Polypeptide derivative, nanofiber and application of nanofiber

A nanofiber, peptide derivative technology, applied in nanotechnology, nanotechnology, nanotechnology for materials and surface science, etc., can solve the problems of complex synthesis process, unfavorable long-term storage, poor water solubility, etc., and achieve a simple preparation process. , The effect of improving the organization retention rate and low cost

Active Publication Date: 2020-01-03
NANKAI UNIV
View PDF9 Cites 4 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, its polypeptide chain length is 16 peptides, the synthesis process is more complicated and the yield is lower; the most important thing is that the hydrogel formed by its self-assembly is a white opaque gel, which has poor water solubility, and a small amount of precipitation occurs after 3 to 5 days. good for long term storage

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 derivative, nanofiber and application of nanofiber
  • Polypeptide derivative, nanofiber and application of nanofiber
  • Polypeptide derivative, nanofiber and application of nanofiber

Examples

Experimental program
Comparison scheme
Effect test

preparation example Construction

[0060] The polypeptide derivatives are synthesized by the known FMOC-short peptide solid-phase synthesis method. Specifically, the preparation method of the polypeptide derivative includes the following steps:

[0061] (1) The C-terminal of the Fmoc-amino acid is bound to the resin;

[0062] (2) removal of Fmoc protecting group, washing;

[0063] (3) The C-terminal of the next Fmoc-amino acid is coupled to the N-terminal of the amino acid or polypeptide on the resin, and washed;

[0064] (4) Repeat steps (2) to (3) until the last amino acid coupling is completed, remove the Fmoc protecting group, and wash;

[0065] (5) X-OH is coupled and washed with the N-terminal of the polypeptide on the resin;

[0066] (6) The polypeptide derivative is excised from the resin to obtain a crude product;

[0067] (7) Use high performance liquid chromatography to purify the crude product.

[0068] According to the second aspect of the present invention, the present invention provides nano...

preparation Embodiment 1

[0094] Synthesis and Preparation of Peptide Derivative Nap-FFGSSSR and Its Nanofibers

[0095] (1) Solid phase synthesis of Nap-FFGSSSR

[0096] Specific steps are as follows:

[0097] 1) Weigh 0.5mmol 2-Cl-Trt resin in a solid-phase synthesizer, add 10mL of anhydrous dichloromethane (hereinafter referred to as DCM), place on a shaker and shake for 5min to fully swell the 2-Cl-Trt resin ;

[0098] 2) Remove the DCM from the solid-phase synthesizer equipped with 2-Cl-Trt resin with ear washing ball;

[0099] 3) Dissolve 0.75 mmol of Fmoc-Arg in 10 mL of anhydrous DCM, add 0.75 mmol of DIPEA, then transfer to the above-mentioned solid-phase synthesizer, add 0.75 mmol of DIPEA, and react at room temperature for 1 h;

[0100] 4) Sealing: Remove the reaction liquid in the solid-phase synthesizer with ear washing balls, then wash with 10 mL of anhydrous DCM, 1 min each time, and wash 5 times in total. Add the prepared volume ratio of anhydrous DCM: DIPEA: methanol = 17:1:2 solut...

Embodiment 1

[0116] Activity Test of Hydrogel of Peptide Derivative Nap-FFGSSSR at the Cell Level

[0117] (1) Promoting the proliferation of mouse myoblasts (C2C12)

[0118] 1) Raise the temperature of the water bath to 37°C in advance, put the medium, serum, etc. into the water bath to preheat, and at the same time turn on the ultra-clean bench UV lamp for half an hour;

[0119] 2) Take out the frozen mouse myoblast C2C12 cells from the liquid nitrogen tank, quickly place them in a water bath at 37°C to thaw the cells, and then quickly transfer them to an ultra-clean bench for the following operations: transfer the cell-containing solution with a pipette Carefully transfer the liquid container to a centrifuge tube containing the medium, centrifuge for 3 minutes, remove the supernatant, resuspend with DMEM medium containing 10% fetal bovine serum, transfer to a petri dish, and then place it in a 37°C incubator to cultivate;

[0120] 3) Observe the state of the cells the next day. After ...

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 provides a polypeptide derivative, nanofiber and application of the nanofiber. The polypeptide derivative can effectively simulate bioactivity of IGF-1 protein and can be used as a substitute of the IGF-1 protein, the production process is simpler, the yield is higher, and the polypeptide derivative has better storage stability. The sequence of the polypeptide derivative is X-Phe-Phe-Gly-Ser-Ser-Ser-Arg, wherein an end group X is Nap or Npx, Phe is an L configuration or a D configuration simultaneously, and the rest are L configurations. A water mixture of the polypeptide derivative forms the nanofiber by a heating and cooling method. The polypeptide derivative can bind with an IGF-1 protein receptor and can be used for treating muscle atrophy and atherosclerosis.

Description

technical field [0001] The invention relates to a polypeptide derivative, nanofiber and application thereof. Background technique [0002] Insulin-like growth factor I (IGF-1) is a growth hormone that plays a vital role in human development, growth, metabolism and homeostasis, and has been extensively studied clinically and in the field of life science research. [0003] Atherosclerosis is an important cause of cardiovascular diseases such as myocardial infarction, coronary heart disease, hypertension, and stroke, and has become one of the main diseases that endanger human health. According to the latest statistics from the World Health Organization (WHO), the number of deaths from cardiovascular and cerebrovascular diseases accounts for 48% of the total number of non-communicable diseases, which is more than twice the number of deaths from cancer. Low circulating levels of IGF-1 have been associated with increased atherosclerotic complications in most observational studies...

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): C07K14/65C07K1/16C07K1/04B82Y30/00A61K38/08A61K9/00A61K9/06A61P21/00A61P9/10
CPCA61K9/0092A61K9/06A61K38/08A61P9/10A61P21/00B82Y30/00C07K14/65
Inventor 杨志谋王玲商宇娜
Owner NANKAI UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products