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Query: UNIPROT:P01189 (
beta-endorphin
)
21,003
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The interaction of the peptide hormone
adrenocorticotropin
with solvent-free planar lipid bilayers (
BLM
) and liposomes was studied by measurements of elasticity modulus perpendicular to the plane of the membrane (E perpendicular, measured by electrostriction), surface potential difference (delta phi m), electrical capacitance, capacitance relaxation following a voltage jump (yielding relaxation times for molecular dipoles or dipolar domains), and fluorescence polarization. Addition of the 6-fold positively charged peptide to one side of the membrane leads to a more positive membrane surface potential, an increase of
BLM
capacitance, a decrease of elasticity modulus, and faster relaxation time constants. This also caused a decrease of DPH fluorescence anisotropy of the liposome suspension modified by fluorescent dye DPH. Mixed
BLM
of palmitoyl-oleoyl-phosphatidylcholine (POPC)+soybean phosphatidylcholine (SBPC) (10:1 w/w), which carry a negative surface charge, exhibit considerably larger changes than electroneutral POPC membranes. Our results confirm that ACTH1-24 binds to
BLM
and interacts with the hydrophobic part of the bilayer.
...
PMID:Interaction of adrenocorticotropin-(1-24)-tetracosapeptide with lipid bilayers. 907 6