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Reconstruction of enzymatic catalytic domains within fully artificial systems has become an interesting but challenging subject, largely due to limited understanding of their evolutionary processes. A long-standing opportunity in the generation of artificial or miniature enzymes has been to design building units capable of performing similar chemistry without the structural complexity of full proteins. Herein, by using a reductionist approach, we explore the sequence\u2013structure\u2013activity landscapes of enzyme evolution by investigating minimal amyloid-forming analogous peptides. Our results reveal that amyloid peptides without encoding canonical catalytic amino acids (like Lys, Ser, His, Glu\/Asp) or metal cofactors can nevertheless catalyze ester hydrolysis through fibril-dependent substrate binding. Minor sequence variations alter supramolecular organization and reorganize solvent-exposed terminal groups, creating distinct catalytic microenvironments and activities. Combining experiments with molecular simulations, we show that these fibril surfaces present topologically different binding grooves that modulate the association of the model substrate. This sequence\u2013structure\u2013activity paradigm of de novo biocatalysts holds promise for predictable and robust construction of peptide-based new functional materials applicable in chemical and biochemical synthesis.<\/jats:p>","DOI":"10.1021\/acsami.6c15642","type":"journal-article","created":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T05:05:50Z","timestamp":1790831150000},"page":"54957-54969","source":"Crossref","is-referenced-by-count":0,"title":["Programmable Artificial Hydrolase Based on Minimalistic Cross-\u03b1\/Cross-\u03b2 Amyloid Assemblies"],"prefix":"10.1021","volume":"18","author":[{"given":"Sukantha","family":"Dey","sequence":"first","affiliation":[{"name":"Ashoka University , , , ,","place":["Sonipat, Haryana, India, 131029"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rohit","family":"Kumar","sequence":"additional","affiliation":[{"name":"Ashoka University , , , ,","place":["Sonipat, Haryana, India, 131029"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4218-0308","authenticated-orcid":true,"given":"Shayon","family":"Bhattacharya","sequence":"additional","affiliation":[{"name":"Bernal Institute, University of Limerick , , ,","place":["Limerick, Ireland, V94T9PX"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4830-552X","authenticated-orcid":true,"given":"Santu","family":"Bera","sequence":"additional","affiliation":[{"name":"Ashoka University , , , ,","place":["Sonipat, Haryana, India, 131029"]},{"name":"Kalinga Institute of Industrial Technology Deemed to be University , , , ,","place":["Bhubaneswar, Odisha, India, 751024"]},{"name":"Kalinga Institute of Industrial Technology Deemed to be University , , , ,","place":["Bhubaneswar, Odisha, India, 751024"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,10,1]]},"reference":[{"issue":"6817","key":"2026101406072761400_cit1","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1038\/35051731","article-title":"Combinatorial and computational challenges for biocatalyst design","volume":"409","author":"Arnold","year":"2001","journal-title":"Nature"},{"issue":"11","key":"2026101406072761400_cit2","doi-asserted-by":"publisher","first-page":"4707","DOI":"10.1021\/acs.chemrev.9b00664","article-title":"Prebiotic Peptides: Molecular Hubs in the Origin of Life","volume":"120","author":"Frenkel-Pinter","year":"2020","journal-title":"Chem. 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