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Immunogenic compositions and methods of use

A multi-layer film and adjacent layer technology, applied in the direction of peptides, specific peptides, chemical instruments and methods, etc., can solve the problems of scaling up cost, lack of biocompatibility, etc.

Inactive Publication Date: 2009-02-11
路易斯安那科技大学研究基金会
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, there are difficulties in using proteins for this purpose
These include limited control over the multilayer structure (since protein surfaces are highly irregular and proteins generally do not adsorb to regularly structured surfaces), limitations on pH (due to pH-dependent protein solubility and structural stability), Lack of biocompatibility when exogenous proteins are used, and the cost of scale-up production (if the gene has not been cloned); unless the protein is identical in a readily available source (e.g., cows), the protein will Must be obtained from the organism for which it is intended to be used, making the cost of large-scale production of the protein prohibitive

Method used

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  • Immunogenic compositions and methods of use
  • Immunogenic compositions and methods of use
  • Immunogenic compositions and methods of use

Examples

Experimental program
Comparison scheme
Effect test

example 2

[0205] Example 2—Experiments Involving Redesigned Polypeptides Containing Cysteine

[0206] b. Peptides

[0207] The peptides used are:

[0208] Tyr Lys Cys Lys Gly Lys Val Lys Val Lys Cys Lys Gly Lys

[0209] Val Lys Val Lys Cys Lys Gly Lys Val Lys Val Lys Cys Lys

[0210] Gly Lys Val Lys

[0211] (SEQ ID NO: 5)

[0212] Tyr Glu Cys Glu Gly Glu Val Glu Val Glu Cys Glu Gly Glu

[0213] Val Glu Val Glu Cys Glu Gly Glu Val Glu Val Glu Cys Glu

[0214] Gly Glu Val Glu

[0215] (SEQ ID NO: 6)

[0216] Unlike the other peptides used in the experiments described here, these two were not designed using human genome information; they were designed for the sole purpose of evaluating the role of disulfide bond formation in peptide film stabilization. The net charge strength of SEQ ID NO: 5 at pH 7 is 16 / 32 (0.5); while the net charge strength of SEQ ID NO: 6 at pH 7 is 16 / 32 (0.5). In both cases, the net charge strength at pH 7 was greater than or equal to about 1 / 2 the total l...

example 3

[0227] Example 3—Experiments Involving Cysteine-Containing Designer Polypeptides

[0228] f.Material

[0229] The essential elements of the experiment were a quartz crystal microbalance apparatus; a silver-coated resonator (9 MHz resonant frequency); a negative 48-residue peptide (LN3) (SEQ ID NO: 4); and the following sequence termed "SP5" The positive 48-residue peptide:

[0230] Tyr Lys Gly Lys Lys Ser Cys His Gly Lys Gly Lys Lys Ser Cys

[0231] His Gly Lys Gly Lys Lys Ser Cys His Gly Lys Gly Lys Lys Ser

[0232] Cys His

[0233] (SEQ ID NO: 7)

[0234] Like the other designed peptides discussed in section (D)(1) above, SP5 was designed using the method described in (D)(1) above to analyze the amino acid sequence of the human blood protein lactoferrin (gi|4505043). ELBL buffer was 10 mM Tris, pH 7.4, 10 mM NaCl and 1 mM DTT. The lysis buffer was 10 mM KCl, pH2. 2 mL peptide solutions of SP5 and LN3 were prepared by adding 4 mg of each peptide to 2 mL of the above bu...

example 4

[0253] Example 4. A polypeptide film comprising an RGD functional domain, wherein the linear charge density intensity of each residue is about 0.75.

[0254] In one embodiment, the functional domain of the composite polypeptide is an RGD sequence, wherein the charge density of the composite peptide is about 0.75. The RGD sequence binds the extracellular portion of the receptor protein integrin, thereby promoting cell adhesion. The sample peptides were designed as follows:

[0255] KKKAKKKGKKKAKKKGRGDKKKAKKKGKKKAKKKY (SEQ ID NO: 8)

[0256] EEEAEEEGEEEAEEEGRGDEEEEAEEEGEEEAEEEY (SEQ ID NO: 9)

[0257] In this example, the polypeptide SEQ ID NO: 8 is a positively charged polypeptide with an RGD functional region, a first surface adsorption region KKKAKKKGKKKAKKKG (SEQ ID NO: 10) and a second surface adsorption region KKKAKKKGKKKAKKKY (SEQ ID NO: 11) . The composite peptide had a net charge strength / residue of +26 / 35 or +0.74 at pH 7. The polypeptide SEQ ID NO: 9 is a negativ...

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Abstract

Disclosed herein is a multilayer film comprising two or more layers of polyelectrolytes, wherein adjacent layers comprise oppositely charged polyelectrolytes. A first layer polyelectrolyte comprises a composite polypeptide comprising one or more surface adsorption regions covalently linked to one or more functional regions, wherein the functional regions generate a single polypeptide chain, and the one or more surface adsorption regions have amino acid sequence motifs composed of 5 to 15 amino acid residues. The one or more functional regions comprise 3 to 250 amino acid residues.

Description

[0001] Cross References to Related Applications [0002] This application is a continuation-in-part of US Nonprovisional Patent Application Serial No. 10 / 652,364, filed August 29, 2003, and claims the benefit of US 60 / 729,828, filed October 25, 2005, the contents of which are incorporated herein by reference. technical field [0003] The present invention relates to the formation of ultrathin multilayer films on suitable surfaces by electrostatic lamination self-assembly ("ELBL"). More specifically, the present invention relates to methods for designing polypeptides for nanofabrication of films, coatings and microcapsules by ELBL for biomedical and other applications. Background technique [0004] ELBL is an established technique in which ultrathin films are assembled by altering the adsorption of oppositely charged polyelectrolytes. The process is based on the reversal of the charge on the surface of the film after each layer is deposited. figure 1 A schematic diagram of ...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K17/00
CPCC07K17/00B82Y30/00A61P31/04A61P31/10A61P31/12A61P31/14A61P31/18A61P35/00A61P37/00A61P37/04
Inventor D·T·海尼
Owner 路易斯安那科技大学研究基金会
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