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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...
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,...
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...
Protein and Protein Structure02:15

Protein and Protein Structure

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 can...
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...
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 6, 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

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Non-functionalized carbon nanotube binding with hemoglobin.

Xiao C Wu1, W J Zhang, Ramaswami Sammynaiken

  • 1Department of Biomedical Engineering, University of Saskatchewan, Saskatoon, Saskatchewan, Canada.

Colloids and Surfaces. B, Biointerfaces
|April 1, 2008
PubMed
Summary
This summary is machine-generated.

Non-functionalized carbon nanotubes can bind with hemoglobin, a key protein in blood. This interaction, detectable by Raman spectroscopy, opens new avenues for biosensing applications, particularly for measuring hydrogen sulfide (H2S) levels.

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Functionalization of Single-walled Carbon Nanotubes with Thermo-reversible Block Copolymers and Characterization by Small-angle Neutron Scattering
09:12

Functionalization of Single-walled Carbon Nanotubes with Thermo-reversible Block Copolymers and Characterization by Small-angle Neutron Scattering

Published on: June 1, 2016

Area of Science:

  • Nanomaterials Science
  • Biochemistry
  • Analytical Chemistry

Background:

  • Carbon nanotubes (CNTs) show promise for biosensing and drug delivery.
  • Understanding CNT-protein interactions is crucial for their biological applications.
  • Previous research focused on functionalized CNTs, leaving non-functionalized CNT interactions less explored.

Purpose of the Study:

  • To investigate the binding behavior of non-functionalized carbon nanotubes with proteins.
  • To determine if this binding can be detected using Raman spectroscopy.
  • To explore potential applications of this interaction in biosensing.

Main Methods:

  • Characterization of hemoglobin binding to non-functionalized carbon nanotubes.
  • Utilizing Raman spectroscopy to identify and analyze the binding event.
  • Assessing the effect of binding on Raman luminescence properties.

Main Results:

  • Demonstrated for the first time that hemoglobin binds to non-functionalized carbon nanotubes.
  • Confirmed that this binding is detectable via changes in Raman spectra.
  • Observed no alteration in Raman luminescence under specific excitation/emission wavelengths post-binding.

Conclusions:

  • Non-functionalized carbon nanotubes can serve as a platform for detecting hemoglobin.
  • This finding enables the development of novel biosensors for blood analytes, such as hydrogen sulfide (H2S).
  • Suggests potential for non-functionalized CNTs in selectively binding other protein groups.