Growth Factor Analogs

a technology of growth factor and analogs, which is applied in the direction of peptides/protein ingredients, peptides, immunoglobulins, etc., can solve the problems of high preparation cost, general difficulty in preparation, and none of these or other known heparin-binding growth factor analogs provide the advantages, so as to stimulate the signaling of growth factor receptors and stimulate cell proliferation.

Inactive Publication Date: 2009-06-04
BIOSURFACE ENG TECH
View PDF53 Cites 23 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0035]Binding of the heparin-binding growth factor analog of formula II to a heparin-binding growth factor receptor can initiate a signal by the heparin-binding growth factor receptor or alternatively can block signaling by the heparin-binding growth factor receptor.
[0043]The invention further provides a method for stimulating growth factor receptor signaling in a cell, the method including contacting the cell with an effective amount of a heparin-binding growth factor analog of formula II. The signaling can stimulate proliferation of the cell, which cell may be part of a mammal.

Problems solved by technology

HBGFs useful in prevention or therapy of a wide range of diseases and disorders may be purified from natural sources or produced by recombinant DNA methods, however, such preparations are expensive and generally difficult to prepare.
However, none of these or other known heparin-binding growth factor analogs provide the advantages described herein below.

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
  • Growth Factor Analogs
  • Growth Factor Analogs
  • Growth Factor Analogs

Examples

Experimental program
Comparison scheme
Effect test

example 1

[0153]The synthetic HBGF analog, PBA1-1, was synthesized by standard solid phase peptide synthesis methods. PBA1-1 has a structure according to formula II, in which the amino acid sequences of the X region is WVLFNANTRDILRRSI (SEQ ID NO:39) (considering the sequence in the conventional N C orientation, notwithstanding that it is branched sequence). Each of the two X region peptides of SEQ ID NO:39 are covalently linked by amide bonds to a lysine residue, the lysine residues corresponding to J1 and J2. The J2 Lys is bound by means of a covalent peptide bond to one terminus of a tripeptide formed from two glycine amino acid residues and corresponding to J3.

[0154]The peptides were assembled stepwise by solid-phase synthesis on a substituted benzhydrylamine resin, using Fmoc chemistry for temporary protection of amino groups in the repetitive cycles. Branching of the chain was accomplished by stepwise growth of identical chains from the side-chain amino groups of consecutive lysyl resid...

example 2

[0157]A synthetic HBGF analog, PBA2-1, was synthesized by standard solid phase peptide synthesis methods. The amino acid sequence KKRVIEIKRV (SEQ ID NO:40) (again considering the sequence in the conventional N→C orientation, notwithstanding that it is branched sequence) corresponds to the two X region peptides.

[0158]The crude preparation was purified as described above in Example 1. The resulting analog had the following structure:

NH2-K-K-G-G-amide    V V    R R    K K    I I    E E    I I    V V    R R    K K    K K

example 3

[0159]A synthetic HBGF analog is synthesized by standard solid phase peptide synthesis methods. The amino acid sequence ISRRLIDRTNANFLVW (SEQ ID NO:41) (again considering the sequence in the conventional N→C orientation, notwithstanding that it is branched sequence) corresponds to the two X region peptides, and is a portion of the known platelet-derived growth factor beta isoform 2 sequence.

[0160]The crude preparation is purified as described above in Example 1. The resulting analog has the following structure:

NH2-K-K-G-G-amide    W W    V V    L L    F F    N N    A A    N N    T T    R R    D D    I I    L L    R R    R R    S S    I I

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
solubleaaaaaaaaaa
affinityaaaaaaaaaa
acidaaaaaaaaaa
Login to view more

Abstract

The invention provides synthetic heparin-binding growth factor analogs of formulas I or II as given in the specification, having two peptide chains branched from a dipeptide branch moiety composed of at least one and preferably two trifunctional amino acid residues, which peptide chain or chains bind a heparin-binding growth factor receptor. The synthetic heparin-binding growth factor analogs are useful as pharmaceutical agents, soluble biologics or as surface coatings for medical devices.

Description

CROSS-REFERENCE TO RELATED APPLICATION[0001]This application is a divisional application of U.S. patent application Ser. No. 11 / 051,292, entitled “Growth Factor Analogs,” filed on Feb. 4, 2005. This application also claims the benefit of the filing of U.S. Provisional Patent Application Ser. No. 60 / 542,272, entitled “Growth Factor Analogs”, filed on Feb. 4, 2004, and the specification thereof is incorporated herein by reference.BACKGROUND OF THE INVENTION[0002]1. Field of the Invention (Technical Field)[0003]The invention relates to the field of synthetic peptides and analogs of heparin-binding growth factors. The invention further relates to the clinical uses of such analogs as soluble drugs and as coatings for medical devices.[0004]2. Description of Related Art[0005]Note that the following discussion refers to a number of publications by author(s) and year of publication, and that due to recent publication dates certain publications are not to be considered as prior art vis-a-vis ...

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): C07K7/08C07K7/06
CPCA61K38/00C07K14/50C07K14/475
Inventor ZAMORA, PAUL O.PENA, LOUIS A.LIN, XINHUA
Owner BIOSURFACE ENG TECH
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

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

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap