Peptide-based hair treatment

Abstract

The treatment according to the invention involves the use of at least one peptide of general formula X-(Xaa)nGQPR(Xaa)mZ for a non-therapeutic cosmetic hair treatment.In the formula, Xaa is an amino acid chosen from proline (P, Pro), glycine (G, Gly), alanine (A, Ala), valine (V, Val), leucine (L, Leu) and isoleucine (I, Ile), the Xaa being chosen independently of each other; with n and m integers which may be equal or different between 0 and 5; at the N-terminal end X is chosen from H, CO-R1, or SO2-R1; at the C-terminal end Z is chosen from OH, OR1, NH2, NHR1, or NR1R2; R1 and R2 being, independently of each other, chosen from an alkyl, aryl, aralkyl, alkylaryl, alkoxy, saccharide and aryloxy group, which may be linear, branched, cyclic, polycyclic, unsaturated, hydroxylated, carbonyl, phosphorylated and / or sulfur-containing, said group having from 1 to 24 carbon atoms and having in its skeleton one or more O, S and / or N heteroatoms. The preferred peptide sequences are Pal-GQPR-OH or Pal-GQPR-NH2.These peptides act on multiple levels: hair follicle stem cells, dermal papillae, signaling pathways, and the extracellular matrix. They can be used for cosmetic hair treatments, particularly to protect the structure of hair and / or body hair, including eyelashes and eyebrows, slow hair loss, induce and / or stimulate growth, prevent depigmentation, and / or induce pigmentation.

Description

Title of the invention: Peptide-based hair treatment

[0001] The present invention relates to a hair treatment, that is to say both capillary (hair) and hairy (including eyelashes and eyebrows) based on peptide(s), from mammals, animals or humans.

[0002] In the context of the present invention, the term "peptide" refers to peptides containing twenty or fewer amino acids, their derivatives, isomers, and complexes with other species such as a metal ion (e.g., copper, zinc, manganese, magnesium, and others). The term "peptides" refers to both natural peptides and (bio)synthetic peptides. It also refers to compositions containing peptides that occur in nature and / or are commercially available.

[0003] The present invention relates to the cosmetics, personal hygiene and care products and dermopharmacy industries, for humans and animals.

[0004] More particularly, the present invention relates to a means for inducing and / or stimulating the growth of hair, body hair, eyelashes and eyebrows, protecting their structure, slowing their loss, preventing their depigmentation and / or inducing their pigmentation.

[0005] Hairs and hairs comprise two parts, the hair follicle (or hair follicular) and the shaft (or hair fiber), as well as annexes, the most important of which are the sebaceous gland, which has a lubricating role, and the arrector pili muscle, which has the role of erecting the hair to regulate temperature or to help with the excretion of sebum.

[0006] To simplify the rest of the description, the terms "hair" or "body hair" will be used interchangeably to encompass "body hair, head hair, eyelashes and eyebrows".

[0007] The hair follicle is the non-visible part. It is divided into 3 segments, from top (epidermis) to bottom (dermis):

[0008] - The infundibulum is located from the surface of the epidermis to the sebaceous gland.

[0009] - The isthmus is located in the dermis, between the sebaceous gland and the insertion site of the arrector pili muscle. This insertion site, also called the bulge, is a niche for stem cells.

[0010] - The bulb is located in the dermis, below the bulge. At the base of the bulb is The papillary dermis is composed of mesenchymal cells called HFDPCs (Human Follicle Dermal Papilla Cells) that interact with other cells in the hair bulb to induce hair growth. The papillary dermis also contains blood vessels that supply the nutrients and oxygen necessary for hair growth. The hair shaft or hair fiber. Above and around the dermal papilla lies a so-called germinal zone containing stem cells (keratinocytes, melanocytes, and matrix cells). The keratinocytes in the germinal zone are pigmented by neighboring melanocytes. These keratinocytes undergo differentiation and apical migration to give rise to the keratogenic zone, where keratin is produced. The matrix cells proliferate and differentiate, giving rise to the hair shaft.

[0011] The hair shaft or fiber is the visible part that is outside the hair follicle. It is composed of 3 layers, from the outside in:

[0012] - The cuticle is composed of cells arranged in scales that protect the hair from external aggressions.

