File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Genetically Programming Stress-Relaxation Behavior in Entirely Protein-Based Molecular Networks

TitleGenetically Programming Stress-Relaxation Behavior in Entirely Protein-Based Molecular Networks
Authors
Issue Date2018
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/toc/amlccd/current
Citation
ACS Macro Letters, 2018, v. 7 n. 12, p. 1468-1474 How to Cite?
AbstractWe report the synthesis of a series of elastin-like polypeptide (ELP)-based molecular networks through the combined use of the covalent bond-forming SpyTag/SpyCatcher chemistry, physically entangled p53dim domains (Xs), and site-directed mutagenesis. The resulting networks shared similar chemical composition but differed significantly in their viscoelasticity. These materials exhibited excellent compatibility toward encapsulated fibroblasts and stem cells. These results point to a versatile strategy for designing viscoelastic materials by tapping into diverse protein-protein interactions. Copyright © 2018 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/275060
ISSN
2017 Impact Factor: 6.131
2015 SCImago Journal Rankings: 2.497
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYang, Z-
dc.contributor.authorKou, S-
dc.contributor.authorWei, X-
dc.contributor.authorZhang, F-
dc.contributor.authorLi, F-
dc.contributor.authorWang, X-
dc.contributor.authorLin, Y-
dc.contributor.authorWan, C-
dc.contributor.authorZhang, W-
dc.contributor.authorSun, F-
dc.date.accessioned2019-09-10T02:34:37Z-
dc.date.available2019-09-10T02:34:37Z-
dc.date.issued2018-
dc.identifier.citationACS Macro Letters, 2018, v. 7 n. 12, p. 1468-1474-
dc.identifier.issn2161-1653-
dc.identifier.urihttp://hdl.handle.net/10722/275060-
dc.description.abstractWe report the synthesis of a series of elastin-like polypeptide (ELP)-based molecular networks through the combined use of the covalent bond-forming SpyTag/SpyCatcher chemistry, physically entangled p53dim domains (Xs), and site-directed mutagenesis. The resulting networks shared similar chemical composition but differed significantly in their viscoelasticity. These materials exhibited excellent compatibility toward encapsulated fibroblasts and stem cells. These results point to a versatile strategy for designing viscoelastic materials by tapping into diverse protein-protein interactions. Copyright © 2018 American Chemical Society.-
dc.languageeng-
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/toc/amlccd/current-
dc.relation.ispartofACS Macro Letters-
dc.rightsThis document is the Accepted Manuscript version of a Published Work that appeared in final form in [JournalTitle], copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see [insert ACS Articles on Request author-directed link to Published Work, see http://pubs.acs.org/page/policy/articlesonrequest/index.html].-
dc.titleGenetically Programming Stress-Relaxation Behavior in Entirely Protein-Based Molecular Networks-
dc.typeArticle-
dc.identifier.emailLin, Y: ylin@hku.hk-
dc.identifier.authorityLin, Y=rp00080-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/acsmacrolett.8b00845-
dc.identifier.scopuseid_2-s2.0-85058122627-
dc.identifier.hkuros304183-
dc.identifier.volume7-
dc.identifier.issue12-
dc.identifier.spage1468-
dc.identifier.epage1474-
dc.identifier.isiWOS:000454183100012-
dc.publisher.placeUnited States-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats