{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,14]],"date-time":"2025-11-14T07:37:53Z","timestamp":1763105873096,"version":"build-2065373602"},"reference-count":59,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2022,5,22]],"date-time":"2022-05-22T00:00:00Z","timestamp":1653177600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Science Centre","award":["UMO 2012\/07\/N\/ST5\/00249"],"award-info":[{"award-number":["UMO 2012\/07\/N\/ST5\/00249"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Amyloid fibrils have been known for many years. Unfortunately, their fame stems from negative aspects related to amyloid diseases. Nevertheless, due to their properties, they can be used as interesting nanomaterials. Apart from their remarkable stability, amyloid fibrils may be regarded as a kind of a storage medium and as a source of active peptides. In many cases, their structure may guarantee a controlled and slow release of peptides in their active form; therefore, they can be used as a potential nanomaterial in drug delivery systems. In addition, amyloid fibrils display controllable stiffness, flexibility, and satisfactory mechanical strength. In addition, they can be modified and functionalized very easily. Understanding the structure and genesis of amyloid assemblies derived from a broad range of amyloidogenic proteins could help to better understand and use this unique material. One of the factors responsible for amyloid aggregation is the steric zipper. Here, we report the discovery of steric zipper-forming peptides in the sequence of the amyloidogenic protein, human cystatin C (HCC). The ability of short peptides derived from this fragment of HCC to form fibrillar structures with defined self-association characteristics and the factors influencing this aggregation are also presented in this paper.<\/jats:p>","DOI":"10.3390\/ijms23105800","type":"journal-article","created":{"date-parts":[[2022,5,22]],"date-time":"2022-05-22T07:13:57Z","timestamp":1653203637000},"page":"5800","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Identification of a Steric Zipper Motif in the Amyloidogenic Core of Human Cystatin C and Its Use for the Design of Self-Assembling Peptides"],"prefix":"10.3390","volume":"23","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5774-3644","authenticated-orcid":false,"given":"Emilia","family":"I\u0142owska","sequence":"first","affiliation":[{"name":"Department of Organic Chemistry, Faculty of Chemistry, University of Gdansk, 80-308 Gdansk, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jakub","family":"Barciszewski","sequence":"additional","affiliation":[{"name":"Institute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1587-6489","authenticated-orcid":false,"given":"Mariusz","family":"Jask\u00f3lski","sequence":"additional","affiliation":[{"name":"Institute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, Poland"},{"name":"Department of Crystallography, Faculty of Chemistry, Adam Mickiewicz University in Poznan, 61-614 Poznan, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Augustyn","family":"Moli\u0144ski","sequence":"additional","affiliation":[{"name":"Department of Biomedical Physics, Faculty of Physics, Adam Mickiewicz University in Poznan, 61-614 Poznan, Poland"},{"name":"NanoBioMedical Centre, Adam Mickiewicz University in Poznan, 61-614 Poznan, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3312-6518","authenticated-orcid":false,"given":"Maciej","family":"Kozak","sequence":"additional","affiliation":[{"name":"Department of Biomedical Physics, Faculty of Physics, Adam Mickiewicz University in Poznan, 61-614 Poznan, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8664-2041","authenticated-orcid":false,"given":"Aneta","family":"Szyma\u0144ska","sequence":"additional","affiliation":[{"name":"Department of Biomedical Chemistry, Faculty of Chemistry, University of Gdansk, 80-308 Gdansk, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2022,5,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"6200","DOI":"10.1073\/pnas.1522282113","article-title":"Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril","volume":"113","author":"Schmidt","year":"2016","journal-title":"Proc. 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