[0013] - The cortex is composed of cortical cells having a fibrous character, of the shape Fusiform, sealed and interlocked. The cortex gives hair its color, strength and resistance.

[0014] - The bone marrow is composed of medullary cells which are degenerated cells and replaced by large vacuoles filled with air and a few grains of melanin.

[0015] Hair and body hair are essential for protecting the skin and scalp from external aggressions. They are mainly composed of keratin.

[0016] Their growth and renewal are primarily determined by the activity of the hair follicles and their matrix environment. Their activity is cyclical and essentially comprises three phases: the anagen phase, the catagen phase, and the telogen phase, which repeat until the hair dies. Thus, hair does not grow continuously, but in successive cycles. This cycle repeats between twenty-five and thirty times during a person's lifetime, thanks to the regenerative capacity of the follicle stem cells located in the bulb region.

[0017] The hair growth cycle begins with the anagen phase, which corresponds to a period of rapid hair growth within the hair follicle. This phase lasts on average from 2 to 5 years. 85% to 90% of hairs are usually in the anagen phase. During this phase, the hair bulb regenerates and then produces the hair fiber. The hair thus grows approximately 1 cm per month. This is a highly proliferative phase resulting from the proximity between the dermal papilla, in contact with blood vessels, and the bulge, where the hair stem cells are located. From this point, the fiber is formed through the intense production of keratin and keratinocytes, which subsequently form the outer cuticles of the hair and the cortex.

[0018] At the end of this anagen phase, the follicle enters a regression phase called the catagen phase, and synthesis ceases. The fiber no longer grows due to a lack of blood supply to the dermal papilla via the blood vessels. This phase lasts only a few weeks and affects approximately 2 to 3% of hairs at any given time. The follicle retracts and gradually involutes. The keratinocytes and melanocytes gradually disappear and the bulb collapses on itself while retaining the dermal papilla.

[0019] Next, the dermal papilla begins to move upwards towards the bulge. This is the telogen phase, which precedes a new anagen phase. 8 to 10% of hairs are in the telogen phase at any given time. They remain in this phase for approximately 6 to 7 months in young people, but longer with increasing age.

[0020] This hair cycle is the same for hairs with different phase durations and therefore different cycle durations, in particular the duration of the anagen phase is shorter for hairs.

[0021] Hair is generally damaged and weakened by the action of external atmospheric agents such as light and weather, as well as by mechanical or chemical treatments such as brushing, combing, dyeing, bleaching, perming and / or straightening, or even repeated washing.

[0022] In addition, during aging, hair becomes thinner and its cycles shorter.

[0023] The hair thus becomes damaged and can become dry, rough, brittle, dull or lead to hair loss reducing hair density.

[0024] To remedy these drawbacks, it is common to use products intended for the treatment of hair or scalp, such as plant extracts, pure synthetic molecules, vitamins and keratin hydrolysates with various sulfur compounds.

[0025] There is therefore always a need for effective products that reduce side effects such as the risks of irritation and allergy, to preserve and / or improve the general condition of the hair and / or body hair.

[0026] To address this problem, the present invention proposes the use of a peptide for cosmetic hair treatment.

[0027] To this end, according to a first object, the present invention proposes the use of at least one peptide of general formula X-(Xaa)nGQPR(Xaa)mZ (SEQ ID NO: 1), wherein:

[0028] - Xaa is an amino acid selected from proline (P, Pro), glycine (G, Gly), alanine (A, Ala), valine (V, Val), leucine (L, Leu) and isoleucine (I, Ile), the Xaa being chosen independently of each other, with n and m being integers which may be equal or different between 0 and 5;

[0029] - at the N-terminal end X is chosen from H, CO-Ri, or SO2-Ri;

[0030] - at the C-terminal end Z is chosen from OH, ORi, NH2, NHRB or NRiR2;

[0031] - Ri and R2 being, independently of each other, chosen from a grouping alkyl, aryl, aralkyl, alkylaryl, alkoxy and aryloxy, which may be linear, branched, cyclic, polycyclic, unsaturated, hydroxylated, carbonyl, phosphorylated and / or sulfurized, said group having from 1 to 24 carbon atoms and which may possess in its skeleton one or more O, S and / or N heteroatoms;

[0032] for a non-therapeutic cosmetic hair treatment.

