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Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart, a...
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The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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Related Experiment Video

Updated: May 27, 2026

In Vitro Chemical Mapping of G-Quadruplex DNA Structures by Bis-3-Chloropiperidines
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Published on: May 12, 2023

β-Hairpin stabilization through an interstrand triazole bridge.

Veronica Celentano1, Donatella Diana, Lucia De Rosa

  • 1Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy.

Chemical Communications (Cambridge, England)
|December 3, 2011
PubMed
Summary

Stabilizing beta-hairpin peptides using a triazole linkage enhances their conformational stability. The triazole

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Last Updated: May 27, 2026

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Area of Science:

  • Medicinal Chemistry
  • Peptide Chemistry
  • Organic Synthesis

Background:

  • Beta-hairpin peptides are crucial structural motifs in many bioactive peptides.
  • Stabilizing these structures is key to developing effective therapeutics.
  • Current methods for stabilization often face challenges with metabolic stability.

Purpose of the Study:

  • To develop a novel method for conformationally stabilizing beta-hairpin peptides.
  • To investigate the impact of triazole linkage modifications on peptide structure.
  • To enable the design of metabolically stable beta-hairpin peptidomimetics.

Main Methods:

  • Synthesis of beta-hairpin peptides with a 1,4-disubstituted 1,2,3-triazole interstrand linkage.
  • Nuclear Magnetic Resonance (NMR) spectroscopy for conformational analysis.
  • Varying the number and position of methylene units on the triazole ring.

Main Results:

  • Successful conformational stabilization of beta-hairpin peptides was achieved.
  • Beta-hairpin content was found to be dependent on the triazole's substituent methylene units.
  • The triazole linkage provides a stable and tunable platform for peptide structure control.

Conclusions:

  • 1,4-disubstituted 1,2,3-triazole linkages effectively stabilize beta-hairpin peptide conformations.
  • Modulating the triazole substituents allows fine-tuning of peptide stability.
  • This approach facilitates the creation of metabolically stable peptidomimetics for therapeutic applications.