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
Snake Venom Compounds: A New Frontier in the Battle Against Antibiotic-Resistant Infections
Toxins,
Journal Year:
2025,
Volume and Issue:
17(5), P. 221 - 221
Published: May 1, 2025
The
occurrence
of
antibiotic-resistant
bacteria
is
a
serious
global
health
issue,
and
it
emphasizes
the
need
for
novel
antimicrobial
agents.
This
review
explores
potential
snake
venom
as
another
alternative
strategy
against
resistance.
Snake
venoms
are
complex
combinations
bioactive
peptides
proteins,
including
metalloproteases
(MPs),
serine
proteases
(SPs),
phospholipase
A2
(PLA2)
enzymes,
three-finger
toxins
(3FTXs),
cysteine-rich
secretory
proteins
(CRISPs),
L-amino
acid
oxidases
(LAAOs),
(AMPs).
antibacterial
products
possess
wide-spectrum
activity
resistant
microbes
via
diverse
mechanisms
such
cell
membrane
disruption,
enzymatic
hydrolysis
microbial
structures,
generation
oxidative
stress,
inhibition
biofilms,
immunomodulation.
Strong
reported
by
most
studies,
but
these
mostly
restricted
to
in
vitro
testing
with
low
translational
use.
Although
preliminary
insights
into
molecular
targets
physiological
effects
exist,
further
studies
needed
clarify
long-term
safety
therapeutic
potential.
Special
attention
given
venom-derived
extracellular
vesicles
(SVEVs),
which
enhance
protecting
them
from
degradation,
improving
bioavailability,
facilitating
targeted
delivery.
Furthermore,
innovative
delivery
strategies
PEGylation,
liposomes,
hydrogels,
microneedle
patches,
biopolymer
films,
nanoparticles
discussed
their
role
reducing
systemic
toxicity
enhancing
efficacy.
rational
modification
expands
utility
pharmacokinetics
minimizing
off-target
effects.
Together,
approaches
highlight
venom-based
therapies
next-generation
antimicrobials
fight
infections.
By
outlining
challenges
directions,
this
positions
an
overlooked
fertile
resource
battle
antibiotic
Language: Английский
Discovery and Characterisation of Novel Poly-Histidine-Poly-Glycine Peptides as Matrix Metalloproteinase Inhibitors
Biomolecules,
Journal Year:
2025,
Volume and Issue:
15(5), P. 706 - 706
Published: May 12, 2025
For
the
first
time,
two
poly-histidine-poly-glycine
peptides
(pHpG-H5
and
pHpG-H7)
were
identified
as
promising
candidates
for
matrix
metalloproteinase
inhibitors.
cDNAs
encoding
pHpG-H5
pHpG-H7
isolated
from
Atheris
squamigera
cDNA
library
constructed
using
oligo(dT)-primed
reverse
transcription.
Deduced
sequences
of
pHpG
systematically
organised
utilised
templates
synthesising
chemical
replicates.
All
synthetic
exhibited
inhibitory
effects
on
human
metalloproteinase-1
(MMP-1).
Spectroscopic
analyses
molecular
modelling
demonstrated
that
disrupt
zinc
ion
coordination
within
central
catalytic
domain
MMP-1,
thereby
inhibiting
its
enzymatic
activity.
As
a
novel
peptide
inhibitor
metalloproteinase,
modulates
multiple
biological
processes,
such
cell
migration
angiogenesis,
suggesting
significant
therapeutic
potential.
Language: Английский