[0033] By "non-therapeutic cosmetic treatment" is meant a treatment which is intended for hair and / or body hair in a healthy state (as opposed to a pathological state), with the aim of beautifying it or preventing (as a preventive measure) aesthetic disorders, for example thinning hair.

[0034] According to the invention, the Xaa may be identical or different. Preferably, the Xaa are chosen from glycine (G, Gly) and alanine (A, Ala).

[0035] Pal-GQPR (SEQ ID NO: 2) is used in several cosmetic active ingredients marketed by Sederma. For example, in the product RIGIN™ as an anti-aging cosmetic active ingredient to improve skin quality, in the product Matrixyl 3000™ in combination with Pal-GHK as an anti-aging cosmetic active ingredient, in the product Haloxyl™ in combination with Pal-GHK, N-hydroxysuccinimide and chrysin as an anti-aging active ingredient, or in the product Synchrolife™ in combination with chrysin and a rosemary extract as an active ingredient to combat the signs of skin fatigue.

[0036] The inventors have shown surprisingly that the peptide according to the invention is particularly interesting for significantly improving the stimulation of hair growth, including eyelashes and eyebrows, and / or slowing down their loss, preventing their depigmentation and / or inducing their pigmentation.

[0037] According to a preferred feature, the peptide according to the invention is modified at its N-terminus and / or C-terminus. Preferably, it is modified only at its N-terminus. The derivatization of the peptide at the N- and / or C-terminus is intended, in particular, to improve the bioavailability of the peptide by enhancing its penetration into the skin or scalp. This effect can also be achieved through vectorization, for example, via encapsulation.

[0038] According to another preferred feature, Ri and / or R2 is an alkyl chain of 1 to 24 carbon atoms, preferably a lipophilic alkyl chain of 3 to 24 carbon atoms.

[0039] According to another preferred feature, X is a CO-Ri acyl group. Preferably, X is selected from an octanoyl (C8), decanoyl (C10), lauroyl (C12), myristoyl (C14), palmitoyl (C16), stearoyl (C18), biotinoyl, elaiidoyl, oleoyl, and lipoyl group. More preferably, X is selected from a lauroyl (C12), myristoyl (C14) group. and palmitoyl (Cl6). Preferably, X is chosen from a panhitoyl (Cl6), myristoyl (C14) and lauroyl (C12). Preferably, X is the palmitoyl (C16).

[0040] According to another preferred characteristic, Z is chosen from OH, OME, OEt and NH2. Preferably, Z is chosen from OH and NH2.

[0041] Peptides comprising in N-terminal or C-terminal position derivatives of particular acids such as those of ascorbic, retinoic, cinnamic, oleanolic, hyaluronic, nicotinic, lipoic, gallic or pantothenic acid are also covered by the present invention.

[0042] The peptides particularly preferred according to the invention are Pal-GQPR-OH (SEQ ID NO: 2) and Pal-GQPR-NH2 (SEQ ID NO: 3).

[0043] The peptides according to the invention may be optically pure, or may consist of the L or D isomers or a mixture thereof. The L isomers, which are those present in nature, may be preferred.

[0044] The present invention also covers derivatives (with modification and / or addition of a chemical function to one or more of the amino acids but without change in the carbon skeleton) and analogues (with modification and / or addition of a chemical function to one or more of the amino acids but with an additional change in the carbon skeleton), complexes with other species such as a metal ion (for example copper, zinc, manganese, magnesium, and others).

[0045] The peptides may, where appropriate, be in the form of salts, in particular hydrochloric salt, or acetate.

[0046] More specifically, the present invention proposes a cosmetic hair treatment adapted to:

[0047] - To protect the structure of the hair and / or body hair, including eyelashes and eyebrows ;

[0048] - To slow down the loss of hair and / or body hair, including eyelashes and eyebrows;

[0049] - To induce and / or stimulate the growth of hair and / or body hair, including eyelashes and eyebrows; and / or

[0050] - To prevent depigmentation and / or induce pigmentation of hair and / or Hair, including eyelashes and eyebrows.

