Search results

Search for "branched peptides" in Full Text gives 1 result(s) in Beilstein Journal of Organic Chemistry.

Enzyme-instructed morphological transition of the supramolecular assemblies of branched peptides

  • Dongsik Yang,
  • Hongjian He and
  • Bing Xu

Beilstein J. Org. Chem. 2020, 16, 2709–2718, doi:10.3762/bjoc.16.221

Graphical Abstract
  • Dongsik Yang Hongjian He Bing Xu Department of Chemistry, Brandeis University, 415 South Street, Waltham, MA 02454, USA 10.3762/bjoc.16.221 Abstract Here, we report the use of an enzymatic reaction to cleave the branch off branched peptides for inducing the morphological transition of the
  • assemblies of the peptides. The attachment of DEDDDLLI sequences to the ε-amine of the lysine residue of a tetrapeptide produces branched peptides that form micelles. Upon the proteolytic cleavage of the branch, catalyzed by proteinase K, the micelles turn into nanofibers. We also found that the acetylation
  • of the N-terminal of the branch increased the stability of the branched peptides. Moreover, these branched peptides facilitate the delivery of the proteins into cells. This work contributes insights for the development of peptide supramolecular assemblies via enzymatic noncovalent synthesis in
PDF
Album
Supp Info
Full Research Paper
Published 04 Nov 2020
Other Beilstein-Institut Open Science Activities