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

Peptides for use in promoting transport of glucose

A glucose transport and natural technology, applied in the direction of peptides, peptide sources, plant peptides, etc., can solve the problems of insulin influence, resistance, and side effects

Inactive Publication Date: 2018-06-08
NURITAS LTD
View PDF21 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, insulin has a range of functions that affect other parts of the body, leading to side effects and insulin resistance

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
  • Peptides for use in promoting transport of glucose
  • Peptides for use in promoting transport of glucose
  • Peptides for use in promoting transport of glucose

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0234]Measuring glucose uptake using 2-deoxyglucose (2-DG) is a widely accepted method for studying glucose uptake in skeletal muscle cells. 2-DG is taken up by glucose transporters and metabolized to 2-DG-6-phosphate (2-DG6P). The amount of accumulated non-metabolized 2-DG6P is proportional to the glucose uptake by cells.

[0235] method:

[0236] 1. Human skeletal muscle myoblasts (Sigma 150-05a) were seeded in skeletal muscle differentiation medium in a 96-well plate at 10,000 cells / well, and differentiated for 72 hours before the experiment.

[0237] 2. Serum starvation of differentiated cells for 24 hours prior to stimulation with insulin or synthetic peptides. After starvation, the serum-free medium was removed, the cells were rinsed with phosphate-buffered saline (PBS), and the medium was replaced with 100 μl of Krebs-Ringer-Phosphate-HEPES (KRPH) and incubated 1 hour.

[0238] 3. Cells were then stimulated with 100 nM insulin for 30 minutes or with 5 μg / mL, 0.5 μg / ...

Embodiment 2

[0243] research description

[0244] Skeletal muscle is the major site of glucose disposal (80%) under insulin-stimulated or postprandial conditions. Under these conditions, glucose transport into skeletal muscle is facilitated primarily by the insulin-responsive glucose transporter GLUT4, which translocates to the cell surface upon insulin or contractile stimulation.

[0245] We determined the effect of six synthetic peptides (SP1-6) and four peptide compositions on GLUT4 translocation in vitro using the L6 rat skeletal muscle cell line. A clone of an overexpressed L6 cell line containing GLUT4 tagged with a c-myc epitope (courtesy of Prof. Amira Klip, Hospital for SickChildren, Toronto) was used to study each Effect of efficacy of synthetic peptides and peptide compositions on GLUT4 translocation in a dose-response design.

[0246] SP2 [SEQ ID7] is a glucose transport promoting fragment of pea protein P13918, while peptides SP1 and SP3-SP6 are comparative peptides.

[024...

Embodiment 3

[0270] Antihyperglycemic properties of peptide compositions I_2_BE and E_1_BE in db / db mice

[0271] preparation

[0272] I_2_BE or E_1_BE is administered as a solution or suspension in purified water. According to the stability data, the 10 mg / ml preparation of the test item in purified water is stable for 10 hours at +2-+8°C in the dark. Therefore, test item formulations were kept at +2-+8°C in the dark and used within 10 hours of preparation. Relevant aspects of the formulation and the maximum storage time are detailed below.

[0273] Material

[0274] Species: mouse.

[0275] Breed: BKS.Cg-Dock7m+ / +Leprdb / J (db / db diabetic mouse) (souche JAXTM mouse strain).

[0276] Choice of species: The mouse was chosen because it is considered a predictor of drug pharmacology in humans and regulatory agencies recognize that this species is suitable for pharmacodynamic studies.

[0277] Age: 8-9 weeks on the day of randomization.

[0278] Body Weight: On the day of randomization,...

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

A natural glucose transport promoting peptide comprising a glucose transport promoting fragment of a protein selected from SEQUENCE ID NO's: 1 to 6, and a composition comprising a plurality of glucosetransport promoting peptides, is described. Also disclosed is the use of the peptides and compositions in improving muscle status in a mammal, especially promoting recovery of muscle following exercise or enhancing physical performance.

Description

Background technique [0001] Nearly 38% of the human body is made up of skeletal muscle. The basic function of this type of muscle is to generate force and allow movement and movement. It is also a key player in global protein metabolism and a major reservoir of amino acids (Wolfe R.R. 2006). Muscle also plays a vital role in the regulation of blood sugar levels. In fact, 80% of the glucose consumed is taken up by skeletal muscle and then converted to glycogen (a form of energy storage). All of this makes skeletal muscle maintenance vital to overall health and well-being. [0002] There are many reasons why muscle health is crucial. First, muscle loss leads to immobility, and as the population ages, this becomes a huge problem. Second, active individuals want to maintain their muscle mass and stay athletic, competitive, and healthy. Finally, low muscle-glucose absorption leads to high blood sugar levels, which can lead to serious conditions such as pre-diabetes and eventu...

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): A61K38/04A61P21/00C07K7/04C07K14/415A61K8/64
CPCC07K14/415C07K7/06C07K7/08A23L33/18A23L2/38A61K38/08A61K38/10A61K38/168A61P3/10A61P5/50A61P21/00A23V2002/00A23V2200/328A23V2250/548A61K38/00A61K8/9789A61K8/9794A61P3/00A61K9/14
Inventor N·哈尔迪C·洛佩兹
Owner NURITAS LTD
Features
  • R&D
  • Intellectual Property
  • Life Sciences
  • Materials
  • Tech Scout
Why Patsnap Eureka
  • Unparalleled Data Quality
  • Higher Quality Content
  • 60% Fewer Hallucinations
Social media
Patsnap Eureka Blog
Learn More

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2025 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com