Fluorophore-Conjugated Diphenylalanine Peptides Reveal Self-Sorting in a Multicomponent Supramolecular System
7 affiliations
- 1Department of Oral Biology, The Goldschleger School of Dental Medicine, Gray Faculty of Medical & Health Sciences, Tel-Aviv University, Tel-Aviv 6997801, Israel
- 2Jan Koum Center for Nanoscience and Nanotechnology, Tel-Aviv University, Tel-Aviv 6997801, Israel
- 3The Center for Physics & Chemistry of Living Systems, Tel-Aviv University, Tel-Aviv 6997801, Israel
- 4School of Chemistry, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel-Aviv University, Tel-Aviv 6997801, Israel
- 5Department of Physiology and Pharmacology, Gray School of Medical Sciences, Gray Faculty of Medical and Health Sciences, Tel Aviv University, Tel-Aviv 6997801, Israel
- 6Department of Chemical Research Support, The Weizmann Institute of Science, Rehovot 7610001, Israel
- 7Sagol School of Neuroscience, Tel Aviv University, Tel-Aviv 6997801, Israel
Abstract
The interplay between distinct molecular building blocks in multicomponent supramolecular systems can lead to co-assembly or self-sorting, yet distinguishing between these modes of organization remains challenging. Here, we developed two intrinsically fluorescent derivatives of the self-assembling dipeptide diphenylalanine (FF): nitrobenzoxadiazole-conjugated FF (NBD-FF) and a coumarin-conjugated tert-butyloxycarbonyl-protected FF derivative (BocFF-DAC). Both derivatives formed fibrillar assemblies while exhibiting spectrally distinct fluorescence, enabling their direct visualization by confocal microscopy. Single-crystal X-ray diffraction of NBD-FF revealed an extended hydrogen-bonded lattice in which the NBD moiety participates directly in intermolecular interactions, including aromatic, hydrophobic, and hydrogen-bonding contacts. This finding demonstrates that the fluorophore acts as an active structural element rather than a passive label. When NBD-FF and BocFF-DAC were assembled together, confocal microscopy revealed predominantly spatially distinct fibrillar populations with limited overlap, consistent with preferential self-sorting rather than uniform co-assembly. These findings establish fluorophore-conjugated short peptides as intrinsically traceable building blocks for investigating multicomponent supramolecular organization, while highlighting that fluorophore conjugation can simultaneously enable visualization and influence the assembly.
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BibTeX
@article{dan2026fluorophoreconjugated,
title = {{Fluorophore-Conjugated Diphenylalanine Peptides Reveal Self-Sorting in a Multicomponent Supramolecular System}},
author = {Yoav Dan and Omri Shelef and Marina Green Buzhor and Linda J. W. Shimon and Ronit Satchi-Fainaro and Doron Shabat and Lihi Adler-Abramovich},
journal = {International Journal of Molecular Sciences},
year = {2026},
month = oct,
doi = {10.3390/ijms27219661},
url = {https://www.mdpi.com/1422-0067/27/21/9661},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Fluorophore-Conjugated Diphenylalanine Peptides Reveal Self-Sorting in a Multicomponent Supramolecular System
AU - Yoav Dan
AU - Omri Shelef
AU - Marina Green Buzhor
AU - Linda J. W. Shimon
AU - Ronit Satchi-Fainaro
AU - Doron Shabat
AU - Lihi Adler-Abramovich
PY - 2026
DA - 2026/10/28
JO - International Journal of Molecular Sciences
DO - 10.3390/ijms27219661
UR - https://www.mdpi.com/1422-0067/27/21/9661
AB - The interplay between distinct molecular building blocks in multicomponent supramolecular systems can lead to co-assembly or self-sorting, yet distinguishing between these modes of organization remains challenging. Here, we developed two intrinsically fluorescent derivatives of the self-assembling dipeptide diphenylalanine (FF): nitrobenzoxadiazole-conjugated FF (NBD-FF) and a coumarin-conjugated tert-butyloxycarbonyl-protected FF derivative (BocFF-DAC). Both derivatives formed fibrillar assemblies while exhibiting spectrally distinct fluorescence, enabling their direct visualization by confocal microscopy. Single-crystal X-ray diffraction of NBD-FF revealed an extended hydrogen-bonded lattice in which the NBD moiety participates directly in intermolecular interactions, including aromatic, hydrophobic, and hydrogen-bonding contacts. This finding demonstrates that the fluorophore acts as an active structural element rather than a passive label. When NBD-FF and BocFF-DAC were assembled together, confocal microscopy revealed predominantly spatially distinct fibrillar populations with limited overlap, consistent with preferential self-sorting rather than uniform co-assembly. These findings establish fluorophore-conjugated short peptides as intrinsically traceable building blocks for investigating multicomponent supramolecular organization, while highlighting that fluorophore conjugation can simultaneously enable visualization and influence the assembly.
SN - 1422-0067
ER -