The question of how the primary sequence of a protein determines its three-dimensional structure remains one of the central challenges in structural biology. Our approach focuses on making de novo designs of peptides and proteins that adopt predetermined secondary and tertiary structures.

At the Conticello Lab, we design synthetic helical peptide filaments inspired by naturally occurring filamentous protein assemblies. These natural systems—including actin, tubulin homologues, flagellin, and pili—exhibit remarkable structural precision and diverse functionalities that we aim to replicate in synthetic systems for applications in controlled release, cargo transport, locomotion, energy transduction, and signal transduction.

The challenge lies in achieving the level of structural control observed in native biological assemblies for synthetic systems. Our research seeks to understand the sequence-structure relationships that govern self-assembly processes and to decipher the structural principles necessary for reliable de novo design of self-assembling peptides.