Probing Pores with Peptide Plugs
نویسندگان
چکیده
منابع مشابه
Probing Pores with Peptide Plugs
Extracellular proteins are made in the cytosol and transported out of the cell. Certain proteins travel the opposite way, from the outside to the cytosol. Most of these proteins are toxins made by bacteria and plants, but evidence is accumulating that certain growth factors can do the same. Toxins that enter the cytosol can, according to current knowledge, be roughly classified into two main gr...
متن کاملProbing Pores with Peptide Plugs: Topology of Membrane-inserted Diphtheria Toxin
Extracellular proteins are made in the cytosol and transported out of the cell. Certain proteins travel the opposite way, from the outside to the cytosol. Most of these proteins are toxins made by bacteria and plants, but evidence is accumulating that certain growth factors can do the same. Toxins that enter the cytosol can, according to current knowledge, be roughly classified into two main gr...
متن کاملModeling peptide binding to anionic membrane pores
Peptide-induced pore formation in membranes can be dissected into two steps: pore formation and peptide binding to the pore. A computational method is proposed to study the second step in anionic membranes. The electrostatic potential is obtained from numerical solutions to the Poisson-Boltzmann equation and is then used in conjunction with IMM1 (implicit membrane model 1). A double charge laye...
متن کاملTransmembrane pores formed by human antimicrobial peptide LL-37.
Human LL-37 is a multifunctional cathelicidin peptide that has shown a wide spectrum of antimicrobial activity by permeabilizing microbial membranes similar to other antimicrobial peptides; however, its molecular mechanism has not been clarified. Two independent experiments revealed LL-37 bound to membranes in the α-helical form with the axis lying in the plane of membrane. This led to the conc...
متن کاملMolecular mechanism of Peptide-induced pores in membranes.
We suggest a physical mechanism by which antimicrobial peptides spontaneously induce stable pores in membranes. Peptide binding to a lipid bilayer causes an internal stress, or internal membrane tension, that can be sufficiently strong to create pores. Like detergents, peptides have a high affinity for the rim of the pore. Binding to the rims reduces the line tension and decreases the number of...
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ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 2000
ISSN: 0022-1295,1540-7748
DOI: 10.1085/jgp.115.4.417