Colloidal gold nanoparticles (GNPs) have found wide-ranging applications in nanomedicine due to their unique optical properties, ease of preparation, and functionalization. To avoid the formation of GNP aggregates in the physiological environment, molecules such as lipids, polysaccharides, or polymers are employed as GNP coatings. Here, we present the colloidal stabilization of GNPs using ultrashort α,β-peptides containing the repeating unit of a diaryl β2,3-amino acid and characterized by an extended conformation. Differently functionalized GNPs have been characterized by ultraviolet, dynamic light scattering, and transmission electron microscopy analysis, allowing us to define the best candidate that inhibits the aggregation of GNPs not only in water but also in mouse serum. In particular, a short tripeptide was found to be able to stabilize GNPs in physiological media over 3 months. This new system has been further capped with albumin, obtaining a material with even more colloidal stability and ability to prevent the formation of a thick protein corona in physiological media.

Exploiting Ultrashort α,β-Peptides in the Colloidal Stabilization of Gold Nanoparticles / R. Bucci, D. Maggioni, S. Locarno, A.M. Ferretti, M.L. Gelmi, S. Pellegrino. - In: LANGMUIR. - ISSN 0743-7463. - 37:38(2021 Sep 28), pp. 11365-11373. [10.1021/acs.langmuir.1c01981]

Exploiting Ultrashort α,β-Peptides in the Colloidal Stabilization of Gold Nanoparticles

R. Bucci
;
D. Maggioni;S. Locarno;A.M. Ferretti;M.L. Gelmi;S. Pellegrino
2021-09-28

Abstract

Colloidal gold nanoparticles (GNPs) have found wide-ranging applications in nanomedicine due to their unique optical properties, ease of preparation, and functionalization. To avoid the formation of GNP aggregates in the physiological environment, molecules such as lipids, polysaccharides, or polymers are employed as GNP coatings. Here, we present the colloidal stabilization of GNPs using ultrashort α,β-peptides containing the repeating unit of a diaryl β2,3-amino acid and characterized by an extended conformation. Differently functionalized GNPs have been characterized by ultraviolet, dynamic light scattering, and transmission electron microscopy analysis, allowing us to define the best candidate that inhibits the aggregation of GNPs not only in water but also in mouse serum. In particular, a short tripeptide was found to be able to stabilize GNPs in physiological media over 3 months. This new system has been further capped with albumin, obtaining a material with even more colloidal stability and ability to prevent the formation of a thick protein corona in physiological media.
Settore CHIM/03 - Chimica Generale e Inorganica
Settore CHIM/06 - Chimica Organica
Article (author)
File in questo prodotto:
File Dimensione Formato  
acs.langmuir.1c01981.pdf

accesso riservato

Tipologia: Publisher's version/PDF
Dimensione 5.67 MB
Formato Adobe PDF
5.67 MB Adobe PDF   Visualizza/Apri   Richiedi una copia
Manuscript (1).pdf

accesso aperto

Tipologia: Pre-print (manoscritto inviato all'editore)
Dimensione 1.76 MB
Formato Adobe PDF
1.76 MB Adobe PDF Visualizza/Apri
Pubblicazioni consigliate

Caricamento pubblicazioni consigliate

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/871192
Citazioni
  • ???jsp.display-item.citation.pmc??? 0
  • Scopus 1
  • ???jsp.display-item.citation.isi??? 1
social impact