Sequence-selective recognition of peptides within the single binding pocket of a self-assembled coordination cage.
نویسندگان
چکیده
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.
منابع مشابه
Molecular Identification of Pre-Existing Immunityin Human against H9N2 Influenza Viruses Using HLA-A*0201 Binding Peptides
Background and Aims: The contribution genetic and antigenic diversity of H9N2 influenza viruses in evading from immune responses, cytotoxic T lymphocytes (CTL) epitopes in hemagglutinin (HA) protein restricted by HLA binding peptides was identified. Materials and Methods: Phylogenetic analyses were carried out for all of full length HA and deduced amino acid sequences of H9N2 viruses available ...
متن کاملSequence-selective encapsulation and protection of long peptides by a self-assembled FeII8L6 cubic cage
Self-assembly offers a general strategy for the preparation of large, hollow high-symmetry structures. Although biological capsules, such as virus capsids, are capable of selectively recognizing complex cargoes, synthetic encapsulants have lacked the capability to specifically bind large and complex biomolecules. Here we describe a cubic host obtained from the self-assembly of FeII and a zinc-p...
متن کاملA self-assembled Pd2L4 cage that selectively encapsulates nitrate.
A M2L4 cage with D4 symmetry was self-assembled from four anthracene-bridged benzimidazole ligands and two Pd(II) ions. The cage features a concise hydrophobic pocket wrapped up by the anthracene walls with eight hydrogen-bond donors pointing inward, which provide a specific binding site for nitrate, with a binding affinity at least two orders of magnitude higher than all the other anions scree...
متن کاملSelective guest recognition by a self-assembled paramagnetic cage complex.
A cubic cage complex assembled from twelve bis-bidentate ligands and eight Co(II) ions provides a cavity that selectively recognises and binds coumarin in MeCN solution. The cage portals are large enough to allow guest exchange, but small enough to provide a kinetic trap; the cage paramagnetism facilitates detailed NMR analysis.
متن کاملDesigning a new tetrapeptide to inhibit the BIR3 domain of the XIAP protein via molecular dynamics simulations
The XIAP protein is a member of apoptosis proteins family. The XIAP protein plays a central role in the inhibition of apoptosis and consists of three Baculoviral IAP Repeat domains. The BIR3 domain binds directly to the N-terminal of caspase-9 and therefore it inhibits apoptosis. N-terminal tetrapeptide region of SMAC protein can bind to BIR3, inhibit it and subsequently induce apoptosis. In th...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Journal of the American Chemical Society
دوره 127 13 شماره
صفحات -
تاریخ انتشار 2005