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Repulsive Backbone-Backbone Interactions Modulate Access to Specific and Unspecific Binding Sites on Surface-Bound

Theresa M Lutz1, Matthias Marczynski1, Maximilian J Grill2

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Removing sulfate groups from mucin glycoproteins unexpectedly reduces small molecule binding. This suggests that anionic motifs influence mucin structure and accessibility, impacting protective functions.

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Structural Biology

Background:

  • Mucin glycoproteins form the protective mucus barrier against pathogens.
  • Mucin-degrading enzymes target anionic glycan chains like sulfate and sialic acid.
  • The structural role of anionic motifs in mucin function is not fully understood.

Purpose of the Study:

  • To investigate the impact of sulfate group removal on mucin binding properties.
  • To explore the influence of anionic motifs on mucin conformation and accessibility.

Main Methods:

  • Enzymatic removal of sulfate groups from mucins.
  • Assessing small molecule binding efficiency to modified mucins.
  • Numerical modeling of mucin macromolecule structure and dynamics.

Main Results:

  • Enzymatic desulfation significantly reduced both specific and unspecific small molecule binding to mucins.
  • This reduction occurred even when binding partners did not target sulfate motifs.
  • Numerical simulations indicated that anionic motifs maintain an elongated mucin conformation via repulsion.
  • Loss of sulfate groups led to a more compacted mucin structure, restricting binding site accessibility.

Conclusions:

  • Anionic motifs, particularly sulfate groups, play a crucial role in maintaining mucin structure and function.
  • The removal of sulfate groups alters mucin conformation, impacting its ability to bind other molecules.
  • Understanding glycan contributions to mucin structure is vital for elucidating their diverse biological roles.