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Use of repeat sequence protein polymers in personal care compositions

a repeat sequence protein and composition technology, applied in the field of personal care compositions, can solve the problems of reducing the affinity of the protein for the negatively charged skin and hair, forming tight, hard fibers that are not suitable for film formation, and not showing all desired characteristics when used in personal care products, so as to improve skin tone and increase the viability of skin fibroblasts

Inactive Publication Date: 2005-06-30
GENENCOR INT INC
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0011] In alternative embodiments, the present invention provides bioactive protein polymers, which show efficacy in cell viability improvement, elastin biosynthesis, collagen biosynthesis, and inhibition of skin metelloprotease MMP1 activity.
[0013] In some most preferred embodiments, the present invention provides personal care compositions comprising an effective amount of a repeat sequence protein polymer or a fragment thereof, and a physiologically acceptable carrier or excipient, wherein the repeat sequence protein polymer provides improved skin tone.
[0014] In some particularly preferred embodiments, the present invention provides personal care compositions comprising an effective amount of a repeat sequence protein polymer or a fragment thereof, and a physiologically acceptable carrier or excipient, wherein the repeat sequence protein polymer increases skin fibroblast viability.
[0027] In some particularly preferred embodiments, the present invention provides personal care compositions comprising an effective amount of a repeat sequence protein polymer or a fragment thereof, with the balance of the composition comprising one or more compounds from the group of carriers, excipients, liposomes, active ingredients, biological or botanical products, humectants, emollients, surfactants, thickening agents, silicone components, organic sunscreens, preservatives, neutralizing agents, perfumes or pigments, and wherein the repeat sequence protein polymer or fragment thereof improves or enhances skin tone.

Problems solved by technology

However, such proteins may not exhibit all desired characteristics when used in personal care products.
For example, natural silk proteins may impart durability but may also form tight, hard fibers that are not suitable for film formation.
Also, many natural proteins have a low isoelectric point, which reduces the affinity of the protein for the negatively charged skin and hair.
Additionally, when more than one protein is needed to impart all desired characteristics to a given formulation, the necessity of using more than one protein may increase the cost and production time for a given personal care product.
Furthermore, proteins generally have poor solubility due to high molecular weight and hydrophobicity.
However, in most embodiments, hydrolyzed proteins have not been found to be as effective as the intact proteins, as the beneficial effects of the self-assembly, nanofibrilation and coating properties have not realized.
However, even chemically modified proteins may not have all desired characteristics.
However, digested silk protein is not as effective as water-soluble silk protein (See e.g., WO 04 / 044172).
However, these preparations required harsh solvents to dissolve the silk protein prior to use.

Method used

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  • Use of repeat sequence protein polymers in personal care compositions
  • Use of repeat sequence protein polymers in personal care compositions
  • Use of repeat sequence protein polymers in personal care compositions

Examples

Experimental program
Comparison scheme
Effect test

example 1

Isolation of SELP

[0167] In this Example, experiments conducted to isolate and purify a genetically engineered silk-elastin repeat sequence protein block copolymer (SELP) from E. coli are described. E. coli containing a specific silk-elastin repeat sequence protein copolymer SELP47K (GC2596-26-A) recombinant DNA was obtained from PPTI. The E. coli may be prepared in accordance with the methods described in U.S. Pat. Nos. 5,243,038 and 6,355,776, incorporated herein by reference. The recovery of kilogram quantities of SELP was also demonstrated. The silk-elastin copolymer SELP47K had a general structure of head—[(GAGAGS)2(GVGVP)3GKGVP(GVGP)4(GAGAGS)2]13-tail (SEQ ID NO:19). The copolymer contained 886 amino acids, with 780 amino acids in the repeating sequence unit. The SELP47K had a molecular weight of about 70,000 Daltons, and the pI of the protein is 10.5.

[0168] Monodispersed silk-elastin protein polymer SELP47K was produced for application testing in the following manner. E. col...

example 2

Preparation of Polydispersed SELP47K for Application Testing

[0181] Experiments involving the purification and preparation of the polydispersed SELP47K silk-elastin protein polymer (GC2596-26-B) for application testing are described in this Example. Cell separation from the fermentation broth was done using microfiltration. A cell disruption to make a cell-extract was done using a French-press. The cell extract was separated from the cell-debris using polyethyleneimine and a filter-aid. The cell extract was mixed with ammonium sulfate to 25% saturation to precipitate the silk-elastin protein polymer. The precipitated silk-elastin protein polymer was further purified by dissolving it in water and reprecipitating it with ammonium sulfate.

[0182] In order to prepare a polydispersed silk-elastin protein polymer, the precipitated silk-elastin protein polymer was again dissolved in water and mixed with a trace amount of protease (BPN′Y217L) (Genencor International). The protease was then ...

example 3

Cleavage of Monodispersed SELP47K

[0184] This Example describes the methods used to cleave monodispersed SELP47K to its monomeric unit. The purification and formation of monomeric unit of SELP47K (4920 kDA molecular weight) (GC2596-26-C) was carried out using monodispersed material of SELP47K produced as in Example 1. The monodispersed SELP47K was dissolved in water and was treated with endopeptidase lysC protease (Sigma) specific for cleaving protein at lysine residue for 30 minutes at room temperature. The lysC protease was then inactivated and destroyed by acid treatment. The monomeric unit of SELP47K was then ultra-filtered until protein polymer solution conductivity reached 50 μS / m2. The monomeric unit of SELP47K solution was then lyophilized to get the solid material and stored at −70 C prior to application testing.

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Abstract

The present invention provides personal care compositions, and more particularly, personal care compositions comprising a bioactively effective amount of a repeat sequence protein polymer. In some particularly preferred embodiments, the present invention provides personal care compositions comprising an effective amount of at least one fragment of a repeat sequence protein polymer having bioactivity.

Description

RELATED APPLICATIONS [0001] This application is a Continuation-in-Part of U.S. patent application Ser. No. 10 / 800,179, filed Mar. 12, 2004, which claims priority under 35 U.S.C. §119 of U.S. Provisional Application Ser. No. 60 / 454,077 filed Mar. 12, 2003.FIELD OF THE INVENTION [0002] The present invention provides personal care compositions, and more particularly, personal care compositions comprising a bioactively effective amount of a repeat sequence protein polymer. In some particularly preferred embodiments, the present invention provides personal care compositions comprising an effective amount of at least one fragment of a repeat sequence protein polymer having bioactivity. BACKGROUND OF THE INVENTION [0003] Proteins have been widely used as ingredients in personal care products, pigment coating, and in bandages to promote wound healing. Use of silk proteins to perform a variety of functions and to impart desired characteristics to product formulations has been described (See ...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): A61K8/64A61Q1/02A61Q1/04A61Q1/06A61Q1/10A61Q1/12A61Q3/00A61Q3/02A61Q5/00A61Q5/02A61Q5/12A61Q17/04A61Q19/00A61Q19/10
CPCA61K8/0212A61Q19/10A61K8/64A61K38/1709A61K2800/28A61Q1/02A61Q1/04A61Q1/06A61Q1/10A61Q1/12A61Q3/00A61Q3/02A61Q5/006A61Q5/02A61Q5/12A61Q17/04A61Q19/00A61Q19/001A61Q19/002A61K8/0229A61P31/04
Inventor KUMAR, MANOJ
Owner GENENCOR INT INC
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