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characterized by a broad phenotypic outcome. A plausible explanation for this outcome is that FKBP22 participates in the biosynthesis of subsets of collagen types: FKBP22 selectively binds to collagens III, IV, VI, and X, but not to collagens I, II, V, and XI. However, these binding mechanisms have never been explored, and they may underpin EDS subtype heterogeneity. Here, we used collagen Toolkit peptide libraries to investigate binding specificity. We observed that FKBP22 binding was distributed along the collagen helix. Further, it (1) was higher on collagen III than collagen II peptides and it (2) was correlated with a positive peptide charge. These findings begin to elucidate the mechanism by which FKBP22 interacts with collagen.<\/jats:p>","DOI":"10.3390\/ijms242015156","type":"journal-article","created":{"date-parts":[[2023,10,13]],"date-time":"2023-10-13T10:04:39Z","timestamp":1697191479000},"page":"15156","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Local Net Charge State of Collagen Triple Helix Is a Determinant of FKBP22 Binding to Collagen III"],"prefix":"10.3390","volume":"24","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2013-0518","authenticated-orcid":false,"given":"Yoshihiro","family":"Ishikawa","sequence":"first","affiliation":[{"name":"Department of Ophthalmology, University of California San Francisco, School of Medicine, San Francisco, CA 941583, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3957-7849","authenticated-orcid":false,"given":"Arkadiusz","family":"Bonna","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Downing Site, Cambridge CB2 1QW, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5127-5328","authenticated-orcid":false,"given":"Douglas B.","family":"Gould","sequence":"additional","affiliation":[{"name":"Department of Ophthalmology, University of California San Francisco, School of Medicine, San Francisco, CA 941583, USA"},{"name":"Department of Anatomy, University of California, San Francisco, CA 94143, USA"},{"name":"Cardiovascular Research Institute, University of California, San Francisco, CA 94158, USA"},{"name":"Bakar Aging Research Institute, University of California, San Francisco, CA 94143, USA"},{"name":"Institute for Human Genetics, University of California, San Francisco, CA 94143, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6130-8808","authenticated-orcid":false,"given":"Richard W.","family":"Farndale","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Downing Site, Cambridge CB2 1QW, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2023,10,13]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"4490","DOI":"10.1038\/s41598-023-31566-z","article-title":"Collagen constitutes about 12% in females and 17% in males of the total protein in mice","volume":"13","author":"Tarnutzer","year":"2023","journal-title":"Sci. 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Cell Sci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"593874","DOI":"10.3389\/fmed.2021.593874","article-title":"Collagen Biosynthesis, Processing, and Maturation in Lung Ageing","volume":"8","author":"Onursal","year":"2021","journal-title":"Front. Med."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1146\/annurev-biochem-013118-111603","article-title":"Quality Control of Procollagen in Cells","volume":"90","author":"Ito","year":"2021","journal-title":"Annu. Rev. Biochem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2479","DOI":"10.1016\/j.bbamcr.2013.04.008","article-title":"A molecular ensemble in the rER for procollagen maturation","volume":"1833","author":"Ishikawa","year":"2013","journal-title":"Biochim. Biophys. Acta."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Ruggiero, F. (2021). The Collagen Superfamily and Collagenopathies, Springer International Publishing.","DOI":"10.1007\/978-3-030-67592-9"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1527","DOI":"10.1002\/ar.24086","article-title":"Genetic Disorders of the Extracellular Matrix","volume":"303","author":"Lamande","year":"2020","journal-title":"Anat. Rec."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1038\/s41572-020-0194-9","article-title":"The Ehlers-Danlos syndromes","volume":"6","author":"Malfait","year":"2020","journal-title":"Nat. Rev. Dis. Primers"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"17052","DOI":"10.1038\/nrdp.2017.52","article-title":"Osteogenesis imperfecta","volume":"3","author":"Marini","year":"2017","journal-title":"Nat. Rev. Dis. 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