Sequence-selective recognition of peptides within the single binding pocket of a self-assembled coordination cage.
The single binding pocket of a self-assembled Pd6L4 coordination cage recognizes oligopeptides in a highly sequence-selective fashion. In particular, the Trp-Trp-Ala sequence is strongly bound by the cavity (Ka >/=106 M-1). Tripeptides possessing the same residues but in different sequences (i.e., Trp-Ala-Trp and Ala-Trp-Trp) show much poorer affinity. Even singly mutated tripeptides with aromatic-aromatic-aliphatic sequences of the residues (e.g., Trp-Trp-Gly and Trp-Tyr-Ala) are not recognized efficiently. X-ray analysis and NMR reveal that all residues of the Trp-Trp-Ala sequence cooperatively interact with the cage via CH-pi and pi-pi interactions.
Tashiro
Shohei
S
Department of Applied Chemistry, School of Engineering, The University of Tokyo, CREST, Japan Science and Technology Agency (JST), 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
Tominaga
Masahide
M
Kawano
Masaki
M
Therrien
Bruno
B
Ozeki
Tomoji
T
Fujita
Makoto
M
D000409:Alanine / Q000737:chemistry; D001665:Binding Sites; D005998:Glycine / Q000737:chemistry; D006639:Histidine / Q000737:chemistry; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D009842:Oligopeptides / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity; D014443:Tyrosine / Q000737:chemistry
D009842:Oligopeptides; D014443:Tyrosine; D006639:Histidine; D000409:Alanine; D005998:Glycine