Human plasma protein adsorption to elastin-like polypeptide nanoparticles

被引:15
|
作者
Bahniuk, Markian S. [1 ]
Alshememry, Abdullah K. [2 ,3 ]
Unsworth, Larry D. [1 ]
机构
[1] Univ Alberta, Dept Chem & Mat Engn, Edmonton, AB T6G 1H9, Canada
[2] King Saud Univ, Dept Pharmaceut, Coll Pharm, Nanobiotechnol Unit, POB 2457, Riyadh 11451, Saudi Arabia
[3] King Saud Univ, Dept Pharmaceut, Coll Pharm, POB 2457, Riyadh 11451, Saudi Arabia
基金
加拿大自然科学与工程研究理事会;
关键词
ENDOTHELIAL-CELL ADHESION; ALBUMIN-BINDING SURFACES; IN-VITRO; THROMBUS FORMATION; PLATELET-ADHESION; MOLECULAR-WEIGHT; SERUM-ALBUMIN; PARTICLE-SIZE; FIBRINOGEN; BIOCOMPATIBILITY;
D O I
10.1116/6.0000027
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Elastin-like polypeptides (ELPs) are being developed for numerous biomedical applications. There is a limited understanding of ELP biocompatibility, with conflicting results in the literature. Protein adsorption is the fate determining event for blood-contacting biomaterials. The aim of this study is to elucidate the biocompatibility of ELP-based nanoparticles by examining the adsorbed proteome from platelet poor human plasma as a function of the physicochemical properties of these nanoparticles: diameter, amino acid hydrophobicity, and chain length. It was found that all ELP constructs had adsorbed an extremely large amount of albumin and high levels of immunoglobulin G and activated complement factor 3. Variations in the compositions of the proteomes across the eight nanoparticle systems studied were observed for plasminogen, fibronectin, activated fibrinogen, and coagulation modulating antithrombin and alpha(2) macroglobulin. Plasma clotting experiments showed that ELP-based nanoparticles slightly inhibited normal blood clotting, with shorter and/or more hydrophilic constructs showing a greater difference from the control than longer or more hydrophobic constructs. These results indicate that ELP nanoparticles, regardless of chain length, particle diameter, or amino acid hydrophobicity, may have the potential to stimulate a humoral immune response via immunoglobulin G and activated complement factor 3 despite the large amounts of albumin adsorbed at the blood-material interface.
引用
收藏
页数:15
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