Drug – bio-affecting and body treating compositions – Preparations characterized by special physical form – Cosmetic – antiperspirant – dentifrice
Reexamination Certificate
1998-03-09
2002-09-17
Jones, W. Gary (Department: 1655)
Drug, bio-affecting and body treating compositions
Preparations characterized by special physical form
Cosmetic, antiperspirant, dentifrice
C424S059000, C424S069000, C424S078030, C435S069100, C514S002600, C514S012200, C530S350000
Reexamination Certificate
active
06451326
ABSTRACT:
BACKGROUND OF THE INVENTION
The human skin consists of two layers; a superficial layer called the epidermis that is epithelial tissue, and a deeper layer called the dermis that consists essentially of connective tissue. These two layers are bound together to form skin, which varies in thickness from less than about 0.5 mm, to 3 or even 4 millimeters. Exposure of the skin to sun, wind, and other factors leads to skin ageing, i.e., loss of moisture in the epidermal layers of the skin, resulting in loss of elasticity, skin tone and texture as degradation of certain proteins present in the skin takes place.
The connective tissue found in skin is essentially an intricate meshwork of interacting, extracellular molecules that constitute the so-called “extracellular matrix”. The extracellular matrix includes proteins that are secreted locally and are widely distributed. The main types of proteins that make up the matrix include collagens, elastin, fibronectin and laminin.
Collagens are a family of highly characteristic fibrous proteins found in all multicellular animals. They are the most abundant proteins in mammals, constituting about 25 percent of their total protein. A central feature of all collagen molecules is their stiff, triple-stranded helical structure. See, for example, Miller and Gay, “The Collagens: An Overview and Update,” pp. 3-41,
Methods in Enzymology
(ed. Colowick and Kaplan), v. 144 (1987), Academic Press, Inc.
Elastin, present in elastic fibers of tissues such as blood vessels and skin, gives these tissues the required ability to recoil after transient stretch. Elastin is the major component of these elastic fibers, where it is present as an extensively cross-linked polypeptide having a peculiar chemical composition. Approximately one third of the amino acids in elastin are glycine, 10-13 percent are proline, and over 40 percent are other amino acids with hydrophobic side chains. Elastin contains very small amounts of hydrophilic amino acids.
Laminin is a large glycoprotein and a major component of basement membranes. Laminin is made by all epithelial cells that have been studied. Laminin is made up of three different subunits disulfide-bonded into an asymmetric cross-linked structure. For review see Barlow et al., “Molecular Cloning of Laminin, ” pp. 404-474 in
Methods in Enzymology,
v. 144 (1987) Academic Press, Inc.
Fibronectin is a cell-surface and blood glycoprotein involved in a variety of cell surface phenomena. It is present as an insoluble form at the cell surface and in connective tissue, and found in soluble form in plasma. For reviews, see Ruoslahti et al., “Fibronectin: Purification, Immunochemical Properties, and Biological Activities,” pp. 803-831, in
Methods in Enzymology,
supra; Hynes et al., “Isolation and Analysis of cDNA and Genomic Clones of Fibronectin and its Receptor,” pp. 447-463, in
Methods in Enzymology,
v. 144, Academic Press, Inc. (1987).
Combinations of components of the extracellular matrix are often incorporated into cosmetic compositions. Elastin, in particular, is often utilized. Because the naturally-occurring crosslinked elastin fibers are insoluble (i.e., insoluble in water, organic solvents, and physiological fluids such as saline, blood, and lymph), the elastin is first rendered soluble using a variety of chemical and enzymatic methods. The rationale behind these procedures is that soluble elastin, and various derivatives thereof, is expected to penetrate into the skin to a greater degree than cross-linked elastin, compensating for loss of elastin during skin ageing. The chemical and enzymatic methods designed to solubilize elastin are problematic, however, because they can induce chemical and structural changes in the elastin molecule itself.
A further consideration when using proteins of the extracellular matrix in cosmetics concerns the degree to which the proteins produce unwanted allergic responses in the subject's skin. Such responses are of particular concern with compositions utilizing elastin since many cosmetics employ solubilized elastin isolated from the neck tendons of young calves or other non-human mammals.
There remains a need for the development of improved strategies, methods, and compositions that allow use of extracellular matrix proteins, particularly human proteins, in cosmetic compositions.
SUMMARY OF THE INVENTION
The present invention pertains to a cosmetic composition including a non naturally-occurring extracellular matrix protein in combination with a cosmetic carrier. The extracellular matrix protein is preferably of human origin and has not been previously cross-linked. The protein is most preferably selected from the group consisting of soluble human procollagen and soluble human tropoelastin. The extracellular matrix protein may include at least one additional non-naturally occurring amino acid sequence moiety, the amino acid sequence moiety selected from the group consisting of a hydrophobic sequence, a hydrophilic sequence, and a lysine-rich sequence.
In preferred embodiments of the present invention, the cosmetic composition is formulated to reproduce one or more aspects of the extracellular matrix found in skin of a selected individual. In particular, one aspect of the present invention involves the recognition that different individuals may produce different allelic variants, or populations of allelic variants of extracellular matrix proteins in their skin. As used herein, the term “allelic variants” refers to different versions of a protein, or a gene encoding that protein, present in the human population. Protein variants can differ from one another by addition, substitution, or deletion of one or more amino acids. Typically, such proteins are produced from gene variants that differ from one another by addition, substitution, or deletion of one or more nucleotides
1
. Alternatively or additionally, such protein variants can be produced by alternative splicing or other processing of genetic sequences.
According to one particularly preferred embodiment of the present invention, a particular individual is selected on the basis of having appealing skin characteristics. The allelic composition of one or more extracellular matrix proteins in that person's skin is identified, and that composition is reproduced in a cosmetic formulation. Those of ordinary skill in the art will recognize that what constitutes “appealing” skin may vary according to the preferences of the manufacturer of the cosmetic or the person onto whom the cosmetic is to be applied, and according to the circumstances under which the cosmetic is to be used. For example, in some contexts, skin is “appealing” if it has attributes characteristic of the skin of an individual who is chronologically younger than the posessor of the skin. In other contexts, skin is “appealing” if it has attributes similar or identical to those of the person to whom the cosmetic is to be applied, so that negative immune reactions can be minimized or avoided.
DETAILED DESCRIPTION OF CERTAIN PREFERRED EMBODIMENTS OF THE INVENTION
Definitions
One aspect of the invention is a cosmetic composition containing a non naturally-occurring form of an extracellular matrix protein. The following definitions clarify the scope of this and other aspects of the invention:
The term “cosmetic” or “cosmetic composition” as used herein, is intended to include any type of product that is applied in any manner directly to the person.
The term “extracellular matrix protein” refers to those macromolecules that constitute the extracellular matrix. The main classes of protein that make up the extracellular matrix are collagens, elastin, fibronectin, and laminin.
“Non naturally-occurring”, when applied to the extracellular matrix proteins of the present invention means polypeptides: (i) produced from nucleic acids that were prepared using recombinant DNA methods; (ii); synthesized by, for example, chemical synthetic methods; (iii) separated from at least some of the biological materials with which the proteins are normally associated in nature, and purified usi
Choate Hall & Stewart
Jarre Brenda Herschbach
Jones W. Gary
Souaya Jehanne
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