Surface Avidity of Anionic Polypeptide Coatings on Layer‐by‐Layer Nanoparticles Target Cancer‐Associated Amino Acid Transporters

I Ivan S. Pires (Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA) M Margaret M. Billingsley (Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA) E Ezra Gordon (Department of Chemical Engineering Massachusetts Institute of Technology 21 Ames Street Cambridge Massachusetts 02139 USA) A Andrew J. Pickering (Department of Chemical Engineering) E Eva Cai (Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA) G Gonzalo J. Esparza (Department of Chemical Engineering Massachusetts Institute of Technology 21 Ames Street Cambridge Massachusetts 02139 USA) M Mae L. Pryor (Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA) A Alexander D. Stoneman (Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA) A Aidan Kindopp (Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA) D Darrell J. Irvine P Paula T. Hammond (Department of Chemical Engineering)

Abstract

Abstract Tumor‐targeted drug delivery enhances therapeutic efficacy while minimizing toxicity. Layer‐by‐layer nanoparticles (LbL‐NPs) coated with anionic polypeptides selectively bind to cancer cells, though the mechanisms have been unclear. Here, we integrated in silico and in vitro approaches—including gene expression analysis, receptor inhibition, and AI‐based protein modeling—to show that poly(L‐glutamate) (PLE)‐coated LbL‐NPs bind with high avidity to SLC1A5, a glutamine transporter overexpressed in cancer. We also discovered that PLE clusters SLC1A5 on the cell membrane, promoting prolonged cell surface retention. Poly(L‐aspartate) (PLD)‐coated NPs similarly bind SLC1A5 but also interact with faster internalizing transporters of anionic amino acids. Correlation analyses across cancer cell lines confirmed a strong link between transporter expression and nanoparticle (NP) association. These findings demonstrate that dense glutamate or aspartate presentation through electrostatically adsorbed polypeptides enables selective targeting of overexpressed transporters, providing a mechanistic framework for receptor‐targeted delivery that leverages metabolic characteristics of a range of solid tumor types.

Article Details

Volume / Issue Vol. 65, Issue 8
Published February 16, 2026
ISSN 1433-7851
Publisher Wiley

Journal Info

Angewandte Chemie International Edition

Wiley

ISSN: 1433-7851 Physical Sciences

Authors (11)

I

Ivan S. Pires

Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA

M

Margaret M. Billingsley

Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA

E

Ezra Gordon

Department of Chemical Engineering Massachusetts Institute of Technology 21 Ames Street Cambridge Massachusetts 02139 USA

A

Andrew J. Pickering

Department of Chemical Engineering

E

Eva Cai

Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA

G

Gonzalo J. Esparza

Department of Chemical Engineering Massachusetts Institute of Technology 21 Ames Street Cambridge Massachusetts 02139 USA

M

Mae L. Pryor

Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA

A

Alexander D. Stoneman

Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA

A

Aidan Kindopp

Koch Institute for Integrative Cancer Research Massachusetts Institute of Technology 500 Main Street Cambridge Massachusetts 02139 USA

D

Darrell J. Irvine

P

Paula T. Hammond

Department of Chemical Engineering