Metabolomics and proteomics: synergistic tools for understanding snake venom inhibition
Archives of Toxicology,
Journal Year:
2025,
Volume and Issue:
unknown
Published: Jan. 6, 2025
Language: Английский
The application of snake venom in anticancer drug discovery: an overview of the latest developments
Expert Opinion on Drug Discovery,
Journal Year:
2025,
Volume and Issue:
unknown, P. 1 - 19
Published: Feb. 26, 2025
Snake
venom
is
a
rich
source
of
toxins
with
great
potential
for
therapeutic
applications.
In
addition
to
its
efficacy
in
treating
hypertension,
acute
coronary
syndrome,
and
other
heart
conditions,
research
has
shown
that
this
potent
enzymatic
cocktail
capable
selectively
targeting
destroying
cancer
cells
many
cases
while
sparing
healthy
cells.
The
authors
begin
by
acknowledging
the
emerging
trends
snake-derived
targeted
therapies
battling
cancer.
An
extensive
literature
review
examining
effects
various
snake
on
cell
lines,
highlighting
specific
hallmarks
each
toxin
targets
presented.
Furthermore,
emphasize
artificial
intelligence
accelerating
venom-based
drug
discovery
treatment,
showcasing
several
innovative
software
applications
field.
Research
indicates
promising
treatment
as
discussed
can
specifically
target
Nevertheless,
variations
composition
venoms,
ethical
issues,
delivery
barriers
limit
their
development
into
effective
therapies.
Thus,
advances
biotechnology,
molecular
engineering,
silico
methods
are
crucial
refinement
venom-derived
compounds,
improving
specificity,
overcoming
these
challenges,
ultimately
enhancing
therapy.
Language: Английский
Growth Inhibitory Peptides: A Potential Novel Therapeutic Approach to Cancer Treatment
Aixin Wang,
No information about this author
Gerald J. Mizejewski,
No information about this author
Chengqi Zhang
No information about this author
et al.
European Journal of Pharmacology,
Journal Year:
2025,
Volume and Issue:
unknown, P. 177554 - 177554
Published: March 1, 2025
Language: Английский
Macrovipera lebetinus obtusa Venom and Its Fractions Affect Human Dermal Microvascular Endothelial and Fibrosarcoma Cells
Nariné Ghazaryan,
No information about this author
Lars van Werven,
No information about this author
Thomas Liepold
No information about this author
et al.
International Journal of Molecular Sciences,
Journal Year:
2025,
Volume and Issue:
26(8), P. 3601 - 3601
Published: April 11, 2025
The
venom
of
Macrovipera
lebetinus
obtusa
(MLO)
has
remarkable
properties
that
are
hard
to
overlook.
This
venom's
described
38
protein
components
work
synergistically,
forming
complexes
greatly
enhance
their
combined
effectiveness.
Previous
studies
have
shown
both
crude
and
one
its
components,
obtustatin,
can
reduce
sarcoma
tumors
by
50%
30%,
respectively.
Obtustatin,
a
member
the
short
disintegrin
family,
inhibits
angiogenic
activity
α1β1
integrin,
adhesive
receptor
collagen
IV.
However,
mechanisms
greater
efficacy
compared
isolated
remain
unclear.
To
investigate
this,
we
propose
an
experimental
explore
certain
low-molecular-weight
MLO
venom.
Our
in
vitro
tests
on
fibrosarcoma
(HT-1080)
cells
using
six
fractions
revealed
cytotoxic
fractions,
which,
through
mass
spectrometry,
were
identified
as
containing
classes
such
dimeric
disintegrins,
acidic
phospholipase
A2,
serine
proteinases.
Notably,
these
exhibited
minimal
toxicity
human
dermal
microvascular
endothelial
(HDEC)
cells,
suggesting
potential
promising
candidate
for
oncotherapy
future.
Language: Английский
Structural and Functional Differences of Rhodostomin and Echistatin in Integrin Recognition and Biological Implications
Yi‐Chun Chen,
No information about this author
Chun‐Hao Huang,
No information about this author
Yao‐Tsung Chang
No information about this author
et al.
Proteins Structure Function and Bioinformatics,
Journal Year:
2025,
Volume and Issue:
unknown
Published: May 2, 2025
ABSTRACT
Rhodostomin
(Rho)
and
Echistatin
(Ech)
are
RGD‐containing
disintegrins
with
different
sizes,
disulfide
bond
patterns,
amino
acid
sequences
in
their
RGD
loops
C‐termini.
Cell
adhesion
analyzes
showed
that
Rho
exhibited
a
5.2‐,
18.9‐,
2.2‐,
1.7‐fold
lower
inhibitory
activity
against
integrins
αvβ3,
α5β1,
αIIbβ3,
αvβ5
comparison
those
of
Ech.
In
contrast,
an
8.8‐fold
higher
than
Ech
inhibiting
integrin
αvβ6.
The
swapping
Ech's
loop
C‐terminal
into
cannot
increase
its
integrins'
activities.
Interestingly,
the
mutation
Rho's
PRGDMP
sequence
YH
caused
8.2‐fold
Structural
they
have
similar
conformations
regions.
Molecular
docking
found
not
only
but
also
region
interacted
integrins,
showing
is
important
for
recognition.
αvβ6
H68
residue
D129
β6.
α5β1
H44
Q191
β1.
78.5‐
10.9‐fold
activities
HUVEC
proliferation
A375
melanoma
cell
migration
Rho.
These
findings
demonstrate
pattern,
loop,
may
cause
functional
differences.
structural
differences
between
support
potential
as
scaffolds
to
design
drugs
targeting
respective
integrins.
Language: Английский
Sea Anemone Heteractis magnifica Toxin Hct-S3 Suppresses the Migration of Solid Ehrlich Adenocarcinoma Cells Inoculated into BALB/C Mice
Biochemistry (Moscow) Supplement Series B Biomedical Chemistry,
Journal Year:
2024,
Volume and Issue:
18(S1), P. S99 - S105
Published: Dec. 1, 2024
Language: Английский
Bicistronic Vector Expression of Recombinant Jararhagin-C and Its Effects on Endothelial Cells
Toxins,
Journal Year:
2024,
Volume and Issue:
16(12), P. 524 - 524
Published: Dec. 3, 2024
Jararhagin-C
(JarC)
is
a
protein
from
the
venom
of
Bothrops
jararaca
consisting
disintegrin-like
and
cysteine-rich
domains.
JarC
shows
modulating
effect
on
angiogenesis
remodeling
extracellular
matrix
constituents,
improving
wound
healing
in
mouse
experimental
model.
purified
crude
venom,
yield
less
than
1%.
The
aim
this
work
was
to
obtain
recombinant
form
test
its
biological
activity.
For
purpose,
bicistronic
vector
pSUMOUlp1
used.
This
allowed
expression
toxin
(rJarC)
fusion
with
small
ubiquitin-related
modifier
(SUMO)
as
well
SUMO
protease
Ulp1.
After
expression,
able
efficiently
remove
rJarC
inside
bacteria.
free
at
expected
molecular
mass
recognized
by
polyclonal
anti-jararhagin
antibodies.
In
terms
activity,
both
native
forms
showed
no
toxicity
HUVEC
cell
line
CRL1730
were
effective
migration
activity
vitro
These
results
demonstrate
successful
production
preservation
which
may
facilitate
further
investigations
into
therapeutic
potential
snake
venom-derived
protein.
Language: Английский