Sequence-Selective Recognition of Peptides within the Single Binding Pocket of a Self-Assembled Coordination Cage
Author(s)
Tashiro, Shohei
Tominaga, Masahide
Kawano, Masaki
Ozeki, Tomoji
Fujita, Makoto
Date issued
2005
In
J. Am. Chem. Soc.
Vol
13
No
127
From page
4546
To page
4547
Subjects
peptide sequence selective binding palladium coordination cage crystal structure
Abstract
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 arom.-arom.-aliph. sequences of the residues (e.g., Trp-Trp-Gly and Trp-Tyr-Ala) are not recognized efficiently. X-ray anal. and NMR reveal that all residues of the Trp-Trp-Ala sequence cooperatively interact with the cage via CH-? and ?-? interactions. [on SciFinder(R)]
Publication type
journal article