Surface energy components of a dye-ligand immobilized pHEMA membranes: Effects of their molecular attracting forces for non-covalent interactions with IgG and HSA in aqueous media
Yükleniyor...
Tarih
2005
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Elsevier
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
In the present paper, we report the study of the adsorption behaviour of human immunoglobulin G (IgG), human serum albumin (HSA) and polyethylenimine (PEI) onto surfaces of Procion Green HE-4BD (PG) immobilized poly(hydroxyethylmethacrylate) (pHEMA) membranes. The adsorption behaviour of the IgG and HSA onto surfaces of the PG-PEI complexed membrane was also studied. Surface wettability and hydrophilicity of all the membranes were investigated by static contact angle measurements. The measurements of the contact angle to various test liquids, i.e., water, glycerol, formamide, diiodomethane (DIM) and ethylene glycol on the investigated membranes were made by sessile drop method. In accordance to the Young equation, the smaller the surface tension of the test liquid, the smaller becomes the contact angles measured on all the investigated membranes surfaces. The highest contact angles were obtained with water, whereas ethylene glycol gave the lowest contact angles for all the tested membranes. Component and parameters of the surface free energy of all the investigated membranes were calculated from measured contact angle values using two methods (the geometric mean by Fowkes and acid-base by van Oss). HSA adsorption was enhanced after complexation of PEI with the immobilized dye-ligand. The adsorption of proteins and PEI significantly changed both the contact angles and component of surface free energies of the investigated membranes. (c) 2005 Elsevier B.V. All rights reserved.
Açıklama
Anahtar Kelimeler
dye-ligands, affinity membranes, HSA, IgG, PEI, adsorption, contact angle, surface energy
Kaynak
International Journal Of Biological Macromolecules
WoS Q Değeri
Q3
Scopus Q Değeri
Q1
Cilt
37
Sayı
5
Künye
closedAccess
