Analogies in the two-dimensional spatial arrangement of adsorbed proteins and adhering bacteria: bovine serum albumin and Streptococcus sanguis 12.
J Biomater Sci Polym Ed
; 3(1): 85-94, 1991.
Article
en En
| MEDLINE
| ID: mdl-1786246
Neither proteins nor bacteria adsorb or adhere homogeneously to a substratum surface. The final two-dimensional spatial arrangement depends on a complicated interplay between protein-protein (bacterium-bacterium) and protein (bacterium)-substratum interactions and the prevailing hydrodynamic conditions. In this paper, results are presented of two separate experiments in which bovine serum albumin (BSA) was adsorbed to, or Streptococcus sanguis 12 was deposited on substrata with different wettabilities in a search for analogies in the two-dimensional spatial arrangement of the absorbed proteins and adhering bacteria. The spatial arrangement of adsorbed BSA, visualized by transmission electron microscopy on replicas of the surface, was island-like on substrata with a low wettability and well distributed on substrata with a high wettability. The spatial arrangement of adhering S. sanguis 12 was observed directly by light microscopy during the experiment and showed a relatively large collection of near-neighbour sites on the low wettability substrata compared with the high wettability substrata. Thus, it seems that the occurrence of island-like structures in protein adsorption is concurrent with a large collection of near-neighbour sites in bacterial adhesion. As a possible explanation for the above analogy, it is suggested that proteins or bacteria are insufficiently immobilized on low wettability substrata owing to weak interaction forces, and they can move over the substratum surface to yield the two-dimensional spatial arrangements observed.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Polímeros
/
Streptococcus sanguis
/
Albúmina Sérica Bovina
Límite:
Animals
Idioma:
En
Revista:
J Biomater Sci Polym Ed
Asunto de la revista:
ENGENHARIA BIOMEDICA
Año:
1991
Tipo del documento:
Article
País de afiliación:
Países Bajos
Pais de publicación:
Reino Unido