Webb Group

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Biomolecule Structure and Function at the Bio/Abio Interface

Summary: Proteins provide an extraordinary range of structures, properties, and functions that could be exploited for novel devices and materials if the biological molecule could be effectively integrated with standard inorganic platforms and devices.  To this end, there is currently great interest in integrating peptides and proteins onto abiological surfaces and materials reliably.  A significant impediment to the advancement of this area is the general observation that the three-dimensional structure and resulting function of biomolecules interacting with a surface or interface can be radically different than in solution, an unavoidable consequence of placing a deformable, solution-phase material in the artificial chemical, structural, and electrostatic environment that occurs on and near surfaces and interfaces. Our group is addressing this challenge with a multidisciplinary research program focused on the physical properties of biomolecules in carefully prepared surface environments.

Strategy:  The Webb group is developing surface chemical functionalization techniques that use noncovalent binding of proteins through long-range electrostatic forces that mimic biological protein-protein interaction mechanisms.  Using our extensive understanding of the chemical functionalization of ideal surfaces such as silicon and gold, our goal is to prepare surfaces on which small peptide motifs, such as an alpha-helix, beta-sheet, or even random coil, is covalently linked to the surface.  The protein motif carries amino acid side chains that will stabilize protein-protein interactions to present a binding surface to a protein introduced from solution.


By replicating the electrostatic interactions that normally enable large biomolecules to interact and function in a living cell, this strategy will coax proteins to remained folded and fully functional at inorganic substrates, thus integrating the structure and function of that protein with an artificial device or material. Furthermore, we are working with collaborators to use our experimental data to test and refine computational methods for predicting biomolecular structure at surfaces.

People:  Whitney Fies, Jeremy First, Santiago Sanchez

Publications: 
Dugger, J. W.; Webb, L. J.  "Preparation and Characterization of Biofunctionalized Inorganic Surfaces."  Langmuir 2015, 31, 10331-10340.  pdf

Dugger, J. W.; Webb, L. J.  "Fibrillar Structures Formed by Covalently-Bound Short Beta-Stranded Peptides on Self-Assembled Monolayers."  Langmuir 2015, 31, 3441-3450. pdf

Raigoza, A. F.; Dugger, J. W.; and Webb, L. J.  "Review: Recent Advances and Current Challenges in Scanning Probe Microscopy of Biomolecular Surfaces and Interfaces."  ACS Appl. Mater. Interface. 2013, 5, 9249-9261.  pdf

Raigoza, A. F. and Webb, L. J.  "Molecularly Resolved Images of Peptide-Functionalized Gold Surfaces by Scanning Tunneling Microscopy."  J. Am. Chem. Soc. 2012, 134, 19354-19357.  pdf

Gallardo, I. F. and Webb, L. J.  "Demonstration of alpha-Helical Structure of Peptides Tethered to Gold Surfaces Using Surface Infrared and Circular Dichroic Spectroscopies."  Langmuir 2012, ASAP DOI: 10.1021/la204927q.  pdf






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