AFM Life Science Workshop - November 4, 2008

Staff scientists from the University of Washington and Veeco's Nano-Bio lab will highlight the the BioScope II in a morning presentation with an afternoon demonstration workshop to follow. Learn about how atomic force microscopy is providing new insights to life science researchers around the world on topics as diverse as neurodegenerative diseases, metabolic dysfunction, infectious diseases, single molecule interactions, implantable medical devices, and many others.

Staff scientists from Veeco's Nano-Bio lab will highlight the latest addition to our suite of bio AFM instruments - the BioScope II. After the lecture, the BioScope II will be demonstrated.

Tuesday, November 4th - Room 215 Fluke Hall, Center for Nanotechnology, University of Washington, Seattle, WA 98195

RSVP:  No fee to attend, but seating is limited.  To register visit AFM_Workshop  


8:30 AM:     Registration and Continental Breakfast
9:00 AM:      Welcome - Paul Charell, Veeco Instruments
9:10 AM:   How Atomic Force Microscopy is Advancing Life Science Research
Dr. Andrea Slade, Veeco   Instruments

Numerous applications demonstrate the unique information that AFM can provide biologists, from imaging single molecules and tissue to  visualization of real time events, such as molecular pulling,  ligand/receptor interactions, membrane reorganization and cell signaling events.  AFM principles will be discussed focusing on primary imaging techniques used for biological samples as well as sample preparation, probe selection, and tips on data acquisition.

9:40 AM:   Mechanisms of Protein Binding to Solids -Molecular Imaging via AFM
Mehmet Sarikaya, Director, Genetically Engineered Materials Science and Engineering Center, University of Washington

Understanding the mechanism of binding and assembly of proteins on solid surfaces are significant as these interfaces provide the bridge between the inorganic and biological entities. Normally, strong interface formations in engineered materials require phase compatibility, lattice matching and strong bonding normally described as chemisorptions or physisorption. In biological systems, however, molecular recognition may also require molecular conformational changes leading to materials recognition, binding, diffusion, and supramolecular self assembly. Here we show AFM investigation of molecular binding, diffusion, and thin film formation of inorganic binding peptides, developed at GEMSEC, and their molecular genetic fusion constructs used as molecular synthesizers, erectors, and assemblers, e.g., in cell adhesion, targeted enzyme immobilization, and biofunctionalization as utility in molecular engineering and medicine.

10:20 AM:    Interactions of the Streptococcal C5a Peptidase with Human Fibronectin 
Dr. Jim Hull    Chemical Engineering  University of Washington
  Understanding the mechanisms of bacterial adhesion to host tissues and the evasion of the hosts defense mechanisms is vital to the development of methods to prevent infection and research to cure infection. Group B Strep (/Streptococcus agalactae/) is a leading cause of meningitis, pneumonia and sepsis in neonates and immunocompromised adults in Western countries. The cell surface endopeptidase streptococcal C5a peptidase (Scp) plays a key role in both pathogenesis and evasion of the hosts defense mechanism. Scp has the interesting property that it will bind to adsorbed fibronectin (Fn), but will not bind to soluble Fn. This dissertation presents a detailed examination of the mechanisms of the Scp-Fn interactions. Scp was recently identified as an Fn adhesin, but the affinity of Scp for Fn was unknown. The affinity measured by Surface Plasmon Resonance (SPR) was in the nM range, which is biologically significant. Since Scp only binds to adsorbed Fn, the structure and reactivity of Fn films on mica was studied with single molecule force spectroscopy, x-ray photoelectron spectroscopy, time-of-flight secondary ion mass spectrometry, and SPR. It was found that the reactivity of the Fn film is dependent on the Fn surface concentration. Live GBS were imaged and probed with Fn tethered to an AFM tip. When the tips were blocked with excess Scp no binding to GBS was observed, indicating that the interaction is specific for Fn. Lastly, single molecule force spectroscopy was used to probe Fn on a surface with Scp tethered to the AFM probe. This work demonstrates that the surface endopeptidase Scp is a Fn adhesin, and the adhesion depends on the surface density of Fn.
11:00 AM:    BREAK
11:15 AM:  BioScope II Demonstration: Combining AFM and optical microscopy
Dr. Kim Reed, Veeco Instruments
12:00 PM: Workshop Ends
1:00 PM:        Scheduled Demonstrations

   RSVP:  No fee to attend, but seating is limited.  To register visit AFM_Workshop  

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