Protein Adsorption On Poly(N-vinylpyrrolidone)-Modified Material Surfaces Prepared By Surface-Initiated Atom Transfer Radical

The uncontrolled, non–specific adsorption of proteins onto the biomaterial surfacecan cause the complex cascade of undesired events when biomedical polymer materialscontact with human blood. Thus, prevention or inhibition of protein adsorption onsurfaces is an important means of improving the biocompatibility of biomaterials. Inthis study, surfaces grafted by poly(N-vinylpyrrolidone)(PVP) and PVP copolymerbrushes were prepared by surface–initiated atom transfer radical polymerization(SI-ATRP). We investigate the plasma protein adsorptions and cell adhesions on thesesurfaces. This study lays an foundation for constructing novel multi–functionalbiomedical polymer materials.1. We developed a method to modify silicon surfaces with good protein resistanceand specific cell attachment. A silicon surface was initially deposited using apoly(NVP-b-HEMA) film through SI-ATRP and then further immobilized using a shortarginine-glycine-aspartate(RGD)peptide. Our results demonstrate that theRGD-modified surfaces can suppress non-specific adsorption of proteins and induce theadhesion of L929cells.2. A new method for the modification of poly(dimethylsiloxane)(PDMS)elastomer surfaces with hydrophilic PVP has been developed. PVP chains were graftedfrom the PDMS surface by SI-ATRP. It was shown that both protein adsorption and celladhesion were inhibited significantly on the PVP-modified PDMS surfaces compared tounmodified controls. It is concluded that modification by SI-ATRP grafting of PVP isan effective method for the preparation of anti-biofouling PDMS materials.3. Well-controlled polymerization of N-vinylpyrrolidone (NVP) on PDMS surfacesby SI-ATRP was carried out by a silanization method. The silanization method wasemployed to form an adhesion layer for initiator attachment. The modification processis a pure chemical method. It doesn’t need expensive equipments such as vacuum UVand can treat the internal surface of materials with special shapes. Our resultsdemonstrate that the RGD-modified surfaces (Si-RGD) can effectively suppressnon-specific protein adsorption, cell and bacterial adhesion.