Assembling of the four individual helices corresponding to the transmembrane segments (S4 in repeat I-IV) ofthe sodium channel

Tetrahedron Letters

Volumn 38, Issue 40, 1997, Pages 7071-7074

  Futaki, Shiroh ^a   Aoki, Mika ^a   Fukuda, Masayuki ^a   Kondo, Fusayo ^a   Niwa, Mineo ^a   Kitagawa, Kouki ^b   Nakaya, Yutaka ^c  

^a UNIVERSITY OF TOKUSHIMA   (Japan)

^b NIIGATA UNIVERSITY OF PHARMACY AND APPLIED LIFE SCIENCES   (Japan)

^c UNIVERSITY OF TOKUSHIMA   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL;

ARTICLE; CIRCULAR DICHROISM; DRUG STRUCTURE; DRUG SYNTHESIS; IN VITRO STUDY; MOLECULAR DYNAMICS; PEPTIDE SYNTHESIS; PROTEIN STRUCTURE;

EID: 0030867021     PISSN: 00404039     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0040-4039(97)01651-1     Document Type: Article

References (22)

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3. c) Tuchscherer, G.; Mutter, M. J. Peptide Sci. 1995, 1, 3-10.
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10. b) Futaki, S.; Ishikawa, T.; Niwa, M.; Kitagawa, K.; Yagami, T. Bioorg. Med. Chem. in press.
11. tBu), respectively.
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19. One possible explanation for the presence of two different channel states is the aggregation of the proteins. A similar observation was reported when TASP molecules formed an ion channel (For example: Oblatt-Montal, M. et al. J. Biol. Chem., 1993, 268, 14601-14607; Pawlak, M. et al. Protein Sci., 1994, 3, 1788-1805). However, these two states were rarely observed successively or simultaneously in our case. This fact would suggest the presence of different conformational states within one protein molecule.
20. One possible explanation for the presence of two different channel states is the aggregation of the proteins. A similar observation was reported when TASP molecules formed an ion channel (For example: Oblatt-Montal, M. et al. J. Biol. Chem., 1993, 268, 14601-14607; Pawlak, M. et al. Protein Sci., 1994, 3, 1788-1805). However, these two states were rarely observed successively or simultaneously in our case. This fact would suggest the presence of different conformational states within one protein molecule.
21. The channel activity of a 22-amino acid residue peptide corresponding to the S4 segment of the repeat IV has been reported by Tosteson (Tosteson, M. et al. Proc. Natl. Acad. Sci., USA 1989, 86, 707-710).
22. Recently, Mutter and his coworkers also demonstrated that a mimic of the complimentarity-determining region of a monoclonal antibody was constructed on a multi-loop introducible template (Mutter, M. et al. Angew. Chem. Int. Ed. Engl. 1996, 35, 1482-1485).