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Volumn , Issue 25, 2009, Pages 4231-4241

Synthesis and biological evaluation of novel gramicidin s analogues

Author keywords

Antibiotics; Conformation analysis; Peptidomimetics; Sugar amino acid

Indexed keywords


EID: 68949105444     PISSN: 1434193X     EISSN: 10990690     Source Type: Journal    
DOI: 10.1002/ejoc.200900460     Document Type: Article
Times cited : (17)

References (35)
  • 1
    • 0032717048 scopus 로고    scopus 로고
    • A number of reviews have been published in relation to CAPs: a R. M. Epand, H. J. Vogel, Biochim. Biophys. Acta 1999, 1462, 11-28;
    • A number of reviews have been published in relation to CAPs: a) R. M. Epand, H. J. Vogel, Biochim. Biophys. Acta 1999, 1462, 11-28;
  • 24
    • 0036462603 scopus 로고    scopus 로고
    • Reviewed in: a S. A. W. Grunner, E. Locardi, E. Lohof, H. Kessler, Chem. Rev. 2002, 102, 491-514;
    • Reviewed in: a) S. A. W. Grunner, E. Locardi, E. Lohof, H. Kessler, Chem. Rev. 2002, 102, 491-514;
  • 30
    • 68949110818 scopus 로고    scopus 로고
    • In the case of AAAs 4 and 5 it is imperative to avoid prolonged existence of the intermediate iminophosphorane by using anhydrous reaction conditions. In anhydrous THF, the intermediate iminophosphorane suffered from nucleofilic attack of the iminophosphorane nitrogen on the AAA carbonyl, resulting in loss of the AAA moiety as depicted below. Premixing the THF with H2O prevented this side reaction to occur as gauged by LCMS analysis See the proposed side reaction during Staudinger reduction
    • 2O prevented this side reaction to occur as gauged by LCMS analysis (See the proposed side reaction during Staudinger reduction.)
  • 31
    • 0015151630 scopus 로고    scopus 로고
    • HNα in peptides is dependent on the dihedral angle φ [C(O)-N(H)-C α -C(O)] allowing the qualitative assignment of secondary structure N. Ramachandran, R. Chandrasekaran, K. D. Kopple, Biopolymers 1971, 10, 2113-2131.
    • HNα in peptides is dependent on the dihedral angle φ [C(O)-N(H)-C α -C(O)] allowing the qualitative assignment of secondary structure N. Ramachandran, R. Chandrasekaran, K. D. Kopple, Biopolymers 1971, 10, 2113-2131.
  • 32
    • 0026597879 scopus 로고    scopus 로고
    • The position of the Hα resonance signal of a residue in a particular peptide, relative to the value of that same residue in a random coil configuration (the chemical shift perturbation, Δ δHα) can be used as an indication of the configuration of that residue. A value of ΔδHα > 0.1 ppm indicates a β-strand, -0.1 < ΔδHα < 0.1 indicates a rondam coil and Δδ Hα < -0.1 ppm indicates a helical configuration. D. S. Wishart, B. D. Sykes, F. M. Richards, Biochemistry 1992, 31, 1647-1651.
    • The position of the Hα resonance signal of a residue in a particular peptide, relative to the value of that same residue in a random coil configuration (the chemical shift perturbation, Δ δHα) can be used as an indication of the configuration of that residue. A value of ΔδHα > 0.1 ppm indicates a β-strand, -0.1 < ΔδHα < 0.1 indicates a rondam coil and Δδ Hα < -0.1 ppm indicates a helical configuration. D. S. Wishart, B. D. Sykes, F. M. Richards, Biochemistry 1992, 31, 1647-1651.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.