[0051] Specifically, it has been shown that the cosmetic treatment according to the present invention is capable of acting at several levels.

[0052] At the level of hair follicle stem cells, collagen XVII is an important molecule that helps maintain the stem cell character of HFSCs (Hair Follicle Stem Cells). HFSCs are slow-cycle cells that have the ability to induce hair growth. When collagen XVII is degraded by elastase, the HFSC niche is altered, as is their ability to induce hair growth. Thus, in By protecting collagen XVII from elastase, the stem cells of the hair follicle are protected and the ability of hair and / or scalp hair to grow and regenerate is maintained.

[0053] At the level of the dermal papillae, which contain HFDPCs that aggregate and form a spherical structure. This HFDPC structure is necessary for the development of hair follicles because their dispersion prevents the formation of hair follicles. HFDPCs are also capable of sending signals to hair stem cells to activate their growth. In addition, the size of the dermal papilla has an effect on hair thickness. Thus, protecting the dermal papillae helps stimulate hair growth and morphogenesis.

[0054] At the level of the ERK (or "Extracellular signal-regulated kinases," which add phosphate groups to other proteins to activate them) and AKT (or protein kinase B, an essential protein in mammalian cell signaling) signaling pathways. These pathways are involved in cell proliferation, differentiation, and apoptosis for ERK, and in cell proliferation, migration, and aggregation for AKT. Activation of these two pathways thus allows the growth of dermal papillae. Phosphorylation of ERK and AKT proteins (denoted pERK and pAKT) leads to the activation of the corresponding signaling pathways. Thus, stimulating the phosphorylation of ERK and AKT proteins allows the division of dermal papilla cells responsible for hair growth and morphogenesis.

[0055] At the level of the extracellular matrix (ECM), a decrease in the synthesis of extracellular matrix proteins, for example, collagen, laminins, and fibronectin, causes a loss of elasticity and tone in the dermis. There is also a decrease in the coherence and organization of hair follicles, a decrease in their anchoring, a decrease in the duration of the anagen phase, and a lengthening of the telogen phase. The hairs are thinner and therefore more fragile. This manifests as a decrease in hair density and a progressive decrease in follicle diameter, giving the hair a sparse, thinner appearance.

[0056] Furthermore, hyaluronic acid is found in the extracellular matrix. Hyaluronic acid is a single-repeat disaccharide polymer that is found mainly in the dermis and epidermis.

[0057] This molecule has the capacity to bind 1000 times its weight in water. It plays a role in skin hydration and in preventing skin and hair aging. Hyaluronic acid contributes to keratinocyte activity, including cell adhesion and proliferation, and interacts with numerous molecules such as cytokines, growth factors, chemokines, and cell receptors. For example, CD44 is a hyaluronic acid receptor present in the cell surface. CD44 is involved in cell-to-cell interactions and cell adhesion.

[0058] A decrease in hyaluronic acid and / or CD44 is accompanied by a decrease in cell proliferation, survival, and motility. Hyaluronic acid, by binding to CD44, leads to the phosphorylation of the AKT protein, thus activating the corresponding metabolic pathway to promote hair growth and morphogenesis. Therefore, stimulating the synthesis of hyaluronic acid and proteins contained in the extracellular matrix allows for better anchoring and growth of the follicle, hair, and / or strand, thereby reducing hair loss and preserving and / or improving their overall condition.

[0059] At the gene level, HAPLN1 (Hyaluronan and Proteoglycan Link Protein 1), a glycoprotein, is known to maintain the integrity of the extracellular matrix and to combat hair loss. It is predominantly expressed during the anagen phase of the hair cycle. HAPLN1 promotes the proliferation of hair matrix cells and inhibits hyaluronic acid degradation. Thus, increased expression of the HAPLN1 gene helps prevent hyaluronic acid degradation, combat hair loss, and increase the proliferation of hair matrix cells.

