Surface　chemical　characteristics　of　biomedical　polymers,　which　are　determined　by　the　migration　and　rearrangement　of　polymeric　chains,　play　an　important　role　in　the　protein　adsorption.　In　this　work,　the　relationship　between　the　architectures　of　amphiphilic　polyesters　and　their　protein　adsorption　resistance　was　investigated.　Three　poly　(e{open}-caprolactone)s　containing　sulfobetaines　(PCL-b-PDEAS)　segments　with　linear,　four　arms　and　six　arms　star-shaped　architectures　were　synthesized　with　the　combination　of　ring-opening　polymerization　(ROP)　and　atom　transfer　radical　polymerization　(ATRP).　The　structures　of　the　amphiphiles　were　confirmed　by　1H　NMR　and　FTIR.　Water　contact　angles　(WCA)　and　X-ray　photoelectron　spectroscopy　(XPS)　were　used　to　study　the　surface　properties　of　the　amphiphilic　copolymer　films.　The　water　contact　angles　were　decreased　due　to　the　surface　migration　of　hydrophilic　segments.　Transmission　electron　microscopy　(TEM)　displayed　the　occurrence　of　microphase　separation　phenomena　for　PCL-b-PDEAS　above　glass　transition　temperature　(Tg).　The　results　showed　that　the　hydrophilic　segments　in　the　copolymers　would　migrate　to　the　surface　of　the　films,　which　resulted　in　the　surface　more　hydrophilic　to　resist　protein　adsorption.　The　adsorption　of　both　fibrinogen　(Fg)　and　bovine　serum　albumin　(BSA)　were　studied.　The　results　showed　that　protein　adsorption　was　depended　on　not　only　the　hydrophilic　chain　migration　but　also　the　shape　of　proteins.　©　2014.