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As an adaptive glassy material, the lens is constituted primarily by densely\u2010packed, polydisperse crystallin proteins that organize to resist aggregation and crystallization at high volume fractions, yet the details of how crystallins coordinate with one another to template and maintain this transparent microstructure remain unclear. The role of individual crystallin subtypes (\u03b1, \u03b2, and \u03b3) and paired subtype compositions, including how they experience and resist crowding\u2010induced turbidity in solution, is explored using combinations of spectrophotometry, hard\u2010sphere simulations, and surface pressure measurements. After assaying crystallin combinations, \u03b2\u2010crystallins emerged as a principal component in all mixtures that enabled dense fluid\u2010like packing and short\u2010range order necessary for transparency. These findings helped inform the design of lens\u2010like hydrogel systems, which are used to monitor and manipulate the loss of transparency under different crowding conditions. When taken together, the findings illustrate the design and characterization of adaptive materials made from lens proteins that can be used to better understand mechanisms regulating transparency.<\/jats:p>","DOI":"10.1002\/advs.202303279","type":"journal-article","created":{"date-parts":[[2023,10,28]],"date-time":"2023-10-28T07:59:10Z","timestamp":1698479950000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Design and Characterization of Model Systems that Promote and Disrupt Transparency of Vertebrate Crystallins In Vitro"],"prefix":"10.1002","volume":"10","author":[{"given":"Michael R.","family":"Bergman","sequence":"first","affiliation":[{"name":"Department of Chemistry and Chemical Biology Northeastern University  360 Huntington Ave Boston MA 02115 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sophia A.","family":"Hernandez","sequence":"additional","affiliation":[{"name":"Department of 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