[0060] It is also known that recombinant human HAPLN1 (rhHAPLN1) activates the ERK signaling pathway, which is induced by the TGF-

[32] gene. Thus, an increase in the TGF-

[32] gene increases ERK phosphorylation and activates the corresponding pathway, enabling the division of dermal papilla cells responsible for hair growth and morphogenesis. Therefore, an increase in the TGF-

[32] gene allows for improved hair growth and morphogenesis.

[0061] At the melanocyte level, a decrease in tyrosinase activity (an enzyme playing an intermediate role in melanin formation) and melanin synthesis leads to hair whitening. Therefore, stimulating melanin synthesis and tyrosinase activity helps prevent graying of hair and / or body hair.

[0062] In vitro test results are given later in the description to demonstrate these specific cosmetic activities, which are beneficial for hair. The detailed description also presents an ex vivo study on the growth of hair fibers and / or hair fibers from hair follicles obtained from facelift surgeries.

[0063] Visually, this translates into an improvement in the overall condition of the hair and / or body hair. Thus, the treatment according to the invention makes it possible to prevent dry, rough, brittle, dull and / or split ends.

[0064] According to a second object, the present invention also proposes the use of a composition, in particular topical, comprising at least one peptide according to the invention and a physiologically acceptable medium.

[0065] By "topical treatment" or "topical use" is meant an application which is intended to act at the site where it is applied.

[0066] By "physiologically acceptable medium" means, according to the present invention, without limitation, an aqueous or hydroalcoholic solution, a water-in-oil emulsion, an oil-in-water emulsion, a microemulsion, an aqueous gel, an anhydrous gel, a serum, a vesicle dispersion, a powder.

[0067] “Physiologically acceptable” means that the composition is suitable for a Topical use in contact with mucous membranes, nails, scalp, hair, including eyelashes and eyebrows, and mammalian skin, particularly human, without risk of toxicity, incompatibility, instability, allergic response, and others.

[0068] This "physiologically acceptable medium" forms what is classically called the excipient of the composition.

[0069] Depending on the physiologically acceptable environment and the concentration of peptide(s), this composition may constitute a concentrated active ingredient intended to be included in a final composition for a consumer, or may directly constitute said final composition, less concentrated.

[0070] In a composition according to the invention, the peptide(s) may be present at a higher or lower concentration depending on its intended use, ranging from 107% to 20% relative to the total weight of the composition, preferably ranging from 106% to 10%, preferably still from 105% to 5%, by weight relative to the total weight of the composition.

[0071] For example, in a composition forming an ingredient according to the invention, at least one peptide according to the invention will be present at a high concentration generally ranging from 100 ppm to 20,000 ppm, preferably from 100 ppm to 5,000 ppm, and even more preferably from 100 ppm to 1,000 ppm. This ingredient will then generally be formulated at between 0.01% and 10%, preferably between 1% and 5%, in the final topical preparation.

[0072] When several peptides according to the invention are present in a composition according to the invention, they may be present in varying relative proportions, in equivalent quantities, or on the contrary in different proportions.

[0073] All percentages and ratios used in this application are expressed in relation to the weight of the total composition and all measurements are taken at 25°C unless otherwise specified.

[0074] According to a particular aspect of the invention, the peptide(s) according to the invention can be solubilized in a lipophilic or hydrophilic matrix with, where appropriate, a solubilizer, depending on the application envisaged.

[0075] The peptide(s) in the treatment according to the invention may be combined with other active ingredients at effective concentrations that can act synergistically or reinforcingly to achieve the desired effects described for the invention, such as the following agents: calming, moisturizing, antioxidant, anti-hair loss, anti-dandruff, restoring the skin flora, acting on the cuticles, on the softness and silkiness of hair and body hair, etc. These active ingredients may be obtained from plant materials, such as plant extracts or products of in vitro plant culture or fermentation.

[0076] The peptide according to the invention can be associated with one or more other active ingredients at effective concentrations that can act synergistically or in reinforcement to achieve the desired effects described for the invention, such as the following agents: filtering radiation, in particular UVA, UVB, IR, from blue light, moisturizing, calming, muscle relaxing, restructuring, acting on microcirculation, acting on the skin microbiome, acting on inflammation, on free radicals, vitamins, anti-wrinkle, etc.

