<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kosuri S</submitter><funding>National Institutes of Health</funding><funding>NIGMS NIH HHS</funding><funding>New Jersey Commission on Spinal Cord Research</funding><funding>National Science Foundation</funding><pagination>e2102101</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9119153</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(10)</volume><pubmed_abstract>Among the many molecules that contribute to glial scarring, chondroitin sulfate proteoglycans (CSPGs) are known to be potent inhibitors of neuronal regeneration. Chondroitinase ABC (ChABC), a bacterial lyase, degrades the glycosaminoglycan (GAG) side chains of CSPGs and promotes tissue regeneration. However, ChABC is thermally unstable and loses all activity within a few hours at 37 °C under dilute conditions. To overcome this limitation, the discovery of a diverse set of tailor-made random copolymers that complex and stabilize ChABC at physiological temperature is reported. The copolymer designs, which are based on chain length and composition of the copolymers, are identified using an active machine learning paradigm, which involves iterative copolymer synthesis, testing for ChABC thermo</pubmed_abstract><journal>Advanced healthcare materials</journal><pubmed_title>Machine-Assisted Discovery of Chondroitinase ABC Complexes toward Sustained Neural Regeneration.</pubmed_title><pmcid>PMC9119153</pmcid><funding_grant_id>NIGMS R35GM138296</funding_grant_id><funding_grant_id>T32 GM135141</funding_grant_id><funding_grant_id>NSF‐DMR‐2118861</funding_grant_id><funding_grant_id>R35 GM138296</funding_grant_id><funding_grant_id>NSF‐DMR‐2118860</funding_grant_id><funding_grant_id>CSCR18IRG007</funding_grant_id><pubmed_authors>Mugnier H</pubmed_authors><pubmed_authors>Schloss R</pubmed_authors><pubmed_authors>Gormley AJ</pubmed_authors><pubmed_authors>Tamasi M</pubmed_authors><pubmed_authors>Patel RA</pubmed_authors><pubmed_authors>Finkel Z</pubmed_authors><pubmed_authors>Cai L</pubmed_authors><pubmed_authors>Borca CH</pubmed_authors><pubmed_authors>Kumar S</pubmed_authors><pubmed_authors>Webb MA</pubmed_authors><pubmed_authors>Yarmush ML</pubmed_authors><pubmed_authors>Perez I</pubmed_authors><pubmed_authors>Kosuri S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Machine-Assisted Discovery of Chondroitinase ABC Complexes toward Sustained Neural Regeneration.</name><description>Among the many molecules that contribute to glial scarring, chondroitin sulfate proteoglycans (CSPGs) are known to be potent inhibitors of neuronal regeneration. Chondroitinase ABC (ChABC), a bacterial lyase, degrades the glycosaminoglycan (GAG) side chains of CSPGs and promotes tissue regeneration. However, ChABC is thermally unstable and loses all activity within a few hours at 37 °C under dilute conditions. To overcome this limitation, the discovery of a diverse set of tailor-made random copolymers that complex and stabilize ChABC at physiological temperature is reported. The copolymer designs, which are based on chain length and composition of the copolymers, are identified using an active machine learning paradigm, which involves iterative copolymer synthesis, testing for ChABC thermo</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 May</publication><modification>2025-05-29T16:22:23.095Z</modification><creation>2025-05-29T16:22:23.095Z</creation></dates><accession>S-EPMC9119153</accession><cross_references><pubmed>35112508</pubmed><doi>10.1002/adhm.202102101</doi></cross_references></HashMap>