TY - JOUR
T1 - Assembly and recognition mechanisms of glycosylated PEGylated polyallylamine phosphate nanoparticles
T2 - A fluorescence correlation spectroscopy and small angle X-ray scattering study
AU - Perez Schmidt, Patricia
AU - Luedtke, Tanja
AU - Moretti, Paolo
AU - Di Gianvincenzo, Paolo
AU - Fernandez Leyes, Marcos
AU - Espuche, Bruno
AU - Amenitsch, Heinz
AU - Wang, Guocheng
AU - Ritacco, Hernan
AU - Polito, Laura
AU - Ortore, M. Grazia
AU - Moya, S. E.
N1 - Publisher Copyright:
© 2023
PY - 2023/9
Y1 - 2023/9
N2 - Hypothesis: Modification of polyallylamine hydrochloride (PAH) with heterobifunctional low molecular weight polyethylene glycol (PEG) (600 and 1395 Da), and subsequent attachment of mannose, glucose, or lactose sugars to PEG, can lead to formation of polyamine phosphate nanoparticles (PANs) with lectin binding affinity and narrow size distribution. Experiments: Size, polydispersity, and internal structure of glycosylated PEGylated PANs were characterized by transmission electron microscopy (TEM), dynamic light scattering (DLS) and small angle X-ray scattering (SAXS). Fluorescence correlation spectroscopy (FCS) was used to study the association of labelled glycol-PEGylated PANs. The number of polymer chains forming the nanoparticles was determined from the changes in amplitude of the cross-correlation function of the polymers after formation of the nanoparticles. SAXS and fluorescence cross-correlation spectroscopy were used to investigate the interaction of PANs with lectins: concanavalin A with mannose modified PANs, and jacalin with lactose modified ones. Findings: Glyco-PEGylated PANs are highly monodispersed, with diameters of a few tens of nanometers and low charge, and a structure corresponding to spheres with Gaussian chains. FCS shows that the PANs are single chain nanoparticles or formed by two polymer chains. Concanavalin A and jacalin show specific interactions for the glyco-PEGylated PANs with higher affinity than bovine serum albumin.
AB - Hypothesis: Modification of polyallylamine hydrochloride (PAH) with heterobifunctional low molecular weight polyethylene glycol (PEG) (600 and 1395 Da), and subsequent attachment of mannose, glucose, or lactose sugars to PEG, can lead to formation of polyamine phosphate nanoparticles (PANs) with lectin binding affinity and narrow size distribution. Experiments: Size, polydispersity, and internal structure of glycosylated PEGylated PANs were characterized by transmission electron microscopy (TEM), dynamic light scattering (DLS) and small angle X-ray scattering (SAXS). Fluorescence correlation spectroscopy (FCS) was used to study the association of labelled glycol-PEGylated PANs. The number of polymer chains forming the nanoparticles was determined from the changes in amplitude of the cross-correlation function of the polymers after formation of the nanoparticles. SAXS and fluorescence cross-correlation spectroscopy were used to investigate the interaction of PANs with lectins: concanavalin A with mannose modified PANs, and jacalin with lactose modified ones. Findings: Glyco-PEGylated PANs are highly monodispersed, with diameters of a few tens of nanometers and low charge, and a structure corresponding to spheres with Gaussian chains. FCS shows that the PANs are single chain nanoparticles or formed by two polymer chains. Concanavalin A and jacalin show specific interactions for the glyco-PEGylated PANs with higher affinity than bovine serum albumin.
KW - FCS
KW - Glycans
KW - Lectin specific binding
KW - PEGylation
KW - Polyamine phosphate nanoparticles
KW - Protein corona
KW - SAXS
UR - http://www.scopus.com/inward/record.url?scp=85157971934&partnerID=8YFLogxK
U2 - 10.1016/j.jcis.2023.04.136
DO - 10.1016/j.jcis.2023.04.136
M3 - Article
C2 - 37156153
AN - SCOPUS:85157971934
SN - 0021-9797
VL - 645
SP - 448
EP - 457
JO - Journal of Colloid and Interface Science
JF - Journal of Colloid and Interface Science
ER -