7 research outputs found
Inward Budding and Endocytosis of Membranes Regulated by de Novo Designed Peptides
Protein-mediated
endocytosis of membrane is a key event in biological
system. The mechanism, however, is still not clear. Using a de novo
designed bola-type peptide KKKLLLLLLLLKKK (K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>) as a protein mimic, we studied how it induced giant
unilamellar vesicle (GUV) to form inward buds or endocytosis at varying
conditions. Results show that the inward budding is initiated as the
charged lipids are neutralized by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>, which results in a negative spontaneous curvature. If the
charged lipids have unsaturated tails, the buddings are slim fibrils,
which can further wrap into a spherical structure. In the case of
saturated charged lipids, the buddings are rigid tubules, stable in
the studied time period. The unsaturated lipid to saturated lipid
ratio in the mother membrane is another key parameter governing the
shape and dynamics of the buds. A complete endocytosis is observed
when K<sub>3</sub>L<sub>8</sub>K<sub>3</sub> is attached with a hydrophobic
moiety, suggesting that hydrophobic interaction helps the buds to
detach from the mother membrane. The molecules in the surrounding
medium, such as negatively charged oligonucleotides, are engulfed
into the GUV via endocytosis pathway induced by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>. Our study provides a novel strategy for illustrating
the endocytosis mechanism by using peptides of simple sequence
Inward Budding and Endocytosis of Membranes Regulated by de Novo Designed Peptides
Protein-mediated
endocytosis of membrane is a key event in biological
system. The mechanism, however, is still not clear. Using a de novo
designed bola-type peptide KKKLLLLLLLLKKK (K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>) as a protein mimic, we studied how it induced giant
unilamellar vesicle (GUV) to form inward buds or endocytosis at varying
conditions. Results show that the inward budding is initiated as the
charged lipids are neutralized by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>, which results in a negative spontaneous curvature. If the
charged lipids have unsaturated tails, the buddings are slim fibrils,
which can further wrap into a spherical structure. In the case of
saturated charged lipids, the buddings are rigid tubules, stable in
the studied time period. The unsaturated lipid to saturated lipid
ratio in the mother membrane is another key parameter governing the
shape and dynamics of the buds. A complete endocytosis is observed
when K<sub>3</sub>L<sub>8</sub>K<sub>3</sub> is attached with a hydrophobic
moiety, suggesting that hydrophobic interaction helps the buds to
detach from the mother membrane. The molecules in the surrounding
medium, such as negatively charged oligonucleotides, are engulfed
into the GUV via endocytosis pathway induced by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>. Our study provides a novel strategy for illustrating
the endocytosis mechanism by using peptides of simple sequence
Inward Budding and Endocytosis of Membranes Regulated by de Novo Designed Peptides
Protein-mediated
endocytosis of membrane is a key event in biological
system. The mechanism, however, is still not clear. Using a de novo
designed bola-type peptide KKKLLLLLLLLKKK (K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>) as a protein mimic, we studied how it induced giant
unilamellar vesicle (GUV) to form inward buds or endocytosis at varying
conditions. Results show that the inward budding is initiated as the
charged lipids are neutralized by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>, which results in a negative spontaneous curvature. If the
charged lipids have unsaturated tails, the buddings are slim fibrils,
which can further wrap into a spherical structure. In the case of
saturated charged lipids, the buddings are rigid tubules, stable in
the studied time period. The unsaturated lipid to saturated lipid
ratio in the mother membrane is another key parameter governing the
shape and dynamics of the buds. A complete endocytosis is observed
when K<sub>3</sub>L<sub>8</sub>K<sub>3</sub> is attached with a hydrophobic
moiety, suggesting that hydrophobic interaction helps the buds to
detach from the mother membrane. The molecules in the surrounding
medium, such as negatively charged oligonucleotides, are engulfed
into the GUV via endocytosis pathway induced by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>. Our study provides a novel strategy for illustrating
the endocytosis mechanism by using peptides of simple sequence
Inward Budding and Endocytosis of Membranes Regulated by de Novo Designed Peptides
Protein-mediated
endocytosis of membrane is a key event in biological
system. The mechanism, however, is still not clear. Using a de novo
designed bola-type peptide KKKLLLLLLLLKKK (K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>) as a protein mimic, we studied how it induced giant
unilamellar vesicle (GUV) to form inward buds or endocytosis at varying
conditions. Results show that the inward budding is initiated as the
charged lipids are neutralized by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>, which results in a negative spontaneous curvature. If the
charged lipids have unsaturated tails, the buddings are slim fibrils,
