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

被引:4
|
作者
Bucci, Raffaella [4 ]
Maggioni, Daniela [1 ]
Locarno, Silvia [2 ]
Ferretti, Anna Maria [3 ]
Gelmi, Maria Luisa [4 ]
Pellegrino, Sara [4 ]
机构
[1] Univ Milan, Dipartimento Chim, I-20133 Milan, Italy
[2] Univ Milan, Dipartimento Fis Aldo Pontremol, I-20133 Milan, Italy
[3] Consiglio Nazl Ric SCITEC CNR, Ist Sci & Tecnol Chim Giulio Natta, I-20138 Milan, Italy
[4] Univ Milan, DISFARM Dipartimento Sci Farmaceut, Sez Chim Gen & Organ A Marchesini, I-20133 Milan, Italy
关键词
HELICAL PEPTIDE; SIZE; ACID; ALBUMIN; SERUM; BIOCOMPATIBILITY; STABILITY; DELIVERY; LIGANDS; SHAPE;
D O I
10.1021/acs.langmuir.1c01981
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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 alpha,beta-peptides containing the repeating unit of a diaryl beta(2,3)-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.
引用
收藏
页码:11365 / 11373
页数:9
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