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Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
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Conformational Dynamics in Extended RGD-Containing Peptides.

William R Lindemann1, Alexander J Mijalis2, José L Alonso3,4

  • 1Department of Materials Science and Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States.

Biomacromolecules
|May 30, 2020
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Disordered binding sites in peptides enhance cell adhesion potency. Flanking residues and transient hydrogen bonds near the RGD sequence are crucial for integrin binding in biomaterials.

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Area of Science:

  • Biomaterials Science
  • Molecular Biology
  • Biochemistry

Background:

  • The Arginine-Glycine-Aspartic acid (RGD) tripeptide is widely used in biomaterials to promote cell adhesion.
  • However, the potency of free or surface-bound RGD is significantly lower than that of the RGD domain within natural proteins.

Purpose of the Study:

  • To investigate how flanking residues influence the conformational dynamics and binding affinity of RGD-containing peptides.
  • To understand the role of transient structures and disorder in the RGD binding site's potency.

Main Methods:

  • Design and synthesis of peptides with varying lengths, derived from fibronectin, containing the RGD sequence.
  • Measurement of conformational dynamics and transient structures of the RGD active site.
  • Assessment of integrin binding affinities.

Main Results:

  • Peptide binding site disorder is essential for RGD peptide potency.
  • Transient hydrogen bonding near the RGD site impacts peptide binding energy landscape and affinity.
  • These effects are independent of longer-range folding interactions.

Conclusions:

  • Short RGD sequences alone do not fully replicate the integrin-targeting properties of extracellular matrix proteins.
  • Peptide binding is a holistic event, necessitating consideration of flanking residues in biomaterial design.
  • Larger peptide fragments beyond the direct binding site should be considered for effective functional biomaterials.