Beilstein J. Org. Chem.2020,16, 2709–2718, doi:10.3762/bjoc.16.221
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 branchedpeptides 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 branchedpeptides 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 branchedpeptides. Moreover, these branchedpeptides 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
Graphical Abstract
Figure 1:
A) The molecular structures of the branched peptides Nap-ffk(NH2-DEDDDLLIG)y (1) and Nap-ffk(AcNH-D...