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However, previous studies used peptides that self\u2010assemble, limiting their potential for large\u2010scale synthesis. In the current study, three peptides were designed: a negatively charged 21\u2010residue peptide (21n), a negatively charged 28\u2010residue peptide (28n), and a positively charged 35\u2010residue peptide (35p). Peptides of opposite charges that were exposed to each other co\u2010assembled into \u03b1\u2010helical coiled\u2010coils. Peptides of different lengths allow for the formation of sticky ends, encouraging linear growth. The peptides include cysteine residues to stabilize fiber growth. Circular dichroism confirmed stable alpha\u2010helical secondary structure, and aggregation assays were conducted to track the assembly of higher\u2010order structures. Transmission electron microscopy was used to visually examine the aggregates that formed. When mixed, the designed peptides co\u2010assembled into large, fibrous aggregates. These fibers were resistant to heat and salt, but they disassembled when exposed to a reducing agent such as dithiothreitol (DTT). Fibers made by pairing 21n or 28n to 35p resulted in different morphologies upon co\u2010assembly under oxidizing conditions. Peptides that are soluble independently but co\u2010assemble into large, disulfide\u2010reinforced fibers present a new platform for tunable, biologically inspired fibers.<\/jats:p>","DOI":"10.1002\/cbic.70536","type":"journal-article","created":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T13:19:12Z","timestamp":1790169552000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Tunable Design for Co\u2010Assembly of Coiled\u2010Coil Fibers Using Oppositely Charged Peptides"],"prefix":"10.1002","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0009-0003-9334-053X","authenticated-orcid":false,"given":"Austin B.","family":"Rue","sequence":"first","affiliation":[{"name":"Department of Chemistry Austin College  Sherman Texas 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