Please use this identifier to cite or link to this item: https://dspace.iiti.ac.in/handle/123456789/9293
Full metadata record
DC FieldValueLanguage
dc.contributor.authorDas, Apurba Kumaren_US
dc.date.accessioned2022-03-17T01:00:00Z-
dc.date.accessioned2022-03-21T11:32:07Z-
dc.date.available2022-03-17T01:00:00Z-
dc.date.available2022-03-21T11:32:07Z-
dc.date.issued2015-
dc.identifier.citationRasale, D. B., & Das, A. K. (2015). Chemical reactions directed peptide self-assembly. International Journal of Molecular Sciences, 16(5), 10797-10820. doi:10.3390/ijms160510797en_US
dc.identifier.issn1661-6596-
dc.identifier.otherEID(2-s2.0-84929359023)-
dc.identifier.urihttps://doi.org/10.3390/ijms160510797-
dc.identifier.urihttps://dspace.iiti.ac.in/handle/123456789/9293-
dc.description.abstractFabrication of self-assembled nanostructures is one of the important aspects in nanoscience and nanotechnology. The study of self-assembled soft materials remains an area of interest due to their potential applications in biomedicine. The versatile properties of soft materials can be tuned using a bottom up approach of small molecules. Peptide based self-assembly has significant impact in biology because of its unique features such as biocompatibility, straight peptide chain and the presence of different side chain functionality. These unique features explore peptides in various self-assembly process. In this review, we briefly introduce chemical reaction-mediated peptide self-assembly. Herein, we have emphasised enzymes, native chemical ligation and photochemical reactions in the exploration of peptide self-assembly. © 2015 by the authors; licensee MDPI, Basel, Switzerland.en_US
dc.language.isoenen_US
dc.publisherMDPI AGen_US
dc.sourceInternational Journal of Molecular Sciencesen_US
dc.subjectacetyl coenzyme Aen_US
dc.subjectamideen_US
dc.subjectascorbic aciden_US
dc.subjectchymotrypsinen_US
dc.subjectcysteineen_US
dc.subjectenzymeen_US
dc.subjectnanomaterialen_US
dc.subjectpeptideen_US
dc.subjectproteinaseen_US
dc.subjectseleniumen_US
dc.subjectthermolysinen_US
dc.subjectthioesteren_US
dc.subjecttriacylglycerol lipaseen_US
dc.subjecttryptophanen_US
dc.subjectactin polymerizationen_US
dc.subjectbiocompatibilityen_US
dc.subjectbiological activityen_US
dc.subjectbiomineralizationen_US
dc.subjectbiotransformationen_US
dc.subjectchemical reactionen_US
dc.subjectcyclizationen_US
dc.subjectenzyme activityen_US
dc.subjectenzyme mechanismen_US
dc.subjectgenetic proceduresen_US
dc.subjecthigh performance liquid chromatographyen_US
dc.subjectligationen_US
dc.subjectmacrocyclizationen_US
dc.subjectmolecular interactionen_US
dc.subjectnanofabricationen_US
dc.subjectnonhumanen_US
dc.subjectpeptide synthesisen_US
dc.subjectphotochemistryen_US
dc.subjectprotein assemblyen_US
dc.subjectprotein hydrolysisen_US
dc.subjectReviewen_US
dc.subjecttissue engineeringen_US
dc.subjecttransesterificationen_US
dc.subjectultrasounden_US
dc.subjectwound healingen_US
dc.subjectbiocatalysisen_US
dc.subjectchemical phenomenaen_US
dc.subjectchemistryen_US
dc.subjecthydrolysisen_US
dc.subjectlighten_US
dc.subjectmolecular modelen_US
dc.subjectsynthesisen_US
dc.subjectBiocatalysisen_US
dc.subjectChemical Phenomenaen_US
dc.subjectHydrolysisen_US
dc.subjectLighten_US
dc.subjectModels, Molecularen_US
dc.subjectPeptidesen_US
dc.titleChemical reactions directed peptide self-assemblyen_US
dc.typeReviewen_US
dc.rights.licenseAll Open Access, Gold, Green-
Appears in Collections:Department of Chemistry

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Altmetric Badge: