Probing the molecular determinants of the activation of toll-like receptor 2/6 by amyloid nanostructures through directed peptide self-assembly-Reference-Cited by-同舟云学术

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Probing the molecular determinants of the activation of toll-like receptor 2/6 by amyloid nanostructures through directed peptide self-assembly

Published:2024 Issue: Volume: Page:
ISSN:1744-683X
Container-title:Soft Matter
language:en
Short-container-title:Soft Matter

Author:

Kihal Nadjib¹²³,Archambault Marie-Jeanne¹²,Babych Margaryta¹²,Nazemi Ali¹³^ORCID,Bourgault Steve¹²^ORCID

Affiliation:

1. Department of Chemistry, Université du Québec à Montréal. C.P.8888, Succursale Centre-Ville, Montréal, H3C 3P8, Canada

2. Quebec Network for Research on Protein Function, Engineering and Applications (PROTEO), Québec, Canada

3. Quebec Centre for Advanced Materials, QCAM, Montreal, Canada

Abstract

The self-assembly of short β-peptide was modulated by introducing N- and C-terminal electrostatic capping motifs in order to elucidate the structural requirements of the activation of TLR2/TLR6 immune receptor by amyloid nanostructures.

Funder

Natural Sciences and Engineering Research Council of Canada

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SM/D4SM00638K

Reference62 articles.

1. Biological and bioinspired materials: Structure leading to functional and mechanical performance

2. Protein Assemblies: Nature-Inspired and Designed Nanostructures

3. Lipopeptide Derivatives of Bacterial Lipoprotein Constitute Potent Immune Adjuvants Combined with or Covalently Coupled to Antigen or Hapten

4. Application of Amyloid-Based Hybrid Membranes in Drug Delivery

5. Vaccination Strategies Based on Bacterial Self-Assembling Proteins as Antigen Delivery Nanoscaffolds

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