concept Videos

Hemoglobin01:24

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Drug Binding to Blood Components01:30

Drug Binding to Blood Components

When drugs enter systemic circulation, they interact with various components of the blood, including proteins such as human serum albumin (HSA), α1-acid glycoprotein (AAG), lipoproteins, globulins, and red blood cells (RBCs).
HSA is the most abundant plasma protein and is vital in drug binding. It contains distinct drug-binding sites, with different drugs exhibiting affinity for specific sites. There are three main drug-binding domains for HSA: sites I, II, and III. These domains are further...

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Related Experiment Video

Updated: Jul 7, 2026

Synthesis, Hemoglobin Encapsulation and Biorthogonal PEGylation in Hierarchically Porous UiO-66 Nanoparticles for Oxygen Delivery Applications
09:24

Synthesis, Hemoglobin Encapsulation and Biorthogonal PEGylation in Hierarchically Porous UiO-66 Nanoparticles for Oxygen Delivery Applications

Published on: May 8, 2026

Modulation of O2 Affinity and Enzymatic Activity of Core‒Shell Structured Hemoglobin Nanoparticles.

Ryo Hoshiya1, Tomoka Araki1, Teruyuki Komatsu1

  • 1Department of Applied Chemistry, Graduate School of Science and Engineering, Chuo University, Bunkyo-ku, Tokyo, Japan.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|July 6, 2026
PubMed
Summary

Researchers developed novel hemoglobin-based oxygen carriers (HBOCs) using nanoparticles. These advanced HBOCs offer tunable oxygen affinity and enhanced antioxidant properties, improving stability and reducing haptoglobin binding for potential red blood cell substitutes.

Keywords:
artificial bloodenzymesheme proteinshemoglobin‐based O2 carrierproteins

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Biofunctionalization of Magnetic Nanomaterials
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Biofunctionalization of Magnetic Nanomaterials

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Using Magnetometry to Monitor Cellular Incorporation and Subsequent Biodegradation of Chemically Synthetized Iron Oxide Nanoparticles
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Using Magnetometry to Monitor Cellular Incorporation and Subsequent Biodegradation of Chemically Synthetized Iron Oxide Nanoparticles

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Last Updated: Jul 7, 2026

Synthesis, Hemoglobin Encapsulation and Biorthogonal PEGylation in Hierarchically Porous UiO-66 Nanoparticles for Oxygen Delivery Applications
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Using Magnetometry to Monitor Cellular Incorporation and Subsequent Biodegradation of Chemically Synthetized Iron Oxide Nanoparticles
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Using Magnetometry to Monitor Cellular Incorporation and Subsequent Biodegradation of Chemically Synthetized Iron Oxide Nanoparticles

Published on: February 27, 2021

Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Biochemistry

Background:

  • Hemoglobin-based oxygen carriers (HBOCs) are explored as red blood cell substitutes.
  • Optimizing oxygen affinity and stability of oxygenated hemoglobin (oxy Hb) is crucial for HBOC performance.
  • Current HBOCs face challenges with stability and undesirable interactions.

Purpose of the Study:

  • To precisely modulate oxygen (O2) affinity and enzymatic antioxidant activity in core-shell structured stroma-free Hb nanoparticles (X-SFHbNPs).
  • To create versatile HBOCs with tunable O2 transport and antioxidant capabilities.
  • To investigate the structural integrity and stability of Hb within the nanoparticles.

Main Methods:

  • Preparation of low-affinity nanoparticles (X-SFHbNP^L) from deoxy Hb (T-state).
  • Circular dichroism (CD) analysis to assess Hb structure under oxygenated conditions.
  • Blending high- and low-affinity nanoparticles to fine-tune O2 affinity.
  • Incorporation of catalase (Cat), superoxide dismutase (SOD), and carbonic anhydrase (CA) into Hb nanoparticles.

Main Results:

  • Core Hb retained T-state structure even when oxygenated.
  • Blending nanoparticles allowed fine-tuning of O2 affinity.
  • POx-SFHbNP preserved intrinsic enzyme activities (Cat, SOD, CA).
  • POx-Hb(Cat/SOD/CA)NPs showed enhanced enzymatic activities.
  • X-SFHbNPs exhibited excellent oxidation resistance with negligible metHb formation.
  • X-SFHbNPs demonstrated reduced binding affinity toward haptoglobin.

Conclusions:

  • Multifunctional Hb nanoparticles offer a versatile platform for advanced HBOCs.
  • Tunable O2 transport and antioxidant capabilities are achievable.
  • These nanoparticles show promise as improved red blood cell substitutes with enhanced stability and reduced immunogenicity.