which can further wrap into a spherical structure. In the case of
saturated charged lipids, the buddings are rigid tubules, stable in
the studied time period. The unsaturated lipid to saturated lipid
ratio in the mother membrane is another key parameter governing the
shape and dynamics of the buds. A complete endocytosis is observed
when K<sub>3</sub>L<sub>8</sub>K<sub>3</sub> is attached with a hydrophobic
moiety, suggesting that hydrophobic interaction helps the buds to
detach from the mother membrane. The molecules in the surrounding
medium, such as negatively charged oligonucleotides, are engulfed
into the GUV via endocytosis pathway induced by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>. Our study provides a novel strategy for illustrating
the endocytosis mechanism by using peptides of simple sequence
Inward Budding and Endocytosis of Membranes Regulated by de Novo Designed Peptides
Protein-mediated
endocytosis of membrane is a key event in biological
system. The mechanism, however, is still not clear. Using a de novo
designed bola-type peptide KKKLLLLLLLLKKK (K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>) as a protein mimic, we studied how it induced giant
unilamellar vesicle (GUV) to form inward buds or endocytosis at varying
conditions. Results show that the inward budding is initiated as the
charged lipids are neutralized by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>, which results in a negative spontaneous curvature. If the
charged lipids have unsaturated tails, the buddings are slim fibrils,
which can further wrap into a spherical structure. In the case of
saturated charged lipids, the buddings are rigid tubules, stable in
the studied time period. The unsaturated lipid to saturated lipid
ratio in the mother membrane is another key parameter governing the
shape and dynamics of the buds. A complete endocytosis is observed
when K<sub>3</sub>L<sub>8</sub>K<sub>3</sub> is attached with a hydrophobic
moiety, suggesting that hydrophobic interaction helps the buds to
detach from the mother membrane. The molecules in the surrounding
medium, such as negatively charged oligonucleotides, are engulfed
into the GUV via endocytosis pathway induced by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>. Our study provides a novel strategy for illustrating
the endocytosis mechanism by using peptides of simple sequence
Inward Budding and Endocytosis of Membranes Regulated by de Novo Designed Peptides
Protein-mediated
endocytosis of membrane is a key event in biological
system. The mechanism, however, is still not clear. Using a de novo
designed bola-type peptide KKKLLLLLLLLKKK (K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>) as a protein mimic, we studied how it induced giant
unilamellar vesicle (GUV) to form inward buds or endocytosis at varying
conditions. Results show that the inward budding is initiated as the
charged lipids are neutralized by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>, which results in a negative spontaneous curvature. If the
charged lipids have unsaturated tails, the buddings are slim fibrils,
which can further wrap into a spherical structure. In the case of
saturated charged lipids, the buddings are rigid tubules, stable in
the studied time period. The unsaturated lipid to saturated lipid
ratio in the mother membrane is another key parameter governing the
shape and dynamics of the buds. A complete endocytosis is observed
when K<sub>3</sub>L<sub>8</sub>K<sub>3</sub> is attached with a hydrophobic
moiety, suggesting that hydrophobic interaction helps the buds to
detach from the mother membrane. The molecules in the surrounding
medium, such as negatively charged oligonucleotides, are engulfed
into the GUV via endocytosis pathway induced by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>. Our study provides a novel strategy for illustrating
the endocytosis mechanism by using peptides of simple sequence
Inward Budding and Endocytosis of Membranes Regulated by de Novo Designed Peptides
Protein-mediated
endocytosis of membrane is a key event in biological
system. The mechanism, however, is still not clear. Using a de novo
designed bola-type peptide KKKLLLLLLLLKKK (K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>) as a protein mimic, we studied how it induced giant
unilamellar vesicle (GUV) to form inward buds or endocytosis at varying
conditions. Results show that the inward budding is initiated as the
charged lipids are neutralized by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>, which results in a negative spontaneous curvature. If the
charged lipids have unsaturated tails, the buddings are slim fibrils,
which can further wrap into a spherical structure. In the case of
saturated charged lipids, the buddings are rigid tubules, stable in
the studied time period. The unsaturated lipid to saturated lipid
ratio in the mother membrane is another key parameter governing the
shape and dynamics of the buds. A complete endocytosis is observed
when K<sub>3</sub>L<sub>8</sub>K<sub>3</sub> is attached with a hydrophobic
moiety, suggesting that hydrophobic interaction helps the buds to
detach from the mother membrane. The molecules in the surrounding
medium, such as negatively charged oligonucleotides, are engulfed
into the GUV via endocytosis pathway induced by K<sub>3</sub>L<sub>8</sub>K<sub>3</sub>. Our study provides a novel strategy for illustrating
the endocytosis mechanism by using peptides of simple sequence