Vincent P. Conticello
Professor
Emory University
Talk Information
Peptide Materials
16 June 2025, 05:05pm - 05:30pm, in the Pacific Jewel Ballroom
L60 – Peptide-Based Nanomaterials: Progress from Structural Analysis to Design
Professor Vincent P. Conticello is a Professor in the Department of Chemistry at Emory University. He also serves as the Scientific Director of the Robert P. Apkarian Integrated Electron Microscopy Core, where he oversees advanced imaging techniques to support research in structural biology and materials science.
Academic Background
Dr. Conticello earned his B.S. in Chemistry from the University of Delaware in 1985. He completed his Ph.D. in Chemistry at Northwestern University in 1990, working under Professor Tobin Marks. Following his doctoral studies, he conducted postdoctoral research at the California Institute of Technology with Professor Robert Grubbs and at the University of Massachusetts Amherst with Professor David Tirrell. He joined the faculty at Emory University in 1995.
Research Focus
Professor Conticello's research centers on the design, synthesis, and characterization of synthetic materials derived from the self-assembly of sequence-specific proteins and peptides. His lab aims to create analogues of biologically derived protein filaments to understand the sequence-structure relationship that underlies the self-assembly process. These insights guide the reliable structural prediction and sequence design of self-assembling peptides, with applications in nanotechnology and materials science.
Notable Contributions
Dr. Conticello has significantly advanced the field of peptide-based nanomaterials through his work on synthetic helical peptide filaments. His research has provided valuable insights into the mechanisms of protein self-assembly and has contributed to the development of novel materials with potential applications in drug delivery, biosensing, and nanofabrication.
Awards and Honors
Professor Conticello's contributions have been recognized with several awards, including the NSF CAREER Award and the Herman Frasch Foundation Fellowship. These honors reflect his commitment to excellence in research and education.
Professional Engagements
Beyond his research, Dr. Conticello is actively involved in mentoring students and advancing the field of chemistry through his leadership roles. As the Scientific Director of the Robert P. Apkarian Integrated Electron Microscopy Core, he facilitates interdisciplinary collaborations and supports cutting-edge research initiatives at Emory University.
Through his innovative research and dedication to education, Professor Vincent P. Conticello continues to make significant contributions to the fields of chemistry and materials science.
Peptide-Based Nanomaterials: Progress from Structural Analysis to Design
Department of Chemistry, Emory University, Atlanta, Georgia, USA
Historically, structurally defined materials on the nanometer length-scale have been challenging to rationally construct and difficult to structurally analyze. Sequence-specific biomolecules, i.e., peptides and nucleic acids, have advantages as design elements for construction of these types of nano-scale materials in that correlations can be drawn between sequence and higher order structure, potentially affording ordered assemblies in which functional properties can be controlled through the progression of structural hierarchy encoded at the molecular level.
However, the predictable design of self-assembled structures requires precise structural control of the interfaces between peptide subunits (protomers). In contrast to the robustness of protein tertiary structure, quaternary structure has been postulated to be labile with respect to mutagenesis of residues located at the protein-protein interface. Self-assembling peptide systems have been employed to interrogate the concept of quaternary structure designability within the structural context of synthetic filaments and nanotubes. These peptide systems provide an understanding of how minor sequence changes can translate into large changes in supramolecular structure.
The emergence of electron cryo-microscopy (cryo-EM) has enabled a revolution in the structural analysis of these peptide-based filaments at near-atomic resolution, which has provided significant evidence that the designability of protein interfaces is a critical consideration for control of supramolecular structure in self-assembling systems.