Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Random peptides that bind to gastro-intestinal tract (GIT) transport receptors and related methods

a technology of git and transport receptor, which is applied in the direction of peptide/protein ingredients, peptide sources, metabolic disorders, etc., can solve the problems of inability to carry out intravenous drug administration, risk of adverse effects, and risk of infection at the site of repeated injections, so as to facilitate its absorption into the systemic system

Inactive Publication Date: 2007-01-11
CYTOGEN CORP
View PDF0 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0031] The proteins of the invention have use in facilitating transport of active agents from the lumenal side of the GIT into the systemic blood system, and / or in targeting active agents to the GIT. Thus, for example, by binding (covalently or noncovalently) a protein of the invention to an orally administered drug, the drug can be targeted to specific receptor sites or transport pathways which are known to operate in the human gastrointestinal tract, thus facilitating its absorption into the systemic system.

Problems solved by technology

Intravenous drug administration suffers from numerous limitations, including (i) the risk of adverse effects resulting from rapid accumulation of high concentrations of drug, (ii) repeated injections which can cause patient discomfort; and (iii) the risk of infection at the site of repeated injections.
Subcutaneous injection is not generally suitable for delivering large volumes or for irritating substances.
Whereas oral administration is generally more convenient, it is limited where the therapeutic agent is not efficiently absorbed by the gastrointestinal tract.
Many anticancer drugs are toxic to the body as well as to malignant cells.
However, because whole cells, rather than intact tissue or polarized cell cultures, are used for screening phage display libraries, this procedure does not provide information regarding sequences whose primary function includes affecting transport across polarized cell layers.

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
  • Random peptides that bind to gastro-intestinal tract (GIT) transport receptors and related methods
  • Random peptides that bind to gastro-intestinal tract (GIT) transport receptors and related methods
  • Random peptides that bind to gastro-intestinal tract (GIT) transport receptors and related methods

Examples

Experimental program
Comparison scheme
Effect test

example 1

Peptide Added at the Final Washing Stage

[0338] Product: Bovine Insulin loaded nanoparticles

[0339] Aim: To prepare a 2 g batch of insulin loaded nanoparticles at a theoretical loading of 50 mg / g and with the peptide ZElan018 added.

Formulation DetailsRG504H (Lot no. 250583)2.0gAcetone45mlEthanol:5mlPVA (aq. 5% w / v)400mlBovine Insulin (Lot no. 86H0674)100mgPeptide: PAX2 (ZElan018)10 mg / 50 mldH2O

Experimental details:

[0340] The 5% w / v PVA solution was prepared by heating water until near boiling point, adding PVA and stirring until cool. The organic phase was prepared by adding acetone, 45 ml, and ethanol, 5 ml, together. The polymer solution was prepared by adding RG504H, 2 g, to the organic phase and stirring until dissolved. The IKA™ reactor vessel was set up, all seals greased and the temperature was set at 25° C. The PVA solution, 400 ml, was added into the reactor vessel and stirred at 400 rpm.

[0341] Bovine insulin, 100 mg, was added into the stirring PVA solution. Using cle...

example 2

Peptide Added at the Beginning of Manufacture

[0345] Product: Bovine Insulin loaded nanoparticles

[0346] Aim: To prepare a 2 g batch of insulin loaded nanoparticles at a theoretical loading of 50 mg / g and with the peptide ZElan018 added at the beginning of manufacture.

Formulation DetailsRG504H (Lot no. 250583)2.0gAcetone45mlEthanol:5mlPVA(aq. 5% w / v)400mlBovine Insulin (Lot no. 65H0640)100mgPeptide: PAX2 (ZElan018ii)10mg

Experimental Details:

[0347] The 5% w / v PVA solution was prepared by heating water until near boiling point, adding PVA and stirring until cool. The organic phase was prepared by adding acetone, 45 ml, and ethanol, 5 ml, together. The polymer solution was prepared by adding RG504H (polyactide-co-glycolide, Boehringer Ingelheim), 2 g, to the organic phase prepared in step above and stirring until dissolved. The IKA™ reactor vessel was set up, all seals greased and the temperature was set at 25° C. The PVA solution, 400 ml, was added into the reactor vessel and stir...

example 3

Peptide Added 1 Hour before Centrifugation

[0351] Product: Bovine Insulin loaded nanoparticles

[0352] Aim: To prepare a 1 g batch of insulin loaded nanoparticles at a theoretical loading of 50 mg / g and with the peptide ZElan018 added 1 hour before centrifugation.

Formulation DetailsRG504H (Lot no. 250583)1.0gAcetone22.5mlEthanol:2.5mlPVA(aq. 5% w / v)200mlBovine Insulin (Lot no. 65H0640)50mgPeptide: PAX2 (ZElan018)5mg

Experimental Details:

[0353] The 5% w / v PVA solution was prepared by heating water until near boiling point, adding PVA and stirring until cool. The organic phase was prepared by adding acetone, 22.5 ml, and ethanol, 2.5 ml, together. The polymer solution was prepared by adding RG504H, 1 g, to the organic phase prepared above and stirring until dissolved. The IKA™ reactor vessel was set up, all seals greased and the temperature was set at 25° C. The PVA solution, 200 ml, was added into the reactor vessel and stirred at 400 rpm.

[0354] Bovine insulin, 50 mg, was added in...

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

PropertyMeasurementUnit
total volumeaaaaaaaaaa
sizeaaaaaaaaaa
nucleic acidaaaaaaaaaa
Login to View More

Abstract

This invention relates to proteins (e.g., peptides) that are capable of facilitating transport of an active agent through a human or animal gastro-intestinal tissue, and derivatives (e.g., fragments) and analogs thereof, and nucleotide sequences coding for said proteins and derivatives. The proteins of the invention have use in facilitating transport of active agents from the lumenal side of the GIT into the systemic blood system, and / or in targeting active agents to the GIT. Thus, for example, by binding (covalently or noncovalently) a protein of the invention to an orally administered drug, the drug can be targeted to specific receptor sites or transport pathways which are known to operate in the human gastrointestinal tract, thus facilitating its absorption into the systemic system.

Description

[0001] This application claims priority to U.S. provisional application Ser. No. 60 / 046,595 filed May 15, 1997, which is incorporated by reference herein in its entirety.1. INTRODUCTION [0002] The present invention relates generally to random peptides capable of specific binding to gastro-intestinal tract (GIT) transport receptors. In particular, this invention relates to peptide sequences and motifs, as well as derivatives thereof, which enhance drug delivery and transport through tissue, such as epithelial cells lining the lumenal side of the gastro-intestinal tract (GIT). Production of peptides, derivatives and antibodies is also provided. The invention further relates to pharmaceutical compositions, formulations and related methods. 2. BACKGROUND OF THE INVENTION [0003] 2.1. Peptide Libraries [0004] There have been two different approaches to the construction of random peptide libraries. According to one approach, peptides have been chemically synthesized in vitro in several for...

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(United States)
IPC IPC(8): A61K38/17C07K14/47
CPCA61K38/28A61K47/48176A61K47/48915A61K47/48215A61K47/48238A61K47/482A61K47/58A61K47/593A61K47/60A61K47/62A61K47/6937
Inventor ALVAREZ, VERNON L.O'MAHONY, DANIEL J.LAMBKIN, IMELDA J.PATTERSON, CATHERINE A.SINGLETON, JUDITHBELINKA, BENJAMIN A. JR.CARTER, JOHN M.CAGNEY, GERARD M.
Owner CYTOGEN CORP
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

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

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com