Peptide conjugates as tools for the study of biological signal transduction

被引:25
作者
Eisele, F [1 ]
Owen, DJ [1 ]
Waldmann, H [1 ]
机构
[1] Univ Karlsruhe, Inst Organ Chem, D-76128 Karlsruhe, Germany
关键词
bioorganic chemistry; enzyme inhibition; organic synthesis; peptide conjugate; signal transduction;
D O I
10.1016/S0968-0896(98)00204-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Today, many biological phenomena are being investigated and understood in molecular detail, and organic chemistry is increasingly being directed towards biological phenomena. This review is intended to highlight this interplay of organic chemistry and biology, using biological signal transduction as an example. Lipo-, glyco-, phospho- and nucleoproteins play key roles in the processes whereby chemical signals are passed across cell membranes and further to the cell nucleus. For the study of the biological phenomena associated with these protein conjugates, structurally well-defined peptides containing the characteristic linkage region of the peptide backbone with the lipid, the carbohydrate or the phosphoric acid ester can provide valuable tools. The multi-functionality and pronounced acid- and base-lability of such compounds renders their synthesis a formidable challenge to conventional organic synthesis. However, the recent development of enzymatic protecting groups, provides one of the central techniques which, when coupled with classic chemical synthesis, can provide access to these complex and sensitive biologically relevant peptide conjugates under particularly mild conditions and with high selectivity. (C) 1999 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:193 / 224
页数:32
相关论文
共 189 条
  • [91] Parallel synthesis and screening of a solid phase carbohydrate library
    Liang, R
    Yan, L
    Loebach, J
    Ge, M
    Uozumi, Y
    Sekanina, K
    Horan, N
    Gildersleeve, J
    Thompson, C
    Smith, A
    Biswas, K
    Still, WC
    Kahne, D
    [J]. SCIENCE, 1996, 274 (5292) : 1520 - 1522
  • [92] Synthesis of sialyl Lewis X mimetics and related structures using the glycosyl phosphite methodology and evaluation of E-selectin inhibition
    Lin, CC
    Shimazaki, M
    Heck, MP
    Aoki, S
    Wang, R
    Kimura, T
    Ritzen, H
    Takayama, S
    Wu, SH
    WeitzSchmidt, G
    Wong, CH
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (29) : 6826 - 6840
  • [93] PROTEIN GLYCOSYLATION - STRUCTURAL AND FUNCTIONAL-ASPECTS
    LIS, H
    SHARON, N
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1993, 218 (01): : 1 - 27
  • [94] LIU L, 1995, METHOD ENZYMOL, V250, P189
  • [95] APPLICATION OF SYNTHETIC PHOSPHO-PEPTIDES AND UNPHOSPHO-PEPTIDES TO IDENTIFY PHOSPHORYLATION SITES IN A SUBREGION OF THE TAU-MOLECULE, WHICH IS MODIFIED IN ALZHEIMERS-DISEASE
    LIU, WK
    MOORE, WT
    WILLIAMS, RT
    HALL, FL
    YEN, SH
    [J]. JOURNAL OF NEUROSCIENCE RESEARCH, 1993, 34 (03) : 371 - 376
  • [96] Liu WK, 1996, J NEUROCHEM, V66, P1131
  • [97] LODISH H, 1996, MOL ZELLBIOLOGIE, pCH20
  • [98] LONGENECKER BM, 1993, ANN NY ACAD SCI, V690, P276
  • [99] Lu KP, 1996, NATURE, V380, P544
  • [100] FARNESYL DERIVATIVES OF RIGID CARBOXYLIC ACIDS-INHIBITORS OF RAS-DEPENDENT CELL-GROWTH
    MARCIANO, D
    BENBARUCH, G
    MAROM, M
    EGOZI, Y
    HAKLAI, R
    KLOOG, Y
    [J]. JOURNAL OF MEDICINAL CHEMISTRY, 1995, 38 (08) : 1267 - 1272