[0077] More specifically, to improve or enhance the general condition of hair and body hair, the peptide according to the invention can be combined, without this list being exhaustive, with one or more active ingredients:

[0078] - an anti-dandruff active ingredient acting as an antifungal: such as Zinc Pyrithione, Ketoconazole, Climbazole, Piroctone Olamine, Selenium Disulfide, Picnidium, or APISCALP™, Matrixyl® or BB-Biont™, active ingredients of the applicant; and / or

[0079] - an active ingredient that slows down or inhibits the growth of yeasts responsible for the condition skin-bound (of the Malassezia genus) and acting favorably on the skin barrier, such as the peptide Pal-KTTKS (SEQ ID NO: 4) or Pal-KTSKS (SEQ ID NO: 5); and / or

[0080] - a moisturizing active ingredient such as DuraQuench IQ™ (CRODA) or INSAPONIFIABLE of SHEA (Sederma); and / or

[0081] - an active ingredient that rebalances the skin microflora such as the active ingredient HAIRSPA™ (SEDERMA);

[0082] - a calming active ingredient such as PACIFEEL™ (SEDERMA); and / or

[0083] - an active ingredient to prevent hair loss and stimulate hair growth such as CAPIGENE™, CAPILECTIN™, PROCAPIL™ (SEDERMA); and / or

[0084] - an active ingredient to strengthen the structure of damaged hair such as CERAMIDE A2™, CERAMIDE HO3™, HELIOGENOL™ (SEDERMA); and / or

[0085] - an active ingredient for smoothing hair such as FRUIT BIO™ (SEDERMA); and / or

[0086] - an active ingredient to protect hair and body hair, including eyelashes and eyebrows, from UV and IR radiation such as VENUCEANE™; and / or

[0087] - an agent for repigmenting hair and body hair, including eyelashes and eyebrows, such as SYLVERFREE™

[0088] Detailed examples are given in the formulation section below.

[0089] The Personal Care Products Council (“International Cosmetic Ingredient Dictionary & Handbook” published by the Cosmetic, Toiletry, and Fragrance Association, Inc., Washington, DC) describes a wide variety, without limitation, of cosmetic and pharmaceutical ingredients commonly used in the personal care industry that are suitable for use as additional ingredients in compositions according to the present invention, provided they are physically and chemically compatible with the other ingredients of the composition and especially with the active ingredients of the present invention. Furthermore, the nature of these additional ingredients must not alter the benefits of the active ingredients of the invention. These additional ingredients may be synthetic or natural, such as plant extracts, or derived from a biofermentation process.

[0090] Other skin care actives, including scalp care, which are particularly useful in combination with the composition according to the invention can be found in the commercial documentation of Sederma, Crodarom and Alban Muller International, and on the website www.croda.com.

[0091] Other examples include the following commercial active ingredients: betaine, glycerol, Actimoist Bio 2™ (Active Organics), AquaCacteen™ (Mibelle AG Cosmetics), Aquaphyline™ (Silab), AquaregulK™ (Solabia), Carciline™ (Greentech), Codiavelane™ (Biotech Marine), Dermaflux™ (Arch Chemicals, Inc.), Hydra'Flow™ (Sochibo), Hydromoist L™ (Symrise), RenovHyal™ (Soliance), Seamoss™ (Biotech Marine), Argireline™ (the trade name for Lipotec's acetyl hexapeptide-3), spilanthol, or an extract of Acmelia oleracea known as Gatuline Expression™, an extract of Boswellia serrata known as Boswellin™, Deepaline PVB™ (Seppic), Syn-AKE™ (Pentapharm), Ameliox™, Bioxilift™ (Silab), PhytoCellTec™Argan (Mibelle), Papilactyl D™ (Silab), Preventhelia™ (Lipotec), or one or more of the following active ingredients sold by Sederma: Subliskin™, Venuceane™, Moist 24™, Vegesome Moist 24™, Essenskin™, Juvinity™, Revidrat™, Resistem™, Chronodyn™, Kombuchka™, Chromocare™,Calmosensine™, Glycokin factor S™, Biobustyl™, Idealift™, Ceramide 2™, Ceramide A2™, Ceramide HO3™, Legance™, Intenslim™, Prodizia™, Beautifeye™, Pacifeel™, Zingerslim™, Meiritage™, Sebuless™, Apiscalp™, Rubistem™, , Citystem™, Neonyca™, NG Unsaponifiables of Shea Butter™, Majestem™, Hydronesis™, Poretect™, Amberstem™, Synchrolife™, Feminage™, Sylverfree™, Ameyezing™, Revitalide™, Mel[o]stem™, Luceane™ or mixtures thereof.

