Pien, Nele published the artcileProteomics as a tool to gain next level insights into photo-crosslinkable biopolymer modifications, Product Details of C5H11NO2S, the publication is Bioactive Materials (2022), 204-220, database is CAplus and MEDLINE.
The distribution of photo-crosslinkable moieties onto a protein backbone can affect a biomaterials crosslinking behavior, and therefore also its mech. and biol. properties. A profound insight in this respect is essential for biomaterials exploited in tissue engineering and regenerative medicine. In the present work, photo-crosslinkable moieties have been introduced on the primary amine groups of: (i) a recombinant collagen peptide (RCPhC1) with a known amino acid (AA) sequence, and (ii) bovine skin collagen (COL BS) with an unknown AA sequence. The degree of substitution (DS) was quantified with two conventional techniques: an ortho-phthalic dialdehyde (OPA) assay and 1H NMR spectroscopy. However, neither of both provides information on the exact type and location of the modified AAs. Therefore, for the first time, proteomic anal. was evaluated herein as a tool to identify functionalized AAs as well as the exact position of photo-crosslinkable moieties along the AA sequence, thereby enabling an in-depth, unprecedented characterization of functionalized photo-crosslinkable biopolymers. Moreover, our strategy enabled to visualize the spatial distribution of the modifications within the overall structure of the protein. Proteomics has proven to provide unprecedented insight in the distribution of photo-crosslinkable moieties along the protein backbone, undoubtedly contributing to superior functional biomaterial design to serve regenerative medicine.
Bioactive Materials published new progress about 63-68-3. 63-68-3 belongs to catalysis-chemistry, auxiliary class Natural product, name is (S)-2-Amino-4-(methylthio)butanoic acid, and the molecular formula is C5H11NO2S, Product Details of C5H11NO2S.
Referemce:
https://courses.lumenlearning.com/boundless-chemistry/chapter/catalysis/,
Catalysis – Wikipedia