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We have designed a self\u2010assembling amphiphilic peptide that folds into a hairpin\u2010like helix\u2010loop\u2010helix (HLH) motif. The \u03b1\u2010helical segments are rich in hydrophobic leucine residues, while the loop segment is positively charged. The morphology of the peptide self\u2010assemblies can be controlled by the preparation method. When prepared from an ethanolic solution at room temperature, these amphiphilic HLHPs self\u2010assemble into spherical particles with a diameter in the sub\u2010100\u00a0nm range, with \u03b1\u2010helical secondary structure and good long\u2010term stability at 4\u00b0C and pH\u00a03. When produced from an aqueous buffer using ultrasonication at elevated temperatures, peptides with a \u03b2\u2010sheet secondary structure are obtained, forming disc\u2010shaped particles which have a high tendency to fuse. The \u03b1\u2010helical nanospheres have been shown to interact with hydrophobic molecules such as 1,6\u2010diphenylhexatriene or Amplex Red. The structural stability of the self\u2010assembling nanospheres is largely dependent on the loop sequence composition: higher charge density and lysine residues instead of arginine residues lead to markedly reduced stability of the spherical particles.<\/jats:p>","DOI":"10.1002\/smll.76207","type":"journal-article","created":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T09:06:02Z","timestamp":1791882362000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Self\u2010Assembling Gemini\u2010Type Amphiphiles From Helix\u2010Loop\u2010Helix Peptides"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-9541-892X","authenticated-orcid":false,"given":"Thomas","family":"Heim","sequence":"first","affiliation":[{"name":"Institute of Organic Chemistry Heidelberg University  Heidelberg 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