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Related Concept Videos

Targeted Cancer Therapies02:57

Targeted Cancer Therapies

The targeted cancer therapies, also known as “molecular targeted therapies,” take advantage of the molecular and genetic differences between the cancer cells and the normal cells. It needs a thorough understanding of the cancer cells to develop drugs that can target specific molecular aspects that drive the growth, progression, and spread of cancer cells without affecting the growth and survival of other normal cells in the body.
There are several types of targeted therapies against specific...
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Tumor Immunotherapy

Immunotherapy is a treatment that boosts or manipulates the immune system to fight diseases, including cancer. For instance, by stimulating an immune response through vaccinations against viruses that cause cancers, like hepatitis B virus and human papillomavirus, these diseases can be prevented. Nonetheless, some cancer cells can avoid the immune system due to their rapid mutation and division. The immune response to many cancers involves three phases: elimination, equilibrium, and escape.
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In humans, more than 80% of the genome gets transcribed. However, only around 2% of the genome codes for proteins. The remaining part produces non-coding RNAs which includes ribosomal RNAs, transfer RNAs, telomerase RNAs, and regulatory RNAs, among other types. A large number of regulatory non-coding RNAs have been classified into two groups depending upon their length – small non-coding RNAs, such as microRNA, which are less than 200 nucleotides in length, and long non-coding RNA (lncRNA)...
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Related Experiment Video

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A Flow Cytometry-Based Cell Surface Protein Binding Assay for Assessing Selectivity and Specificity of an Anticancer Aptamer
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A Flow Cytometry-Based Cell Surface Protein Binding Assay for Assessing Selectivity and Specificity of an Anticancer Aptamer

Published on: September 13, 2022

Tumor-specific protein human galectin-1 interacts with anticancer agents.

Sabato D'Auria1, Lidia Petrova, Constance John

  • 1Laboratory for Molecular Sensing, Institute of Protein Biochemistry, CNR, Via P. Castellino, 111, 80131 Naples, Italy.

Molecular Biosystems
|October 14, 2009
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Summary

Recombinant human galectin-1 (hGal-1) binds to porphyrins used in cancer photodynamic therapy (PDT). This interaction suggests hGal-1

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Published on: July 12, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Therapy

Background:

  • Recombinant human galectin-1 (hGal-1) is a tumor-specific lectin.
  • Porphyrin compounds are crucial in photodynamic therapy (PDT) for cancer treatment.
  • Lectins can bind to both carbohydrate and non-carbohydrate ligands.

Purpose of the Study:

  • To investigate the novel binding activity of hGal-1 to porphyrin compounds.
  • To explore the potential of hGal-1 as a delivery molecule in PDT.

Main Methods:

  • Studied Zn-porphyrin (ZnTPPS) interaction with hGal-1 using porphyrin fluorescence emission.
  • Measured binding of Mn/Au-porphyrins and adenine to hGal-1 via intrinsic protein fluorescence quenching.
  • Analyzed binding curves and used TNS fluorescent probe to identify hydrophobic regions.

Main Results:

  • hGal-1 exhibits high-affinity binding to Zn-, Mn-, and Au-porphyrins with dissociation constants (K(D)) of 0.6-1.5 microM.
  • Binding data suggest a single binding site for porphyrins or adenine on hGal-1.
  • hGal-1 interacts with TNS, indicating the presence of hydrophobic regions and multiple binding sites for TNS in dimeric hGal-1.

Conclusions:

  • hGal-1 demonstrates significant porphyrin-binding capacity, classifying it as a porphyrin-binding protein.
  • The high affinity and binding characteristics suggest hGal-1's potential as a targeting delivery molecule for PDT applications.
  • hGal-1's dual binding ability (carbohydrate and non-carbohydrate) broadens its potential applications in targeted therapies.