Unlock instant, AI-driven research and patent intelligence for your innovation.

Polypeptide TAT-836-871 with learning and memory capacity improving function and application of polypeptide TAT-836-871

A technology of learning and memory ability and peptides, which can be applied to medical preparations with non-active ingredients, medical preparations containing active ingredients, peptides, etc., and can solve the problems of poorly understood post-translational regulation mechanism of neural cadherin.

Active Publication Date: 2015-10-07
PEKING UNIV
View PDF0 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, the post-translational regulatory mechanisms of neural cadherins are poorly understood

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Polypeptide TAT-836-871 with learning and memory capacity improving function and application of polypeptide TAT-836-871
  • Polypeptide TAT-836-871 with learning and memory capacity improving function and application of polypeptide TAT-836-871
  • Polypeptide TAT-836-871 with learning and memory capacity improving function and application of polypeptide TAT-836-871

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0056] Example 1, Discovery of the polypeptide TAT-836-871

[0057] The amino acid sequence of N-cadherin is shown in sequence 4 of the sequence listing.

[0058] 1. PKD1 binds to amino acids 836-871 of N-cadherin

[0059] In vitro pull-down experiments found that PKD1 binds to the intracellular C-terminus of N-cadherin ( figure 1 Middle A). A series of truncation mutants were constructed for different domains of the intracellular C-terminus of N-cadherin, and it was finally confirmed that PKD1 binds through the amino acid sequence at position 836-871 of N-cadherin ( figure 1 Middle B).

[0060] The amino acid sequence at positions 836-871 of the wild-type N-cadherin protein (hereinafter referred to as N-cadherin or N-cad) was deleted to obtain a mutant of N-cadherin, referred to as N-cadΔ836-871 below.

[0061] 2. N-cadΔ836-871 reduces the localization of N-cadherin on the cell membrane surface

[0062] N-cadherin and N-cadΔ836-871 were overexpressed in N2A cells, and th...

Embodiment 2

[0066] Embodiment 2, the function of TAT-836-871

[0067] 1. Preparation of cortical neurons in gestational day 18 rats

[0068] The rat species used to prepare cortical neurons is SD rat.

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

The invention discloses polypeptide TAT-836-871 with a learning and memory capacity improving function and application of the polypeptide TAT-836-871. The polypeptide TAT-836-871 can be polypeptide a1) with amino acid sequences shown as sequences 1 in sequence tables; the polypeptide TAT-836-871 can be polypeptide a2) with amino acid sequences shown as 10th-45th positions in the sequences 1 in the sequence tables; and 1-10 amino acid residues in the polypeptide a1) and the polypeptide a2) are substituted and / or deleted and / or added to obtain derived polypeptide with the learning and memory capacity improving function. An experiment proves that the learning and memory capacity of a user can be improved by the polypeptide.

Description

technical field [0001] The invention relates to the field of biotechnology, in particular to a polypeptide TAT-836-871 capable of improving learning and memory and its application. Background technique [0002] In the nervous system, synapses are the sites where two neurons connect and transmit information. The formation and function of synapses are critical to neural circuits and higher-level functions of the brain. When the nerve impulse is transmitted to the axon terminal and reaches the pre-synapse, it causes the release of the pre-synaptic transmitter, acts on the post-synaptic receptor, causes the activation of the downstream intracellular signaling pathway, and completes the transmission of signals between neurons. The occurrence, maturation and plasticity of synapses are crucial to the functions of neural circuits and nervous systems. It plays a key role in the pathogenesis of many diseases such as Alzheimer's disease. Therefore, studying the key regulatory mechani...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(China)
IPC IPC(8): C07K19/00C12N15/62A61K38/17A61K47/48A61P25/00
Inventor 王韵岑程李文琪李刚罗丽达
Owner PEKING UNIV