Faculty Advisor

Camesano, Terri Anne

Abstract

Protein adhesins are an important type of surface structure, and are components of some Gram-negative bacterial outer membranes, such as the LapA adhesin of Pseudomonas fluorescens. Atomic force microscopy (AFM) was used to characterize surface structures of P. fluorescens Pf0-1. AFM data was modeled using the Alexander - de Gennes (A-dG) relation for steric repulsion. We found that the lapG mutant strain of P. fluorescens behaved like a classical polymer brush, in which the spacing between molecules was very small (3.3 nm), which would allow intermolecular interactions between protein units. Taken together, our results and these recent studies support the finding that LapA adhesin conformation is related to irreversible bacterial adhesion.

Publisher

Worcester Polytechnic Institute

Date Accepted

December 2013

Major

Chemical Engineering

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Chemical Engineering

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