Biological membranes play pivotal roles in the cellular activities. Transmembrane proteins are the central molecules that conduct membrane-mediated biochemical functions such as signal transduction and substance transportation. Not only the molecular functions but also the supramolecular properties of the transmembrane proteins such as self-assembly, delocalization, orientation and signal response are essential for controlling cellular activities. Here we report anisotropic ligand responses of a synthetic multipass transmembrane ion channel. An unsymmetrical molecular structure allows for oriented insertion of the synthetic amphiphile to a bilayer by addition to a pre-formed membrane. Complexation with a ligand prompts ion transportation by forming a supramolecular channel, and removal of the ligand deactivates the transportation function. Biomimetic regulation of the synthetic channel by agonistic and antagonistic ligands is also demonstrated not only in an artificial membrane but also in a biological membrane of a living cell.

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A survey of five newly developed microsatellite DNA markers in skipjack tuna Katsuwonus pelamis revealed high levels of polymorphism in two samples off the west coast of India (Minicoy Island and Kochi coast) and one sample off the Japan coast. Although significant differentiation (P < 0Á01) in the number of specific alleles was observed between Minicoy and Kochi samples, the F-statistics values among the samples were very low (average ¼ 0Á0014) and not significant (P ¼ 0Á284).

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