5 research outputs found
Β«ΠΠ°Π»ΠΎΠ±ΡΠ΄ΠΆΠ΅ΡΠ½ΠΈΠΉΒ» ΠΌΠ°ΡΠΊΠ΅ΡΠΈΠ½Π³
Π ΡΠΌΠΎΠ²Π°Ρ
ΡΡΠΎΠ³ΠΎΠ΄Π½ΡΡΠ½ΡΠΎΡ Π΅ΠΊΠΎΠ½ΠΎΠΌΡΡΠ½ΠΎΡ ΠΊΡΠΈΠ·ΠΈ, ΡΠΊΠ° Π·Π°ΡΠ΅ΠΏΠΈΠ»Π° Π²ΡΡ Π²ΡΡΡΠΈΠ·Π½ΡΠ½Ρ ΠΏΡΠ΄ΠΏΡΠΈΡΠΌΡΡΠ²Π°, ΡΠ° ΠΏΠΎΡΡΡΠΉΠ½ΠΎΠ³ΠΎ Π·Π½ΠΈΠΆΠ΅Π½Π½Ρ ΡΠΊΡΠ°ΡΠ½ΡΡΠΊΠΎΡ Π½Π°ΡΡΠΎΠ½Π°Π»ΡΠ½ΠΎΡ Π²Π°Π»ΡΡΠΈ Π°ΠΊΡΡΠ°Π»ΡΠ½ΠΈΠΌΠΈ ΡΡΠ°ΡΡΡ ΠΏΠΈΡΠ°Π½Π½Ρ ΠΏΠΎΡΡΠΊΡ ΡΠΏΠΎΡΠΎΠ±ΡΠ² Π΅ΠΊΠΎΠ½ΠΎΠΌΡΡ ΠΊΠΎΡΡΡΠ². ΠΠΈΡΡΡΠ΅Π½Π½ΡΠΌ ΡΠ°ΠΊΠΈΡ
ΠΏΡΠΎΠ±Π»Π΅ΠΌ ΠΌΠΎΠΆΠ΅ ΡΡΠ°ΡΠΈ Β«ΠΌΠ°Π»ΠΎ Π±ΡΠ΄ΠΆΠ΅ΡΠ½ΠΈΠΉΒ» ΠΌΠ°ΡΠΊΠ΅ΡΠΈΠ½Π³, ΡΠΊΠΈΠΉ Π΄ΠΎΠΏΠΎΠΌΠΎΠΆΠ΅ ΡΠΎΠ·Π²ΠΈΠ²Π°ΡΠΈΡΡ ΠΏΡΠ΄ΠΏΡΠΈΡΠΌΡΡΠ²Ρ Π· Π²ΠΈΠΊΠΎΡΠΈΡΡΠ°Π½Π½ΡΠΌ ΠΌΡΠ½ΡΠΌΠ°Π»ΡΠ½ΠΎΡ ΠΊΡΠ»ΡΠΊΠΎΡΡΡ ΡΠ΅ΡΡΡΡΡΠ².
