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Volumn 2, Issue 17, 2000, Pages 2721-2723

Structure of (-)-neodysidenin from Dysidea herbacea. Implications for biosynthesis of 5,5,5-trichloroleucine peptides

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; COTRANSPORTER; DIPEPTIDE; MEMBRANE PROTEIN; NEODYSIDENIN; SODIUM IODIDE SYMPORTER; THIAZOLE DERIVATIVE;

EID: 0034710498     PISSN: 15237060     EISSN: None     Source Type: Journal    
DOI: 10.1021/ol006326u     Document Type: Article
Times cited : (39)

References (26)
  • 5
    • 0039639488 scopus 로고
    • (a) Charles, C.; Braekman, J. C.; Daloze, D.; Tursch, B. Tetrahedron Lett. 1978, 1516-1520. Note the configuration of 2 reported in this paper is incorrect. For the correction of configuration (2S,5R,7S,13S), see:
    • (1978) Tetrahedron Lett. , pp. 1516-1520
    • Charles, C.1    Braekman, J.C.2    Daloze, D.3    Tursch, B.4
  • 6
    • 0006086777 scopus 로고
    • (b) Biskupiak, J. E.; Ireland, C. M. Tetrahedron Lett. 1984, 25, 2935-2936 and ref 12b for a comprehensive review of configurational assignments in this family of peptides.
    • (1984) Tetrahedron Lett. , vol.25 , pp. 2935-2936
    • Biskupiak, J.E.1    Ireland, C.M.2
  • 16
    • 85088714939 scopus 로고    scopus 로고
    • note
    • 3.
  • 21
    • 0040231307 scopus 로고    scopus 로고
    • unpublished and dysideathiazole (see ref 12b)
    • It is interesting to note that, under the same hydrolysis conditions, herbacic acid (7, see ref 7a) returned starting material, essentially unchanged, as did other N-methyl trichloroleucine derivatives 1 (Molinski, T. F.; Taylor, S. W., unpublished) and dysideathiazole (see ref 12b).
    • Molinski, T.F.1    Taylor, S.W.2
  • 22
    • 51849181148 scopus 로고
    • Marfey, P. Carlsberg. Res. Commun. 1984, 49, 591-596. L-leucine derivative, rt 18.9 min: D-leucine, 23.1 min. See Supporting Information for HPLC experimental conditions.
    • (1984) Carlsberg. Res. Commun. , vol.49 , pp. 591-596
    • Marfey, P.1
  • 23
    • 0039047453 scopus 로고    scopus 로고
    • note
    • Acid hydrolysis of N-thiazole-modified peptides, without prior oxidative degradation of the heterocyclic ring, results in racemization at the α-carbon (ref 4b).
  • 24
    • 0025045219 scopus 로고
    • 2S aq) were unsuccessful. MECC, a variant of capillary electrophoresis, gave excellent separation, removal of neutral artifacts, and short retention times.
    • (1990) J. Chromatogr. , vol.516 , pp. 241-249
    • Tran, A.D.1    Blanc, T.2    Leopold, E.J.3
  • 25
    • 0039047451 scopus 로고    scopus 로고
    • note
    • GCMS of the sample revealed partial racemization of 6 under hydrolysis conditions (6 M HCl, 100 °C, 10 h, ∼12:1 ratio of S:R). We surmise that the mechanism of epimerization at C-3 of 6 is reversible thermal elimination of HCl from the trichloroisopropyl group. During a second hydrolysis of 4, under more harsh conditions (12 h, 110 °C), the racemization of 6 appeared to be complete.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.