Show simple item record

Files in this item

Thumbnail

Item metadata

dc.contributor.authorBajpayee, Nikhil
dc.contributor.authorVijayakanth, Thangavel
dc.contributor.authorRencus-Lazar, Sigal
dc.contributor.authorDasgupta, Sneha
dc.contributor.authorV. Desai, Aamod
dc.contributor.authorJain, Rahul
dc.contributor.authorGazit, Ehud
dc.contributor.authorMisra, Rajkumar
dc.date.accessioned2023-12-15T00:36:04Z
dc.date.available2023-12-15T00:36:04Z
dc.date.issued2023-02-01
dc.identifier282335338
dc.identifierfb13ca0e-c7d4-47ee-8355-ec14b7e928f2
dc.identifier85143885373
dc.identifier000923147100001
dc.identifier.citationBajpayee , N , Vijayakanth , T , Rencus-Lazar , S , Dasgupta , S , V. Desai , A , Jain , R , Gazit , E & Misra , R 2023 , ' Exploring helical peptides and foldamers for the design of metal helix frameworks : current trends and future perspectives ' , Angewandte Chemie International Edition , vol. 62 , no. 6 , e202214583 . https://doi.org/10.1002/anie.202214583en
dc.identifier.issn1433-7851
dc.identifier.otherRIS: urn:07B6B5FC61C1BF68CDE7A033197441B3
dc.identifier.urihttps://hdl.handle.net/10023/28876
dc.descriptionFunding: T.V. thanks Tel Aviv University for the postdoctoral fellowship. E.G. thanks European Research Council PoC project Piezogel (966813) and Ministry of Science and Technology (MOST) Israel-China Program (3-19130). This research was supported by the DST Inspire Faculty Fellowship (No. DST/INSPIRE/04/2020/002499) from the Department of Science and Technology, New Delhi. R. M is also thankful to the National Institute of Pharmaceutical Education and Research, S. A. S. Nagar for providing the research facilities.en
dc.description.abstractFlexible and biocompatible metal peptide frameworks (MPFs) derived from short and ultra-short peptides have been explored for the storage of greenhouse gases, molecular recognition, and chiral transformations. In addition to short flexible peptides, peptides with specifically folded conformations have recently been utilized to fabricate a variety of metal helix frameworks (MHFs). The secondary structures of the peptides govern the structure-assembly relationship and thereby control the formation of three-dimensional (3D)-MHFs. Particularly, the hierarchical structural organization of peptide-based MHFs has not yet been discussed in detail. Here, we describe the recent progress of metal-driven folded peptide assembly to construct 3D porous structures for use in future energy storage, chiral recognition, and biomedical applications, which could be envisioned as an alternative to the conventional metal-organic frameworks (MOFs).
dc.format.extent12
dc.format.extent1922878
dc.language.isoeng
dc.relation.ispartofAngewandte Chemie International Editionen
dc.subjectHelical peptidesen
dc.subjectFoldamersen
dc.subjectMetal-helix frameworksen
dc.subjectPorous structuresen
dc.subjectBio-compatibilityen
dc.subjectQD Chemistryen
dc.subject3rd-NDASen
dc.subjectMCCen
dc.subject.lccQDen
dc.titleExploring helical peptides and foldamers for the design of metal helix frameworks : current trends and future perspectivesen
dc.typeJournal itemen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.identifier.doi10.1002/anie.202214583
dc.description.statusPeer revieweden
dc.date.embargoedUntil2023-12-15


This item appears in the following Collection(s)

Show simple item record