Β«ΠΠ°Π»ΠΎΠ±ΡΠ΄ΠΆΠ΅ΡΠ½ΠΈΠΉΒ» ΠΌΠ°ΡΠΊΠ΅ΡΠΈΠ½Π³ β ΡΠ΅ ΠΌΠ°ΡΠΊΠ΅ΡΠΈΠ½Π³ΠΎΠ²Ρ ΡΠ½ΡΡΡΡΠΌΠ΅Π½ΡΠΈ Π·Π°Π»ΡΡΠ΅Π½Π½Ρ ΠΉ ΡΡΡΠΈΠΌΠ°Π½Π½Ρ ΠΊΠ»ΡΡΠ½ΡΡΠ², ΡΠΊΡ ΠΏΡΠΈΠΏΡΡΠΊΠ°ΡΡΡ ΠΌΡΠ½ΡΠΌΠ°Π»ΡΠ½Ρ Π²ΠΈΡΡΠ°ΡΠΈ, Π° ΡΠ½ΠΎΠ΄Ρ ΠΌΠΎΠΆΠ½Π° Π²Π·Π°Π³Π°Π»Ρ ΠΎΠ±ΡΠΉΡΠΈΡΡ Π±Π΅Π· Π±ΡΠ΄ΠΆΠ΅ΡΡ
On Crystal versus Fiber Formation in Dipeptide Hydrogelator Systems
Naphthalene dipeptides have been shown to be useful low-molecular-weight
gelators. Here we have used a library to explore the relationship
between the dipeptide sequence and the hydrogelation efficiency. A
number of the naphthalene dipeptides are crystallizable from water,
enabling us to investigate the comparison between the gel/fiber phase
and the crystal phase. We succeeded in crystallizing one example directly
from the gel phase. Using X-ray crystallography, molecular modeling,
and X-ray fiber diffraction, we show that the molecular packing of
this crystal structure differs from the structure of the gel/fiber
phase. Although the crystal structures may provide important insights
into stabilizing interactions, our analysis indicates a rearrangement
of structural packing within the fibers. These observations are consistent
with the fibrillar interactions and interatomic separations promoting
1D assembly whereas in the crystals the peptides are aligned along
multiple axes, allowing 3D growth. This observation has an impact
on the use of crystal structures to determine supramolecular synthons
for gelators
On Crystal versus Fiber Formation in Dipeptide Hydrogelator Systems
Naphthalene dipeptides have been shown to be useful low-molecular-weight
gelators. Here we have used a library to explore the relationship
between the dipeptide sequence and the hydrogelation efficiency. A
number of the naphthalene dipeptides are crystallizable from water,
enabling us to investigate the comparison between the gel/fiber phase
and the crystal phase. We succeeded in crystallizing one example directly
from the gel phase. Using X-ray crystallography, molecular modeling,
and X-ray fiber diffraction, we show that the molecular packing of
this crystal structure differs from the structure of the gel/fiber
phase. Although the crystal structures may provide important insights
into stabilizing interactions, our analysis indicates a rearrangement
of structural packing within the fibers. These observations are consistent
with the fibrillar interactions and interatomic separations promoting
1D assembly whereas in the crystals the peptides are aligned along
multiple axes, allowing 3D growth. This observation has an impact
on the use of crystal structures to determine supramolecular synthons
for gelators
On Crystal versus Fiber Formation in Dipeptide Hydrogelator Systems
Naphthalene dipeptides have been shown to be useful low-molecular-weight
gelators. Here we have used a library to explore the relationship
between the dipeptide sequence and the hydrogelation efficiency. A
number of the naphthalene dipeptides are crystallizable from water,
enabling us to investigate the comparison between the gel/fiber phase
and the crystal phase. We succeeded in crystallizing one example directly
from the gel phase. Using X-ray crystallography, molecular modeling,
and X-ray fiber diffraction, we show that the molecular packing of
this crystal structure differs from the structure of the gel/fiber
phase. Although the crystal structures may provide important insights
into stabilizing interactions, our analysis indicates a rearrangement
of structural packing within the fibers. These observations are consistent
with the fibrillar interactions and interatomic separations promoting
1D assembly whereas in the crystals the peptides are aligned along
multiple axes, allowing 3D growth. This observation has an impact
on the use of crystal structures to determine supramolecular synthons
for gelators
On Crystal versus Fiber Formation in Dipeptide Hydrogelator Systems
Naphthalene dipeptides have been shown to be useful low-molecular-weight
gelators. Here we have used a library to explore the relationship
between the dipeptide sequence and the hydrogelation efficiency. A
number of the naphthalene dipeptides are crystallizable from water,
enabling us to investigate the comparison between the gel/fiber phase
and the crystal phase. We succeeded in crystallizing one example directly
from the gel phase. Using X-ray crystallography, molecular modeling,
and X-ray fiber diffraction, we show that the molecular packing of
this crystal structure differs from the structure of the gel/fiber
phase. Although the crystal structures may provide important insights
into stabilizing interactions, our analysis indicates a rearrangement
of structural packing within the fibers. These observations are consistent
with the fibrillar interactions and interatomic separations promoting
1D assembly whereas in the crystals the peptides are aligned along
multiple axes, allowing 3D growth. This observation has an impact
on the use of crystal structures to determine supramolecular synthons
for gelators