title: Specific and nonspecific interaction forces between Escherichia coli and silicon nitride, determined by poisson statistical analysis.
abstract: The nature of the physical interactions between Escherichia coli JM109 and a model surface (silicon nitride) was investigated in water via atomic force microscopy (AFM). AFM force measurements on bacteria can represent the combined effects of van der Waals and electrostatic forces, hydrogen bonding, steric interactions, and perhaps ligand-receptor type bonds. It can be difficult to decouple these forces into their individual components since both specific (chemical or short-range forces such as hydrogen bonding) and nonspecific (long-range colloidal) forces may be present in the overall profiles. An analysis is presented based on the application of Poisson statistics to AFM adhesion data, to decouple the specific and nonspecific interactions. Comparisons with classical DLVO theory and a modified form of a van der Waals expression for rough surfaces were made in order to help explain the nature of the interactions. The only specific forces in the system were due to hydrogen bonding, which from the Poisson analysis were found to be -0.125 nN. The nonspecific forces of 0.155 nN represent an overall repulsive interaction. These nonspecific forces are comparable to the forces calculated from DLVO theory, in which electrostatic-double layer interactions are added to van der Waals attractions calculated at the distance of closest approach, as long as the van der Waals model for "rough" spherical surfaces is used. Calculated electrostatic-double layer and van der Waals interactions summed to 0.116 nN. In contrast, if the classic (i.e., smooth) sphere-sphere model was used to predict the van der Waals forces, the sum of electrostatic and van der Waals forces was -7.11 nN, which appears to be a large overprediction. The Poisson statistical analysis of adhesion forces may be very useful in applications of bacterial adhesion, because it represents an easy way to determine the magnitude of hydrogen bonding in a given system and it allows the fundamental forces to be easily broken into their components.
authors.affiliation: Department of Chemical Engineering, Worcester Polytechnic Institute, Worcester, Massachusetts 01609, USA.
authors.forename: Nehal I
authors.initials: NI
authors.lastname: Abu-Lail
authors.forename: Terri A
authors.initials: TA
authors.lastname: Camesano
mesh_terms: D001422:Bacterial Adhesion / Q000502:physiology*; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006860:Hydrogen Bonding; D018625:Microscopy, Atomic Force; D016012:Poisson Distribution; D011485:Protein Binding; D017655:Silicon Compounds / Q000737:chemistry*; D055672:Static Electricity; D013499:Surface Properties; D013816:Thermodynamics
chemical_list: D029968:Escherichia coli Proteins; D017655:Silicon Compounds; C032734:silicon nitride