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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Tunable multivalent Fe(II)-based glycoassemblies as mimetics for native high-mannose glycans

Emerson Hall1, Yu-Shien Sung2, Chad W Priest2

  • 1Department of Biochemistry and Molecular Biophysics, University of California San Diego, La Jolla CA.

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Chemically defined multivalent glycan displays mimic high mannose glycans (HMGs) and inhibit lectin binding. These Fe(II) iminopyridine complexes offer tunable interactions for biological applications.

Palabras clave:
glicanoslectinasquímica de carbohidratosglicobiologíaquímica biofísicacomplejos de hierroinhibidoresuniónafinidadmiméticos

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Área de la Ciencia:

  • Química de Carbohidratos
  • Química Biofísica
  • Glicobiología

Sus antecedentes:

  • Los glicanos de alta cantidad de manosa (HMG) son cruciales en procesos biológicos como el plegamiento de proteínas y la inmunidad.
  • Las lectinas se unen a los HMG a través de interacciones multivalentes, que involucran múltiples azúcares y sitios de unión de lectinas.

Objetivo del estudio:

  • Crear pantallas de glicanos multivalentes químicamente definidas utilizando complejos de iminopiridina Fe(II).
  • Investigar la interacción de estas pantallas con Griffithsin monomérica (mGRFT) como lectina modelo.
  • Explorar su potencial como miméticos de HMG e inhibidores competitivos.

Principales métodos:

  • Síntesis de complejos de iminopiridina Fe(II) con valencia de glicano controlada, longitud del brazo y visualización de manosa.
  • Caracterización de interacciones utilizando interferometría de biolayer (BLI), calorimetría de titulación isotérmica (ITC) y espectroscopía de RMN.
  • Modificaciones moleculares sistemáticas para ajustar la afinidad de unión.

Principales resultados:

  • Los ensamblajes de glicanos Fe(II) exhibieron un rango de afinidad de unión (KD) de >1000 veces con mGRFT.
  • La afinidad de unión fue ajustable alterando la longitud de la cadena del sacárido y el número de azúcares mostrados.
  • Demostró la capacidad de estos ensamblajes para imitar los HMG nativos.

Conclusiones:

  • Los ensamblajes de glicanos Fe(II) sintonizables sirven como miméticos efectivos para los glicanos de alta cantidad de manosa.
  • Estos ensamblajes pueden funcionar como inhibidores competitivos de la unión de glicanos nativos por lectinas.
  • El estudio proporciona una plataforma para el diseño de moléculas basadas en glicanos con propiedades de unión controladas.