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Porous Peptide Complexes by a Folding‐and‐Assembly Strategy
Author(s) -
Sawada Tomohisa,
Yamagami Motoya,
Akinaga Shuji,
Miyaji Tatsuki,
Fujita Makoto
Publication year - 2017
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201700458
Subject(s) - tripeptide , peptide , folding (dsp implementation) , protein folding , ligand (biochemistry) , self assembly , sequence (biology) , chemistry , biophysics , crystallography , nanotechnology , combinatorial chemistry , materials science , biochemistry , receptor , biology , engineering , electrical engineering
Concerted folding and assembly processes are necessary for protein self‐assembly, yet such a concerted strategy has rarely been attempted by synthetic chemists. In this work, we have created a new porous peptide structure through a coordination‐driven folding‐and‐assembly strategy. A porous framework with 1.5 nm‐sized pores and a P II helical peptide scaffold was successfully obtained by complexation of AgNTf 2 and tripeptide ligands containing the Gly‐Pro‐Pro sequence. The pores were modified in various ways with retention of the latent P II helical conformation of the peptide ligand.
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