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Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Phthalic Acid Ester-Binding DNA Aptamer Selection, Characterization, and Application to an Electrochemical Aptasensor
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Structure-guided development of Pb2+-binding DNA aptamers.

Hehua Liu1, Yanqing Gao1, Johnsi Mathivanan2

  • 1Shanghai Public Health Clinical Center, State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, School of Life Sciences, Fudan University, 2005 Songhu Road, Yangpu District, Shanghai, 200438, People's Republic of China.

Scientific Reports
|January 11, 2022
PubMed
Summary

This study reveals the structural basis for lead(II) ion (Pb2+) binding to a thrombin binding aptamer (TBA). Understanding these G-quadruplex structures aids in developing better Pb2+ sensors.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Environmental Science

Background:

  • Lead(II) ion (Pb2+) pollution poses significant health and environmental risks.
  • DNA aptamers are used for Pb2+ detection, but their binding mechanisms are not fully understood.

Purpose of the Study:

  • To elucidate the structural mechanisms of Pb2+ binding to the thrombin binding aptamer (TBA).
  • To provide insights for developing improved Pb2+-detection aptamers.

Main Methods:

  • High-resolution crystal structure determination of Pb2+-TBA complexes.
  • Mutagenesis studies and circular dichroism (CD) spectroscopy.

Main Results:

  • Three high-resolution crystal structures of Pb2+-TBA complexes were determined, showing intramolecular G-quadruplex formation.
  • Pb2+ ions coordinate within the central G-tetrads with shorter distances compared to K+.
  • Specific linkers (T3T4, T12T13, and T7G8T9) were identified as crucial and adaptable for Pb2+ binding and aptamer structure.

Conclusions:

  • The study provides detailed structural insights into Pb2+-TBA interactions.
  • The findings facilitate the rational design and optimization of Pb2+-binding aptamers for sensing applications.