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Related Concept Videos

Peptide Bonds02:43

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Stem cells are undifferentiated cells that divide and produce different types of cells. Ordinarily, cells that have differentiated into a specific cell type are post-mitotic—that is, they no longer divide. However, scientists have found a way to reprogram these mature cells so that they “de-differentiate” and return to an unspecialized, proliferative state. These cells are also pluripotent like embryonic stem cells—able to produce all cell types—and are therefore...
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Stem cells are undifferentiated cells that divide and produce more stem cells or progenitor cells that differentiate into mature, specialized cell types. All the cells in the body are generated from stem cells in the early embryo, but small populations of stem cells are also present in many adult tissues including the bone marrow, brain, skin, and gut. These adult stem cells typically produce the various cell types found in that tissue—to replace cells that are damaged or to continuously...
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Embryonic stem (ES) cells are undifferentiated pluripotent cells, meaning they can produce any cell type in the body. This gives them tremendous potential in science and medicine since they can generate specific cell types for use in research or to replace body cells lost due to damage or disease.
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Embryonic Stem Cells00:57

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Embryonic stem (ES) cells were first discovered in mice in 1981 by Martin Evans. In 1998, James Thomson identified a method to isolate embryonic stem cells from humans. Human embryonic stem cells (hESCs) are obtained from 3-5 day old embryos that remain unused after an in vitro fertilization procedure.
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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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Liquid-cell Transmission Electron Microscopy for Tracking Self-assembly of Nanoparticles
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Stem cell tracking using effective self-assembled peptide-modified superparamagnetic nanoparticles.

Lei Gu1, Xue Li, Jing Jiang

  • 1Huaxi MR Research Center (HMRRC), Department of Radiology, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, 610041, China. wuminscu@scu.edu.cn.

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|June 20, 2018
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Summary
This summary is machine-generated.

Peptide-modified superparamagnetic iron oxide nanoparticles (SPIONs) enhance stem cell labeling for improved MRI tracking. These biocompatible peptide-SPIONs show increased efficiency and safety in mesenchymal stem cells (MSCs).

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Biomedical Imaging

Background:

  • Superparamagnetic iron oxide nanoparticles (SPIONs) are biocompatible MRI contrast agents.
  • SPIONs are utilized for stem cell labeling and tracking.
  • Peptide amphiphiles (PAs) have applications in tissue engineering and drug delivery.

Purpose of the Study:

  • To design a self-assembled peptide amphiphile (PA).
  • To conjugate PA to SPIONs for enhanced stem cell labeling.
  • To evaluate the efficacy and safety of peptide-SPIONs for mesenchymal stem cell (MSC) tracking via MRI.

Main Methods:

  • Design and synthesis of self-assembled peptide amphiphiles.
  • Conjugation of PAs to SPIONs.
  • Labeling of rat mesenchymal stem cells (MSCs) with peptide-SPIONs.
  • In vitro and in vivo evaluation of labeling efficiency, cellular uptake, MRI contrast enhancement (T2 relaxivity), and cytotoxicity.

Main Results:

  • Peptide-SPIONs demonstrated improved internalization and labeling efficiency in MSCs.
  • Enhanced T2 relaxivity was observed both in vitro and in vivo.
  • The peptide-SPIONs were found to be non-toxic to MSCs.
  • Improved MRI contrast for labeled stem cells.

Conclusions:

  • Self-assembled peptide-modified SPIONs are effective for labeling MSCs.
  • These peptide-SPIONs offer enhanced MRI contrast and tracking capabilities.
  • The developed nanomaterials show potential for in vivo stem cell tracking using MRI.