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Proteomimetic surface fragments distinguish targets by function.

Attila Tököli1, Beáta Mag1, Éva Bartus1,2

  • 1Department of Medical Chemistry, University of Szeged Dóm tér 8 H6720 Szeged Hungary martinek.tamas@med.u-szeged.hu.

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Summary
This summary is machine-generated.

Foldameric local surface mimetics (LSMs) effectively mimic protein surfaces for drug discovery. These LSM probes can identify binding sites on challenging protein targets, aiding in the development of new therapeutics.

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Area of Science:

  • Biochemistry
  • Medicinal Chemistry
  • Drug Discovery

Background:

  • Fragment-centric design aims to create protein surface mimetics.
  • Developing locally biomimetic structures remains a significant challenge.

Purpose of the Study:

  • To construct foldameric local surface mimetic (LSM) libraries.
  • To evaluate protein affinity patterns, ligand promiscuity, and protein druggability of LSMs.

Main Methods:

  • Constructed foldameric LSM libraries based on H14 helices.
  • Utilized pull-down assays with diverse protein targets.
  • Analyzed binding affinities, patterns, and side chain enrichment.

Main Results:

  • LSM probes demonstrated sufficient binding affinity for orthosteric and non-orthosteric sites.
  • Binding tendencies correlated with target interactome size.
  • LSMs distinguished between structurally similar proteins, indicating low promiscuity.
  • Binding patterns mimicked native protein-protein interfaces.

Conclusions:

  • Foldameric LSMs serve as effective probes and building blocks for undruggable protein interfaces.
  • LSMs show potential in fragment-centric drug discovery approaches.
  • These mimetics offer a promising strategy for targeting complex protein interactions.