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Related Concept Videos

Hemoglobin01:24

Hemoglobin

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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...
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Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

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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,...
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Gene Families01:57

Gene Families

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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...
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Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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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...
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Related Experiment Video

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Encapsulating Cytochrome c in Silica Aerogel Nanoarchitectures without Metal Nanoparticles while Retaining Gas-phase Bioactivity
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Hemoglobin-Based Nanoarchitectonic Assemblies as Oxygen Carriers.

Yi Jia1, Li Duan2, Junbai Li1

  • 1Beijing National Laboratory for Molecular Sciences, CAS Key Lab of Colloid, Interface and Chemical Thermodynamics, Institute of Chemistry, Chinese Academy of Sciences, Beijing, 100190, China.

Advanced Materials (Deerfield Beach, Fla.)
|October 20, 2015
PubMed
Summary
This summary is machine-generated.

Artificial oxygen carriers using hemoglobin offer a promising alternative to blood transfusions. Advances in nano-biotechnology have led to the development of acellular and cellular hemoglobin-based oxygen carriers with significant advantages.

Keywords:
hemoglobinlayer-by-layer assemblynanoarchitectonicsoxygen carriers

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Area of Science:

  • Biotechnology
  • Nanomedicine
  • Biochemistry

Background:

  • Traditional blood transfusions face challenges including limited supply and safety concerns.
  • Hemoglobin is a natural oxygen-transport molecule with ideal properties for artificial carriers.
  • There is a significant clinical demand for effective artificial oxygen carriers.

Purpose of the Study:

  • To review recent advancements in hemoglobin-based oxygen carriers (HBOCs).
  • To highlight progress in both acellular and cellular HBOCs.
  • To discuss the advantages of novel HBOCs over existing blood substitutes.

Main Methods:

  • Review of recent scientific literature on HBOCs.
  • Analysis of developments in nano-biotechnology applied to hemoglobin.
  • Categorization of HBOCs into acellular and cellular types.

Main Results:

  • Hemoglobin assemblies show great development as artificial oxygen carriers.
  • Acellular and cellular HBOCs represent key areas of progress.
  • Novel HBOCs demonstrate advantages compared to traditional oxygen carriers.

Conclusions:

  • Hemoglobin-based oxygen carriers are a rapidly developing field.
  • Nanotechnology is crucial for creating advanced HBOCs.
  • These novel carriers hold significant potential for clinical applications and future research.