Tools for Structural Lectinomics: From Structures to Lectomes
BBA Advances,
Год журнала:
2025,
Номер
unknown, С. 100154 - 100154
Опубликована: Март 1, 2025
Lectins
are
ubiquitous
proteins
that
interact
with
glycans
in
a
variety
of
molecular
processes
and
as
such,
also
play
role
diseases,
whether
infectious,
chronic
or
cancer-related.
The
systematic
study
lectins
is
therefore
essential,
particular
for
understanding
cell-cell
communication.
Accumulated
protein
three-dimensional
structural
data
the
past
decades
boosted
advance
AI-based
prediction
opened
up
new
options
to
characterise
known
often
be
multimeric
multivalent.
This
article
reviews
methods
obtain
structures
lectins,
current
available
lectin
3D
their
interactions,
how
this
knowledge
used
classify
these
shows
combination
an
array
bioinformatics
tools
should
make
binding
specificity
possible
near
future.
Язык: Английский
Controlling Glycan Folding with Ionic Functional Groups
Journal of the American Chemical Society,
Год журнала:
2025,
Номер
unknown
Опубликована: Апрель 24, 2025
Glycans
are
intrinsically
flexible
molecules
that
can
adopt
many
conformations.
These
often
carry
ionic
functional
groups
influence
glycan's
conformational
preferences,
dynamics,
and
aggregation
tendencies.
Inspired
by
these
mechanisms,
we
have
engineered
a
glycan
sequence
whose
secondary
structure
be
precisely
manipulated
using
groups.
We
strategically
incorporated
substituents
into
adopting
hairpin
conformation.
Complementary
stabilized
the
closed
conformers,
while
repulsions
shifted
populations
toward
open
forms.
External
stimuli,
such
as
pH
variations
or
enzyme
addition,
enabled
us
to
dynamically
control
hairpin's
opening
closing.
Additionally,
changes
in
protonation
states
led
aggregation,
suggesting
opportunities
for
creation
of
responsive
glycan-based
materials.
Язык: Английский
The synergy of experimental and computational approaches for visualizing glycoprotein dynamics: Exploring order within the apparent disorder of glycan conformational ensembles
Current Opinion in Structural Biology,
Год журнала:
2025,
Номер
92, С. 103049 - 103049
Опубликована: Апрель 29, 2025
Understanding
the
dynamic
behavior
of
glycoproteins
is
crucial
for
deciphering
their
biological
roles.
This
review
explores
synergistic
use
experimental
and
computational
methods
to
address
this
complex
challenge.
Glycans,
with
inherent
flexibility
structural
diversity,
pose
significant
obstacles
traditional
analysis.
Innovative
techniques
offer
valuable
snapshots
glycan
conformations,
but
often
lack
context
a
physiological
environment.
Computational
simulations
provide
atomic-level
detail
explore
full
range
motions,
require
extensive
resources
validation.
Integrating
these
approaches,
by
using
data
refine
validate
models,
essential
accurately
capturing
interplay
between
glycans
proteins.
combined
strategy
promises
unlock
deeper
understanding
glycoprotein
function
inform
design
novel
therapeutics.
Язык: Английский
Effects of Different Adduct Ions, Ionization Temperatures, and Solvents on the Ion Mobility of Glycans
Molecules,
Год журнала:
2025,
Номер
30(10), С. 2177 - 2177
Опубликована: Май 15, 2025
The
structural
analysis
of
glycans
remains
a
major
challenge
due
to
their
high
isomeric
complexity
and
conformational
flexibility
arising
from
diverse
glycosidic
linkages
dynamic
three-dimensional
structures.
Ion
mobility-mass
spectrometry
(IM-MS)
has
been
attracting
attention
as
way
develop
the
glycans.
In
this
study,
effects
ionization
conditions-including
different
types
adduct
ions,
temperatures,
solvent
environments-on
ion
mobility
behavior
were
systematically
investigated.
IM-MS
measurements
ethylamine-tagged
showed
broad
arrival
time
distributions
monoprotonated
ions
indicating
presence
multiple
conformers
Increased
temperatures
use
methanol
further
broadened
distribution,
suggesting
enhanced
dynamics
glycan
ions.
contrast,
sodium
yielded
narrower
distributions,
implying
that
interactions
between
constrained
flexibility.
These
results
demonstrate
parameters
have
significant
impact
on
in
gas
phase.
This
study
provides
insights
into
analytical
conditions
for
highlights
utility
method
powerful
tool
elucidating
structure
dynamics.
Язык: Английский