Abstract
In Chap. 29, “Agonists and Antagonists of Membrane-Bound Receptors,” receptors were discussed that allow a signal transmission from outside the cell to its interior. Numerous processes in the cell are initiated by these systems that alter the cell’s state. In addition to this type of information exchange, a cell must also have other ways to remain constantly in contact with its environment. To accomplish this task, they have many other surface receptors. For example, the cell’s integrin receptor not only can accept signals from outside, it can also transmit signals into the environment. If a cell moves, for example in a blood vessel or in tissue, it must remain in constant communication with the environment during the translocation. In this way, leukocytes find their way to sites of infection as part of immune response to pathogens. For this, they receive signals from the environment through their surfaces by using special surface receptors. In viral disease, a virus attempts to adhere to a host cell and finally to penetrate the cell. The recognition of endogenous cell-surface receptors or special adhesion molecules initially occurs before the target cell under attack can be reprogrammed in the invasion process. After viral maturation and reproduction, the new virus must be budded and released from the infected host cell (exocytosis). Proteins that are exposed to the surface also regulate this process. Drugs can be used to intervene in both processes: the attack by and release of viruses. Our immune system uses specific surface proteins to distinguish between diseased and healthy cells. Influencing these processes leads to immune stimulation. The structure and function of the above-mentioned surface receptors shall be discussed in this chapter. How specific ligands can suppress or reprogram the actual tasks of these surface receptors to lead to a successful therapeutic concept shall be explained.
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Bibliography
General Literature
Andronati SA, Karaseva TL, Krysko AA (2004) Peptidomimetics– antagonists of the fibrinogen receptors: molecular design, structures, properties and therapeutic applications. Curr Med Chem 11:1183–1211
Chhabra SR, Abdul Rahim AS, Kellam B (2003) Recent progress in the design of selectin inhibitors. Mini Rev Med Chem 3:679–687
De Palma AM, Vliegen I, De Clercq E, Neyts J (2008) Selective inhibitors of picornavirus replication. Med Res Rev 28:823–884
Doranz BJ, Baik SW, Doms RW (1999) Use of a gp120 binding assay to dissect the requirements and kinetics of human immunodeficiency virus fusion events. J Virol 12:10346–10358
Kolata G (2001) The story of the great influenza pandemic of 1918 and the search for the virus that caused it. Touchstone, New York
Lazoura E, Apostolopoulos V (2005) Rational peptide-based vaccine design for cancer immunotherapeutic applications. Curr Med Chem 12:629–639
Matthews T, Salgo M et al (2004) Enfuvirtide: the first therapy to inhibit the entry of HIV-1 into host CD4 lymphocytes. Nat Rev Drug Discov 3:215–225
Shimaoka M, Springer TA (2003) Therapeutic antagonists and conformational regulation of integrin function. Nat Rev Drug Discov 2:703–716
Somers WS, Tang J, Shaw GD, Camphausen RT (2000) Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLeX and PSGL-1. Cell 103:467–479
von Itzstein M (2007) The war against influenza: discovery and development of sialidase inhibitors. Nat Rev Drug Discov 6:967–974
Special Literature
Douat-Casassus C, Marchand-Geneste N, Diez E, Gervois N, Jotereau F, Quideau S (2007) Synthetic anticancer vaccine candidates: rational design of antigenic peptide mimetics that activate tumor-specific T-cells. J Med Chem 50:1598–1609
Garboczi DN et al (1996) Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384:134–141
Jiang S, Zhao Q, Debnath AK (2002) Peptide and non-peptide HIV fusion inhibitors. Curr Pharm Des 8:563–580
Kim CU, Lew W et al (1997) Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J Am Chem Soc 119:681–690
Kim CU, Lew W et al (1998) Structure–activity relationship studies of novel carbocyclic influenza neuraminidase inhibitors. J Med Chem 41:2451–2460
Kolatkar PR et al (1999) Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor. EMBO J 18:6249–6259
Kranich R, Busemann AS et al (2007) Rational design of novel, potent small molecule pan-selectin antagonists. J Med Chem 50:1101–1115
Ku TW, Ali FE, Barton LS et al (1993) Direct design of a potent non-peptide fibrinogen receptor antagonist based on the structure and conformation of a highly constrained cyclic RGD peptide. J Am Chem Soc 115:8861–8862
Smith PW, Sollis SL et al (1996) Novel inhibitors of influenza silaidases related to GGI67. Bioorg Med Chem Lett 6:2931–2936
Williams MA, Lew W et al (1997) Structure–activity relationships of carbocyclic influenza neuraminidase inhibitors. Bioorg Med Chem Lett 7:1837–1842
Zablocki JA, Rico JG, Garland RB, Zablocki JA, Rico JG, Garland RB et al (1995) Potent in vitro and in vivo inhibitors of platelet aggregation based upon the Arg-Gly-Asp sequence of fibrinogen. (Aminobenzamidino)succinyl (ABAS) series of orally active fibrinogen receptor antagonists. J Med Chem 38:2378–2394
Zhang Y et al (2004) Structural and virological studies of the stages of virus replication that are affected by antirhinovirus compounds. J Virol 78:11061–11069
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Klebe, G. (2013). Ligands for Surface Receptors. In: Klebe, G. (eds) Drug Design. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-17907-5_31
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DOI: https://doi.org/10.1007/978-3-642-17907-5_31
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