ADSORPTION OF ADHESIVE PROTEINS FROM THE MARINE MUSSEL, MYTILUS-EDULIS, ON POLYMER-FILMS IN THE HYDRATED STATE USING ANGLE-DEPENDENT X-RAY PHOTOELECTRON-SPECTROSCOPY AND ATOMIC-FORCE MICROSCOPY

Citation
Am. Baty et al., ADSORPTION OF ADHESIVE PROTEINS FROM THE MARINE MUSSEL, MYTILUS-EDULIS, ON POLYMER-FILMS IN THE HYDRATED STATE USING ANGLE-DEPENDENT X-RAY PHOTOELECTRON-SPECTROSCOPY AND ATOMIC-FORCE MICROSCOPY, Langmuir, 13(21), 1997, pp. 5702-5710
Citations number
33
Categorie Soggetti
Chemistry Physical
Journal title
ISSN journal
07437463
Volume
13
Issue
21
Year of publication
1997
Pages
5702 - 5710
Database
ISI
SICI code
0743-7463(1997)13:21<5702:AOAPFT>2.0.ZU;2-S
Abstract
The adsorption of mussel adhesive protein (MAP) from the marine mussel Mytilus edulis has been investigated on polystyrene (PS) and poly(oct adecyl methacrylate) (POMA) surfaces using angle dependent X-ray photo electron spectroscopy (XPS) and atomic force microscopy(AFM). AFM imag es previously published in the dehydrated state using contact mode are compared with images acquired in the hydrated state using fluid Tappi ng Mode to assess the contribution that hydration has on the architect ure of the adsorbed proteins. To further characterize the adsorbed pro tein layer XPS analysis was performed at liquid nitrogen (LN2) tempera ture without dehydrating the samples and at room temperature after the surfaces were dehydrated. The differences observed upon dehydration c an be attributed to the strength of the interactions between MAP and t he two surfaces. The AFM and XPS data indicate that adsorbed MAP is st abilized on the surface of the PS through interactions that prevent th e protein layer from being disrupted upon dehydration. The adsorbed MA P on the POMA surface is representative of a loosely bound protein lay er that becomes highly perturbed upon dehydration.