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Vince Conticello

Vince Conticello

Biomolecular Chemistry

Chemistry Building
Department of Chemistry
Emory University
Emerson 203
Atlanta, GA 30322



B.S. University of Delaware, 1985; Ph.D., Norhtwestern University, 1990; Postdoctoral Research Fellow, California Institute of Technology, 1991; University of Massachusetts, 1992

National Science Foundation Early Faculty CAREER Award (1999-2003), Herman Frasch Foundation Fellow (1997-2002), N.S.F. Predoctoral Fellow; SOHIO Predoctoral Fellow.

Research Interests

My research interests lie primarily in the synthesis, characterization, and applications of materials with controlled microstructures, particularly novel biomaterials. The application of organic and biological materials in complex technologies, including biomedical applications, requires the ability to specify the structure and properties of the material precisely at the primary level. The ultimate goal in this respect is the synthesis of "intelligent" materials in which changes occurring at the molecular level act cooperatively to induce a well-defined, macroscopic response. Biological materials based on protein polymers have advantages over conventional organic polymers for these types of applications since in vivo protein expression ensures absolute specificity of the structural parameters, i.e., molecular size, composition, sequence, and stereochemistry, for the nascent polypeptide (Figure 1). Utilizing the principles of protein structure and the concepts of material science as a guide, non-natural protein-based materials can be designed that are capable of self-assembly into unique geometries on the basis of their primary structure. These materials form the basis for a new generation of "designer" biomaterials in which both structural and functional properties can be programmed into the polymer at the molecular level.

Synthesis of Biologically Responsive Polypeptides

The genetically directed biosynthesis of protein polymers enables the modular assembly of hybrid polypeptides consisting of alternating blocks of a structural domain and a biologically competent recognition motif. The structural domain is comprised of tandem repeats of an oligopeptide sequence that is capable of self organization into a well-defined, three dimensional structure, e.g., silk, elastin, collagen, and keratin. The nature of the structural domain determines the physical characteristics of the protein polymer such as crystallinity, ability to form crosslinks, and gel or film forming capacity. The biological recognition motifs, which can consist of short, linear peptide sequences or entire, autonomously folded protein modules, are incorporated for their functional characteristics, e.g. as enzyme modification and cleavage sites, cell binding sites, or antibody epitopes. These domains are interspersed throughout the supporting matrix of the structural protein polymer and can potentially modify its properties upon interaction with a biological substrate. These types of materials should find application as agents of controlled release, as biological sensing devices, or as cellular scaffolds.
Patterned Protein Arrays

Conventional approaches for the immobilization of biomolecules on surfaces are limited in applicability due to the lack of specificity in the derivatization process, typically a covalent cross-linking process. One method to circumvent this problem is to employ strongly interacting polypeptide subunits--one of which is immobilized on the surface and the other is fused to the target protein--to drive the specific assembly of the active complex on the surface.

An example of this procedure utilizes the high affinity intermolecular association of charge complementary, amphiphilic a-helices into a specific hetero-dimeric coiled coil as the driving force for the assembly process. Positively charged lysine residues on one helix and negatively charged glutamic acid residues on the other strongly destabilizes homodimer formation by charge repulsion. The two polypeptides spontaneously dimerize affording the a-helical coiled coil with nanomolar affinity. The derivatization of a target surface with a specific a-helical protomer enables it to selectively recognize and bind to a complementary sequence fused to the target protein. The incorporation of helical recognition domains with different binding specificities allows the independent targeting of proteins with different activities to the surface. This technique can be coupled with conventional photolithographic methods to afford spatially addressable arrays of proteins on a surface, each with a distinct and uniquely definable activity. This method could be employed for the immobilization of biomolecules or even whole cells on a surface in patterned arrays that would be useful for the construction of multi-analyte biosensors. The orientation of the individual biomolecules could be specified accurately with micron resolution.

Recent Publications

Yao, X.L.; Conticello, V.P. and Hong, M. "nvestigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR" Mag. Reson. Chem, 2004, 42, 267-275.

Zimenkov, Y.; Conticello, V.; Guo, L. and Thiyagarajan "Rational design of a nanoscale helical scaffold derived from self-assembly of a dimeric coiled coil motif" Tetrahedron, 2004, 60, 7237-7246.

Apkarian, R.P.; Wright, E.R.; Seredyuk, V.A.; Eustis, S. Lyon, A.L.; Conticello, V.P. and Menger, F. "In-lens cryo-high resolution scanning electron microscopy: methodologies for molecular imaging of self-assembled organic hydrogels" Microsc Microanal, 2003, 9, 286-295.

Wright, E.R.; Conticello, V.P. and Apkarian, R.P. "Morphological characterization of elastin-mimetic block copolymers utilizing cryo- and cryoetch- HRSEM" Microsc Microanal, 2003, 9, 171-182.

Hong, M.; Isailovic, D.; McMillan, R.A. and Conticello, V.P. "Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis" Biopolymers, 2003, 70, 158-168.

Lu, K.; Jacob, J.; Thiyagaajan, P.; Conticello, V.P. and Lynn, D.G. "Exploiting amyloid fibril lamination for nanotube assembly" Am Chem Soc, 2003, 125, 6391-6393.


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