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Public reporting burden for this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the data needed, and completing and reviewing the collection of information. Send comments regarding this burden estimate or any other aspect of this collection of Information, including suggestions for reducing this burden, to Washington Headquarters Services, Directorate for Information Operations and Reports, 1215 Jefferson Davis Highway, Suite 1204, Arlington, VA 22202-4302, and to the Office of Management and Budget, Paperworlc Reduction Project (0704-01881, Washington, DC 20503. A6iNCY VSt ONLY (Leave blank)2. REPORT DATE 15.Aug.03 REPORT TYPE AND DATES COVERED MAJOR REPORT TITLE AND SUBTITLE"SPECIFIC AND SELECTIVE BIOSENSOR FOR SALMONELLA AND IT'S DETECTION IN THE ENVIRONMENT" FUNDING NUMBERS AUTHOR(S)CAPT OLSEN ERIC V PERFORMING ORGANIZATION NAME(S) AND ADDRESS(ES)AUBURN UNIVERSITY MAIN CAMPUS , 1998, O'Sullivan and Guilbault, 1999, Cavicacute, et al., 1999, Ivnitski, et al., 1999, 5 Kaspar et al., 2000. Acoustic waves in TSM are excited by the application of a radio frequency 6 alternating voltage to the piezoelectric crystal. Changes in the resonance frequency are usually 7 attributed to the effect of the added mass due to the binding at the solid-liquid interface. Acoustic 6The acoustic devices theory and biological applications were recently reviewed (Kaspar et 7 al., 2000, Cavicacute, et al., 1999, Ivnitski, et al., 1999. 8In our previous work we demonstrated the feasibility of a biosensor based on Langmuir-9 Blodgett monolayers of an antibody for the rapid and sensitive detection of Salmonella 10 typhimurium in liquid samples (Pathirana, et al., 2000). In the present work we investigated 11 specificity and selectivity of the biosensor under environmental conditions and after 12 environmental aging of the biosensors. Additionally, we studied the effects on the biosensor 13 signal of bacterial positioning at the liquid-surface interface.14 2. Materials and methods 19Three types of tests were employed to examine the reactivity of antibodies: 20(1) a dot blot ELISA test using nitrocellulose or nylon filters with antigen fixed and subjected to 21 chromogenic anti-mouse (for monoclonal antibody) or anti-animal-based antibody conjugated 22 with enzyme assay; (2) kit tests for target organisms; and (3) agglutination tests.

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Patented signal analytic algorithms applied to hydrophobically transformed, numerical amino acid sequences have previously been used to design short, protein‐targeted, L or D retro‐inverso peptides. These peptides have demonstrated allosteric and/or indirect agonist effects on a variety of G‐protein and tyrosine kinase coupled membrane receptors with 30% to over 80% hit rates. Here we extend these approaches to a globular protein target. We designed eight peptide ligands targeting an ELISA antibody responsive protein, β‐galactosidase, βGAL. Three of the eight 14mer peptides allosterically activated βGAL with ELISA methodology. Using Bayesian statistics, this 38% hit rate would have occurred 2 × 10−9 by chance. These peptides demonstrated binding site competitive or noncompetitive interactions, suggesting allosteric site multiplicity with respect to their βGAL binding‐mediated ELISA signal. Kinetic studies demonstrated the temperature dependence of the βGAL peptide binding functions. Using the van't Hoff relation, we found evidence for enthalpy–entropy compensation. This relation is often found for hydrophobic interactions in aqueous media, and is consistent with the postulated hydrophobic series encoding underlying our protein‐targeted, peptide design methods. It appears that our algorithmic, hydrophobic autocovariance eigenvector template approach to the design of allosteric peptides targeting membrane receptors may also be applicable to the design of peptide ligands targeting nonmembrane involved globular proteins. © 2006 Wiley Periodicals, Inc. Biopolymers 85: 38–59, 2007.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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