Science: There is a problem with the neural circuit, which is repaired by synthesized proteins.

The human brain contains trillions of synapses in a vast network of neurons.
synhapus remodeling is critical to ensuring effective reception and integration of external stimuli and the storage and retrieval of information.
Synapses are constructed and reshaped by synactal tissue proteins, a process that disrupts the balance of excitability and inhibitory neurotransition, leading to mental and neurological disorders such as autism spectrum disorders, epilepsy, schizophrenia, and Alzheimer's disease.
, it is important to study how neurons regulate the repair of neuron circuits.
recently, researchers from Keruji University, Oxford University and the German Center for Neurodegenerative Diseases published a research paper in Science entitled Asynthetic synaptic solution proteins glutamatergic neuronal circuits, which synthesizes a new type of synaptic tissue protein that can effectively repair or reshape neuronal circuits.
synapses are the basic structure and functional units in the neural circuit.
as a bridge for neuron communication, synapses are highly dynamic, and their remodeling is essential for all aspects of brain physiology.
, abnormal processes can cause an imbalance between excitable and inhibitory signals.
, synapse formation is regulated by synactal tissue proteins.
, extracellular stent proteins (EPs) such as cer cerebral protein 1 (Cbln1) and neuron pentapeptide toxin 1 (NP1) can quickly induce synapse differentiation by binding pre- and/or post-synapse cell surface proteins during synhaptic clearances.
the researchers hypothesized that synthetic molecules combined with the structural characteristics of Cbln1 and NP1 could be used to reverse the absence of excitable synapses and promote structural and functional recovery of damaged neuron circuits.
the structural design and application of NP1 to collect the ABPA subtype ion glutamate recessor (AMPAR) after the synapse, responsible for excitable nerve transfer through its positive pentaprotein domain.
, NP1 does not induce pre-synapse differentiation in the body.
Cbln1 interacts with the cell-adhesive molecular neurotoxin (Nrx) through its N-side polystructum domain, thus facilitating pre-synapse differentiation, but without binding to AMPAR.
the researchers have synthesized a soluble hexamer ES (CPTX) that contains the polysorbic domain of Cbln1 and the pentagonocycline domain of NP1.
, CPTX selectively combines pre-synapse Nrx with Namore affinity.
the structural design and physiological characteristics of CPTX, the researchers found that CPTX regulates bidirectional synapses as well as excitable synapses before and after synapses.
in the body, CPTX increased the number of functional excitable synapses and improved gait in mice that would be co-dysfunctional.
addition, injecting CPTX into the sea mass of mice with Alzheimer's disease model restores the number of synapses, promotes excited synapse delivery, and improves sea horse dependent learning.
, in mouse models with spinal cord injuries, a single injection of CPTX into the damaged tissue recombines the excitability circuit and restores movement.
CPTX restores PF-PC synapses and motion coordination in mice that the GluD2 gene knocks out, and the researchers synthesized a new synact tissue protein, CPTX, that interacts with pre-synhap neurotoxins and post-synhapamp AMPA ion glutamates and induces the formation of excitable synapses in the body and beyond.
CPTX restored synapse function, motion coordination and memory in mouse models with co-brain disorders, Alzheimer's disease, and spinal cord injuries.
, CPTX, as a prototype of a structurally oriented biologic agent, can effectively repair or reshape neuron circuits and is expected to be used to treat mental and neurological disorders.
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