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Full-Text Articles in Physical Sciences and Mathematics
Hiv Fusion Peptide Penetrates, Disorders, And Softens T-Cell Membrane Mimics., Stephanie Tristram-Nagle, Rob Chan, Edgar Kooijman, Pradeep Uppamoochikkal, Wei Qiang, David Weliky, Pradeep Uppamoochikkal
Hiv Fusion Peptide Penetrates, Disorders, And Softens T-Cell Membrane Mimics., Stephanie Tristram-Nagle, Rob Chan, Edgar Kooijman, Pradeep Uppamoochikkal, Wei Qiang, David Weliky, Pradeep Uppamoochikkal
Prof. Stephanie Tristram-Nagle Ph.D.
This work investigates the interaction of N-terminal gp41 fusion peptide (FP) of human immunodeficiency virus type 1 (HIV-1) with model membranes in order to elucidate how FP leads to fusion of HIV and T-cell membranes. FP constructs were (i) wild-type FP23 (23 N-terminal amino acids of gp41), (ii) water-soluble monomeric FP that adds six lysines on the C-terminus of FP23 (FPwsm), and (iii) the C-terminus covalently linked trimeric version (FPtri) of FPwsm. Model membranes were (i) LM3 (a T-cell mimic), (ii) 1,2-dioleoyl-sn-glycero-3-phosphocholine, (iii) 1,2-dioleoyl-sn-glycero-3-phosphocholine/30 mol% cholesterol, (iv) 1,2-dierucoyl-sn-glycero-3-phosphocholine, and (v) 1,2-dierucoyl-sn-glycero-3-phosphocholine/30 mol% cholesterol. Diffuse synchrotron low-angle x-ray scattering from fully …
Crac Motif Peptide Of The Hiv-1 Gp41 Protein Thins Sopc Membranes And Interacts With Cholesterol., Alexander Greenwood, Jianjun Pan, Thalia Mills, John Nagle, Richard Epand, Stephanie Tristram-Nagle
Crac Motif Peptide Of The Hiv-1 Gp41 Protein Thins Sopc Membranes And Interacts With Cholesterol., Alexander Greenwood, Jianjun Pan, Thalia Mills, John Nagle, Richard Epand, Stephanie Tristram-Nagle
Prof. Stephanie Tristram-Nagle Ph.D.
This study uses low-angle (LAXS) and wide-angle (WAXS) X-ray synchrotron scattering, volume measurements and thin layer chromatography to determine the structure and interactions of SOPC, SOPC/cholesterol mixtures, SOPC/peptide and SOPC/cholesterol/peptide mixtures. N-acetyl-LWYIK-amide (LWYIK) represents the naturally-occurring CRAC motif segment in the pretransmembrane region of the gp41 protein of HIV-1, and N-acetyl-IWYIK-amide (IWYIK), an unnatural isomer, is used as a control. Both peptides thin the SOPC bilayer by approximately 3 A, and cause the area/unit cell (peptide+SOPC) to increase by approximately 9 A2 from the area/lipid of SOPC at 30 degrees C (67.0+/-0.9 A2). Model fitting suggests that LWYIK's average position …