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Peer-reviewedCC BY 4.0Small (Weinheim an Der Bergstrasse, Germany)

Photo‐Switched Catalytic Amyloids

4 affiliations
  1. 1Department of Chemistry Ben‐Gurion University of the Negev Beer Sheva Israel
  2. 2Ilse Katz Institute (IKI) for Nanoscale Science and Technology Ben‐Gurion University of the Negev Beer Sheva Israel
  3. 3Department of Chemical Engineering Columbia University in the City of New York New York New York USA
  4. 4Avram and Stella Goldstein‐Goren Department of Biotechnology Engineering Ben‐Gurion University of the Negev Beer Sheva Israel

Abstract

Light–mediated assembly of catalytic agents furnishes powerful means for spatiotemporal control of chemical reactions. Here, we demonstrate photo‐switched hierarchical assembly of catalytic amyloid fibrils, through mixing an amphiphilic cross‐ß peptide with a merocyanine photo‐switch. The peptide monomers, comprising phenylalanine‐lysine repeats, do not self‐assemble in water because of the electrostatic repulsion between the positively charged lysine side chains; however, upon light‐induced merocyanine‐spiropyran transformation, amyloid fibrils were formed. Interestingly, increasing the mole ratio between the merocyanine photo‐switch and the peptide gave rise to a remarkable assembly of aligned elongated fibrils. The process was fully reversible as light turn‐off resulted in fibril disintegration. Notably, the photoinduced amyloid fibrils catalyzed hydrolysis of β‐lactam antibiotics, offering a platform for light‐mediated degradation of antibiotic pollutants in water. Microscopic and spectroscopic experiments reveal that the photoinduced transient catalytic amyloids were likely formed through π–π interactions between the spiropyran moieties and the aromatic residues of the phenylalanines, while electrostatic interactions between the negative sulfonates and lysine sidechains on the fibrils’ surface were responsible for the macroscale alignment. The amyloid‐merocyanine system represents a new concept for light‐regulated assembly of catalytic amyloids, which may have also played a role in prebiotic evolution processes.

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BibTeX
@article{bhaumik2026photoswitched,
  title = {{Photo‐Switched Catalytic Amyloids}},
  author = {Shubhra Kanti Bhaumik and Sisira Mambram Kunnath and Elad Arad and Einat Nativ‐Roth and Arunavo Chatterjee and Albert Batushansky and Nitzan Shauloff and Hanna Rapaport and Raz Jelinek},
  journal = {Small (Weinheim an Der Bergstrasse, Germany)},
  year = {2026},
  month = aug,
  doi = {10.1002/smll.75302},
  url = {https://doi.org/10.1002/smll.75302},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Photo‐Switched Catalytic Amyloids
AU  - Shubhra Kanti Bhaumik
AU  - Sisira Mambram Kunnath
AU  - Elad Arad
AU  - Einat Nativ‐Roth
AU  - Arunavo Chatterjee
AU  - Albert Batushansky
AU  - Nitzan Shauloff
AU  - Hanna Rapaport
AU  - Raz Jelinek
PY  - 2026
DA  - 2026/08/18
JO  - Small (Weinheim an Der Bergstrasse, Germany)
DO  - 10.1002/smll.75302
UR  - https://doi.org/10.1002/smll.75302
AB  - Light–mediated assembly of catalytic agents furnishes powerful means for spatiotemporal control of chemical reactions. Here, we demonstrate photo‐switched hierarchical assembly of catalytic amyloid fibrils, through mixing an amphiphilic cross‐ß peptide with a merocyanine photo‐switch. The peptide monomers, comprising phenylalanine‐lysine repeats, do not self‐assemble in water because of the electrostatic repulsion between the positively charged lysine side chains; however, upon light‐induced merocyanine‐spiropyran transformation, amyloid fibrils were formed. Interestingly, increasing the mole ratio between the merocyanine photo‐switch and the peptide gave rise to a remarkable assembly of aligned elongated fibrils. The process was fully reversible as light turn‐off resulted in fibril disintegration. Notably, the photoinduced amyloid fibrils catalyzed hydrolysis of β‐lactam antibiotics, offering a platform for light‐mediated degradation of antibiotic pollutants in water. Microscopic and spectroscopic experiments reveal that the photoinduced transient catalytic amyloids were likely formed through π–π interactions between the spiropyran moieties and the aromatic residues of the phenylalanines, while electrostatic interactions between the negative sulfonates and lysine sidechains on the fibrils’ surface were responsible for the macroscale alignment. The amyloid‐merocyanine system represents a new concept for light‐regulated assembly of catalytic amyloids, which may have also played a role in prebiotic evolution processes.
SN  - 1613-6810
SN  - 1613-6829
ER  -