Supramolecular Heterodimer Peptides Assembly for Nanoparticles Functionalization.
Fiche publication
Date publication
mars 2024
Journal
Advanced healthcare materials
Auteurs
Membres identifiés du Cancéropôle Est :
Dr MIRJOLET Céline, Pr PIVOT Xavier, Dr HARLEPP Sébastien, Dr DONZEAU Mariel, Dr KLYMCHENKO Andrey, Dr DETAPPE Alexandre, Dr SCHMUTZ Marc
Tous les auteurs :
Mathieu C, Ghosh S, Draussin J, Gasser A, Jacquot G, Banerjee M, Gupta T, Schmutz M, Mirjolet C, Tillement O, Lux F, Klymchenko A, Donzeau M, Pivot X, Harlepp S, Detappe A
Lien Pubmed
Résumé
Nanoparticle (NP) surface functionalization with proteins, including monoclonal antibodies (mAbs), mAb fragments, and various peptides, has emerged as a promising strategy to enhance tumor targeting specificity and immune cell interaction. However, these methods often rely on complex chemistry and suffer from batch-dependent outcomes, primarily due to limited control over the protein orientation and quantity on NP surfaces. To address these challenges, we present a novel approach based on the supramolecular assembly of two peptides to create a heterotetramer displaying V Hs on NP surfaces. This approach effectively targets both tumor-associated antigens (TAAs) and immune cell-associated antigens. In vitro experiments showcased its versatility, as we biofunctionalized various NP types, including liposomes, PLGA NPs, and ultrasmall silica-based NPs, and evaluated the V Hs targeting of known TAAs (HER2 for breast cancer, CD38 for multiple myeloma) and an immune cell antigen (NKG2D for natural killer (NK) cells). In in vivo studies using a HER2+ breast cancer mouse model, our approach demonstrated enhanced tumor uptake, retention, and penetration compared to the behavior of nontargeted analogs, affirming its potential for diverse applications. This article is protected by copyright. All rights reserved.
Référence
Adv Healthc Mater. 2024 03 5;:e2304250