title: Antifouling properties of oligo(lactose)-based self-assembled monolayers.
abstract: The antifouling (AF) properties of oligo(lactose)-based self-assembled monolayers (SAMs), using four different proteins, zoospores of the green alga Ulva linza and cells of the diatom Navicula incerta, were investigated. The SAM-forming alkylthiols, which contained 1, 2 or 3 lactose units, showed significant variation in AF properties, with no differences in wettability. Non-specific adsorption of albumin and pepsin was low on all surfaces. Adsorption of lysozyme and fibrinogen decreased with increasing number of lactose units in the SAM, in agreement with the generally observed phenomenon that thicker hydrated layers provide higher barriers to protein adsorption. Settlement of spores of U. linza followed an opposite trend, being greater on the bulkier, more hydrated SAMs. These SAMs are more ordered for the larger saccharide units, and it is therefore hypothesized that the degree of order, and differences in crystallinity or stiffness between the surfaces, is an important parameter regulating spore settlement on these surfaces.
authors: a Division of Molecular Physics , IFM, Linköping University , Linköping , Sweden.
authors: Roni
authors: R
authors: Nugraha
authors: John A
authors: JA
authors: Finlay
authors: Sophie
authors: S
authors: Hill
authors: Timmy
authors: T
authors: Fyrner
authors: Wetra
authors: W
authors: Yandi
authors: Maureen E
authors: ME
authors: Callow
authors: James A
authors: JA
authors: Callow
authors: Thomas
authors: T
authors: Ederth
mesh_terms: D000327:Adsorption; D057219:Biofouling / Q000517:prevention & control*; D017377:Diatoms / Q000187:drug effects* / Q000502:physiology; D007785:Lactose / Q000737:chemistry*; D015394:Molecular Structure; D011506:Proteins / Q000737:chemistry; D013499:Surface Properties; D044445:Ulva / Q000187:drug effects* / Q000502:physiology; D017155:Wettability
chemical_list: D011506:Proteins; D007785:Lactose
keywords: Navicula incerta; Ulva linza; marine biofouling; oligo(lactose); protein resistance; self-assembled monolayer