Professor Mobley

Our research is directed at understanding the mechanisms of viral fusion. We have studied primarily the fusion peptide (FP) from HIV. At low concentrations, FP binds to the membrane as an alpha helix from residues 1 to 15. (See 1ERF figure) A spin-label attached to methionine 19 senses a polar environment, whereas a spin-label attached to the N-terminus behaves as if it were at the twelfth carbon of the membrane phospholipid acyl group.(see met-spin labeled FP in membrane figure) At higher concentrations, more of FP is in the beta conformation. The alpha conformation is probably necessary for insertion into the membrane, but beta may be required for the fusion.

Recent Publications

Gordon LM, Nisthal A, Lee AB, Eskandari S, Ruchala P, Jung C-L, Waring AJ, Mobley PW (2008) Structural and Functional Properties of Peptides Based on the N-terminus of HIV-1 gp41 and the C-terminus of the Amyloid-beta Protein. Biochimica et Biophysica Acta, 1778(10), 2127-37

Mobley PW, Barry JA, Waring AJ, Sherman MA, Gordon LM (2007) Membrane Perturbing Actions of HIV Type 1 Glycoprotein 41 Domains are Inhibited by Helical C-Peptides. AIDS Research and Human Retroviruses, 23(2), 224 - 242

Mobley P, Nisthal M, Julius J, Kelber J, Gonzalez A, Eskandari S, Waring A, and Gordon L (2005) The HIV-1 Fusion Peptide has Amyloid Properties. Proceedings of the 19th American Peptide Symposium, pgs 686-687. S. Blondelle, Editor

Gordon LM, Mobley PW, Lee W, Eskandari S, Kaznessis YN, Sherman MA, Waring AJ (2004) Conformational mapping of the N-terminal peptide of HIV-1 gp 41 in lipid detergent and aqueous environments using 13C-enhanced Fourier transform infrared spectroscopy. Protein Science, 13: 1012 - 1030

Gordon LM, Mobley PW, Pilpa R, Sherman MA, Waring AJ (2002) Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using 13C-enhanced Fourier transform infrared spectroscopy. Biochim Biophys Acta, 1559(2): 96-120.

Mobley PW, Waring AJ, Gordon LM (2002) Structure and Activity of the N-Terminal Peptides of HIV-1 Glycoprotein 41 Types M (Major) and O (Outlier) in Proceedings of the 2nd International and 17th American Peptide Symposium, pgs 963-964. M Lebl and RA Houghten, Editors

Mobley PW, Pilpa R, Brown C, Waring AJ, Gordon LM.(2001) Membrane-perturbing domains of HIV type 1 glycoprotein 41. AIDS Res Human Retroviruses, 17(4):311-27.

Mobley PW, Waring AJ, Sherman MA, Gordon LM (1999) Membrane interactions of the synthetic N-terminal peptide of HIV-1 gp41 and its structural analogs. Biochim Biophys Acta, 1418(1):1-18.

Waring, AJ, Mobley, PW Gordon, LM (1998) Conformational mapping of a viral fusion peptide in structure-promoting solvents using circular dichroism and electrospray mass spectrometry. Proteins, Suppl 2:38-49.

Curtain CC, Lowe MG, Arunagiri CK, Mobley PW, Macreadie IG, Azad AA (1997) Cytotoxic activity of the amino-terminal region of HIV type 1 nef protein. AIDS Res Hum Retrovir, 13(14): 1213-1220.