Rational Design of a Reversible pH-Responsive Switch for Peptide Self-Assembly
Abstract
Peptide TZ1H, based on the heptad sequence of a coiled-coil trimer, undergoes fully reversible, pH-dependent self-assembly into long-aspect-ratio helical fibers. Substitution of isoleucine residues with histidine at the core d-positions of alternate heptads introduces a mechanism by which self-assembly is coupled to the protonation state of the imidazole side chain. Circular dichroism spectroscopy, transmission electron microscopy, and microrheology techniques revealed that the self-assembly of TZ1H coincides with a distinct coil-helix conformational transition that occurs within a narrow pH range near the pKa of the imidazole side chains of the core histidine residues.
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Achieving the desired balance between multiple target coiled-coil states often requires several rounds of trial-and-error and a detailed understanding of the energetic factors that discriminate between alternative topologies and oligomerization states.
“While this has been accomplished in a number of cases,18−31 achieving the desired balance between multiple target coiled-coil states often requires several rounds of trial-and-error and a detailed understanding of the energetic factors that discriminate between alternative topologies and oligomerization states.”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [20]
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Crystal structure of an isoleucine-zipper trimer
Harbury, P. B., Kim, P. S., & Alber, T. (1994) · Nature · doi:10.1038/371080a0 · Cited by 472 · see citing works
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Design of a Selective Metal Ion Switch for Self-Assembly of Peptide-Based Fibrils
Dublin, S. N., & Conticello, V. P. (2008) · Journal of the American Chemical Society · doi:10.1021/ja0775016 · Cited by 156 · see citing works
Self-citationNotari, E., Wood, C. W., & Michel, J. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c01695 · Cited by 4 · see citing works
- Authors
- Zimenkov, Y., Dublin, S. N., Ni, R., Tu, R. S., Breedveld, V., Apkarian, R. P., & Conticello, V. P.
- Affiliations
- Georgia Institute of Technology (US)
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-05-01
- Volume
- 128
- Issue
- 21
- Pages
- 6770-6771
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2008543105
- Cited by
- 212
- References
- 1
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 11 · 2023: 9 · 2022: 6 · 2021: 10 · 2020: 13 · 2019: 11 · 2018: 6 · 2017: 28 · 2016: 8 · 2015: 5 · 2014: 10 · 2013: 8 · 2012: 13
- FWCI
- 7.13
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of the American Chemical Society (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Energy
- Division of Chemistry
- Topics
- Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- peptide self-assembly, reversible self-assembly, helical fibers, histidine substitution, imidazole protonation, helix-coil transition, conformational change, peptide nanofibers
- MeSH terms
- Amino Acid Sequence, Circular Dichroism, Histidine, Hydrogen-Ion Concentration, Isoleucine, Molecular Sequence Data, Peptides, Protein Conformation, Microscopy, Electron, Transmission
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