TY - JOUR
T1 - Simultaneous Stabilization and Multimerization of a Peptide α-Helix by Stapling Polymerization
AU - Lee, Young Joo
AU - Han, Sanghun
AU - Lim, Yong Beom
N1 - Publisher Copyright:
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2016/7/1
Y1 - 2016/7/1
N2 - Maintaining specific conformations of peptide ligands is crucial for improving the efficacy of biological interactions. Here, a one-pot polymerization strategy for stabilizing the α-helical conformation of peptides while simultaneously constructing multimeric ligands is presented. The new method, termed stapling polymerization, uses radical polymerization between acryloylated peptide side chains and vinylic monomers. Studies with model peptides indicate that i, i+7 crosslinking is effective for the helix stabilization, whereas i, i+4 crosslinking is not. The stapling polymerization results in the formation of peptide-polyacrylamide conjugates that include ≈3-16 peptides in a single conjugate. This stapling polymerization provides a simple but powerful methodology to fabricate multimeric α-helices that can further be developed to modulate multivalent biomacromolecular interactions.
AB - Maintaining specific conformations of peptide ligands is crucial for improving the efficacy of biological interactions. Here, a one-pot polymerization strategy for stabilizing the α-helical conformation of peptides while simultaneously constructing multimeric ligands is presented. The new method, termed stapling polymerization, uses radical polymerization between acryloylated peptide side chains and vinylic monomers. Studies with model peptides indicate that i, i+7 crosslinking is effective for the helix stabilization, whereas i, i+4 crosslinking is not. The stapling polymerization results in the formation of peptide-polyacrylamide conjugates that include ≈3-16 peptides in a single conjugate. This stapling polymerization provides a simple but powerful methodology to fabricate multimeric α-helices that can further be developed to modulate multivalent biomacromolecular interactions.
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U2 - 10.1002/marc.201600179
DO - 10.1002/marc.201600179
M3 - Article
C2 - 27162197
AN - SCOPUS:84977644727
VL - 37
SP - 1021
EP - 1026
JO - Macromolecular Rapid Communications
JF - Macromolecular Rapid Communications
SN - 1022-1336
IS - 13
ER -