Sequence‐Tunable Phase Behavior and Intrinsic Fluorescence in Dynamically Interacting Peptides
Abstract
A conceptual framework towards understanding biological condensed phases is emerging, derived from biological, biomimetic, and synthetic sequences. However, de novo peptide condensate design remains a challenge due to an incomplete understanding of the structural and interactive complexity. We designed peptide modules based on a simple repeat motif composed of tripeptide spacers (GSG, SGS, GLG) interspersed with adhesive amino acids (R/H and Y). We show, using sequence editing and a combination of computation and experiment, that n→π* interactions in GLG backbones are a dominant factor in providing sufficient backbone structure, which in turn regulates the water interface, collectively promoting liquid droplet formation. Moreover, these R(GLG)Y and H(GLG)Y condensates unexpectedly display sequence‐dependent emission that is a consequence of their non‐covalent network interactions, and readily observable by confocal microscopy.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Nov 16, 2023
- Source ID
- 10.1002/ange.202311479
Entities
People
- Deborah Sementa
- Dhwanit Dave
- Rachel S Fisher
- Rein V Ulijn
- Shana Elbaum‐garfinkle
- Tong Wang
Organizations
- Air Force Office of Scientific Research
- CUNY Graduate School and University Center
- City University of New York
- Hunter College