NMR studies of peptide T, an inhibitor of HIV infectivity, in an aqueous environment
| Autor: | Devin N. Sears, Robert Tycko, Angel C. de Dios |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Anti-HIV Agents
Protein Conformation Stereochemistry Peptide Biochemistry chemistry.chemical_compound Structural Biology Drug Discovery Glycerol Nuclear Magnetic Resonance Biomolecular Molecular Biology Pharmacology chemistry.chemical_classification Aqueous solution biology Chemistry Organic Chemistry Water Peptide T Biological activity General Medicine Envelope glycoprotein GP120 Solutions Monomer Solid-state nuclear magnetic resonance biology.protein Molecular Medicine |
| Zdroj: | Journal of Peptide Science. 10:622-630 |
| ISSN: | 1099-1387 1075-2617 |
| DOI: | 10.1002/psc.571 |
| Popis: | The synthetic octapeptide peptide T (ASTTTNYT) has been shown to interfere with binding of the HIV-1 envelope glycoprotein gp120 to the chemokine receptor R5, thus preventing viral infection. This study investigated the degree of conformational order of two analogs of peptide T, one biologically active (D-Ala peptide T amide) and one inactive (D-Ala, D-Tyr peptide T amide) using nuclear magnetic resonance (NMR) spectroscopy in an aqueous environment, both in solution and in the frozen solid state. Standard solution NMR techniques such as DQFCOSY, HMQC, ROESY and inversion recovery measurements have been utilized to characterize these peptides. Solid state NMR experiments were likewise employed to study the peptides in a frozen glycerol:water mixture. The NMR results indicate that the monomeric form of both peptide T analogs have considerable conformational heterogeneity. Solid state NMR studies indicate aggregation of D-Ala peptide T, possibly into a β-sheet structure, at concentrations higher than 10 mM. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd. |
| Databáze: | OpenAIRE |
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