{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T14:07:36Z","timestamp":1790690856316,"version":"4.1.0"},"reference-count":72,"publisher":"American Chemical Society (ACS)","license":[{"start":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T00:00:00Z","timestamp":1790380800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100006770","name":"American Chemical Society Petroleum Research Fund","doi-asserted-by":"publisher","award":["69034-DNI3"],"award-info":[{"award-number":["69034-DNI3"]}],"id":[{"id":"10.13039\/100006770","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Tryptophan is a biologically important redox-active amino acid whose functions in proteins, including long-range electron transfer, protection against oxidative damage, and environmental sensing, are governed not only by its chemical identity but also by its precise structural organization. Inspired by this biological principle, we investigated whether controlling the organization of tryptophan within crystalline materials could provide a strategy for modulating its physicochemical properties and molecular accessibility. Using identical molecular components but distinct assembly pathways, tryptophan was organized either as a confined guest within a preformed Zn\u2013imidazolate framework, yielding a star-shaped crystalline architecture, or as an integral coordination component during framework growth, producing a distinct layered Zn\u2013tryptophan crystalline framework. Although assembled from the same building blocks, these two organization modes generated fundamentally different crystal structures, morphologies, and mechanisms of biomolecule incorporation. In both architectures, incorporation of tryptophan into the crystalline environment preserved its intrinsic fluorescence while producing robust fluorescence under multiple excitation wavelengths, highlighting the strong influence of molecular organization on its optical response. The structural modes also exhibited distinct encapsulation efficiencies and pH-dependent molecular accessibility, while secondary Ca2+-crosslinked alginate fixation provided an additional level of control over guest retention without disrupting the underlying crystalline architecture. These results demonstrate that engineering the structural organization of tryptophan provides a versatile strategy for tuning the optical behavior, molecular accessibility, and functional integration of a biologically important redox-active amino acid in crystalline materials, establishing a foundation for future biomimetic redox architectures, responsive sensing platforms, and controlled molecular delivery.<\/jats:p>","DOI":"10.1021\/acsabm.6c01612","type":"journal-article","created":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T20:01:23Z","timestamp":1790452883000},"source":"Crossref","is-referenced-by-count":0,"title":["Engineering the Structural Organization of Tryptophan in Crystalline Materials for Tunable Functionality"],"prefix":"10.1021","author":[{"given":"Oliver","family":"Ton","sequence":"first","affiliation":[{"name":"Texas Tech University , , , ,","place":["Lubbock, Texas, United States, 79409"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sidhanth","family":"Duvvuri","sequence":"additional","affiliation":[{"name":"Texas Tech University , , , ,","place":["Lubbock, Texas, United States, 79409"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3672-0731","authenticated-orcid":true,"given":"Carol","family":"Korzeniewski","sequence":"additional","affiliation":[{"name":"Texas Tech University , , , ,","place":["Lubbock, Texas, United States, 79409"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2992-0575","authenticated-orcid":true,"given":"Raheleh","family":"Ravanfar","sequence":"additional","affiliation":[{"name":"Texas Tech University , , , ,","place":["Lubbock, Texas, United States, 79409"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,26]]},"reference":[{"issue":"8","key":"2026092909131929500_cit1","doi-asserted-by":"publisher","first-page":"593","DOI":"10.1038\/nchembio.186","article-title":"Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli","volume":"5","author":"Bennett","year":"2009","journal-title":"Nat. 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