The helix-to-sheet transition of an HIV-1 fusion peptide derivative changes the mechanical properties of lipid bilayer membranes.

Heller, William T; Zolnierczuk, Piotr A

Heller, William T; Zolnierczuk, Piotr A.

Affiliation

Heller WT; Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, United States of America. Electronic address: hellerwt@ornl.gov.
Zolnierczuk PA; Forschungszentrum Jülich GmbH, Jülich Centre for Neutron Science at SNS, Oak Ridge National Laboratory, Oak Ridge, TN 37831, United States of America.

Biochim Biophys Acta Biomembr ; 1861(3): 565-572, 2019 03 01.

Article in En | MEDLINE | ID: mdl-30550881

Subject(s)

Biomechanical Phenomena/physiology; HIV Envelope Protein gp41/chemistry; Lipid Bilayers/chemistry; Membrane Fusion/drug effects; Amino Acid Sequence; Cell Membrane/drug effects; Cell Membrane/physiology; Circular Dichroism; Dynamic Light Scattering; HIV Envelope Protein gp41/pharmacology; HIV-1/physiology; Humans; Lipid Bilayers/metabolism; Magnetic Resonance Spectroscopy; Membrane Fluidity/drug effects; Membrane Fusion/genetics; Models, Molecular; Peptides/chemistry; Peptides/pharmacology; Protein Structure, Secondary/physiology; Structure-Activity Relationship

Key words

Bilayer dynamics; HIV-1 fusion peptide; Membrane rigidity; Neutron spin echo spectroscopy

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Biomechanical Phenomena / HIV Envelope Protein gp41 / Lipid Bilayers / Membrane Fusion Limits: Humans Language: En Journal: Biochim Biophys Acta Biomembr Year: 2019 Document type: Article Country of publication: Netherlands

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