[0001] This application claims the benefit of U.S. Provisional Application No.
60/729,880, which was filed on 24 Oct. 2005. U.
S. Provisional Application No. 60/729,880 is incorporated by reference in its entirety.
composition, and more specifically to a topical skin care composition [0004] 2. Description of the Related Art [0005] Collagen is one of the long, fibrous structural proteins whose enzymes. Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, making up about 40% of the total.
It is tough and inextensible, with great tensile strength, and is the main component of cartilage, ligaments and tendons, and the main protein component of bone and teeth. Along with soft keratin, it is responsible for skin strength and elasticity, and its degradation leads to wrinkles that accompany aging. Collagen strengthens blood vessels and plays a role in tissue development.
Collagen is present in the cornea and lens of the eye in crystalline form. It is also used in cosmetic surgery and burn [0006] Collagen occurs in many places throughout the body, and in many different forms, each form being known as a type. There are at least 12 different types of collagen, with Type I collagen being the most abundant.
The basic triple-helix structure of Type I collagen is the domains at their amino or carboxyl terminal ends. Type I collagen may be found in skin, tendons, and bone, and Types I-III are recognized as [0009] The basic structural unit of Type I, II, and III collagen is tropocollagen, which is cross-linked to from large fibers of collagenous tissues. Tropocollagen is made of three polypeptide chains called .
alpha. chains, where each of the .alpha.
chains is wound around the other to form a triple helix structure. Every third AA or IA in the .alpha.
chain [0010] Sixty percent of the .alpha. chains are made of either the sequence Gly-Pro-X or the sequence Gly-X-Hyp, where X may be any AA or IA.
The remaining forty percent of the .alpha. chains are various sequences of AAs and IAs, with every third AA or IA being a glycine.
The AAs and IAs can take place. Three enzymes are required for proper hydroxylation: lys1 hydroxylase, prolyl-4-hydroxylase, and prolyl-3-hydroxylase. 5-hydroxylysine.
Prolyl-4-hydroxylase converts prolines in the sequence X-Pro-Gly to 4-hydroxyproline. Prolyl-3-hydroxylase converts prolines in the sequence Hyp-Pro-Gly to 3-hydroxyproline. The above hydroxylation reactions require Fe.
sup.2+, ascorbic acid (vitamin C), oxygen, and .alpha.
-ketoglutarate in the chemical reaction that is described below in replication of skin cells, the topical application of tropocollagen factors has been used to treat skin conditions such as sun-burn, malasma, wrinkling, telangiectasias (spider-veins), and dilated pores. [0014] However, as was explained above, in order to hydroxylate new collagen proteins in order to synthesize new Type I, II, and III collagen, the tropocollagen factors found in conventional topical ascorbic acid, such as an ascorbate, and tropocollagen factors, such as proline, glycine, and lysine, in a skin care composition for topical application. Compared to conventional products that provide little or no additional ascorbic acid, the presence of the increased amounts of collagen proteins (Types I, II, and III), and in turn, the increased replication of, among other things, skin cells.
transitional metal, such as copper, in a topical product may [0020] When expressing concentrations of a substance, the mass-volume percentage may be used for solutions made from solid reagents. For purposes of this disclosure, the mass-volume percentage, which is abbreviated as "% m/v," is defined as the mass of the solute in grams hundred. The mass-volume percentage denotes the mass of the substance in according to some preferred embodiments of the invention, as well as the preferred concentration ranges for those ingredients.
In Table I, the 20070092471 - - Cosmetic composition for the oxidative treatment of hair or skin, prepared by mixing of at least two components, in which dehydroascorbic acid or a dehydroascorbic acid salt or a dehydroascorbic acid derivative is generated from ascorbic acid, ascorbic acid derivative and ascorbic acid salt prior to application by an enzyme ...
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