[0092] Among the plant extracts (in the form of conventional extracts or prepared by an in vitro method) that can be used as additional active ingredients, the following may be mentioned, in particular, in addition to and in particular: extracts of ivy, for example of common ivy (Hedera helix), Bupleurum chinensis, Bupleurum falcatum, arnica (Arnica montana L.), rosemary (Rosmarinus officinalis N.), calendula (Calendula officinalis), sage (Salvia officinalis L.), ginseng (Panax ginseng), ginkgo biloba, St. John's wort (Hyperycum perforatum), butcher's broom (Ruscus aculeatus L.), meadowsweet (Filipendula ulmaria L.), Java tea (Orthosiphon stamincus Benth.), artichoke (Cynara scolymus), algae (Fucus vesiculosus), birch (Betula alba), green tea,cola nut (Cola nipida), Indian chestnuts, bamboo, Centella asiatica, heather, fucus, willow, piloselle, ash extracts, cangzhu extracts, Crysanthellum indicum extracts, plants of the genus Armeniacea, Atracty, Pharbino, Pharmatino , Flemingia, of Coleus as C. forskohlii , C. blumei, C. esquirolii, C. scutellaroides , C. xanthantus and C. barbatus, as an extract of roots of Coleus barbatus, extracts of Ballote, Guioa, Davallia, Terminalia, Barringtonia, Trobia, Antioch, Antioch Argania, Dioscoreae as Dioscorea opposita or Mexicain, extracts of Ammi visnaga, Siegesbeckia, in particular Siegesbeckia orientalis, plant extracts of the family Ericaceae, in particular extracts of blueberries (Vaccinium angustium) of Arfosilo, Arfosilo vera, of plants containing sterols (especially phytosterols), of Manjistha (extract of plants of the genus Rubia,in particular Rubia cordifolia), Guggal (extract of plants of the genus Commiphora, in particular Commiphora mukul), an extract of kola, chamomile, purple clover, Piper methysticum (Kava Kava of Sederma), Bacopa monieri (Bacocalmine™, Sederma) and foliage of Merhi, glacier, glaze mulberry, melaleuca (tea tree), Larrea divaricata, Rhabdosia rubescens, Euglena gracilis, Fibraurea recisa hirudinea, Chaparral sorghum, sunflower, Enantia chlorantha, Mitracarpe of the genus Spermacocea, Busonia, Lawsonia, Lawsonia, i. of Adiantium capillus-veneris L., of Chelidonium majus, of Luffa cylindrica, of "Japanese Mandarin" (Citrus reticulata blanco var. unshiu), of Camélia sinensis, of Imperata cylindrical, of Glaucium flavum, of Cupressus sempervirens, of Polygonatum multiflorum, of Logravely, Sambuly of Phaseolus lunatus, of Centaurium, of Macrocystis pyrifera , of Tumera diffusa, of Anemarrhena asphodeloides,of Portulaca pilosa, , Humulus lupulus, Arabica coffee, Ilex paraguariensis, Globularia cordifolia, Oxydendron arboreum, Albizzia julibrissin, Zingiber zerumbet smith, Astragalus membranaceus, Atractylodes macrocephalae, Plantago lanceolata, Leontopodium alpinum (or eldelweiss), Mirabilis jalapa, Apium graveolens, Marrubium vulgare, Buddleja davidii Franch., Syringa vulgaris, Engelhardia chrysolepsis, Monarda didyma, or orchids.

[0093] The compositions according to the present invention may comprise peptides, including, but not limited to, di-, tri-, tetra-, penta- and hexapeptides and their repeats and derivatives. According to a particular embodiment, the concentration of the additional peptide in the composition varies between 10⁷% and 20%, preferably between 10⁶% and 10%, preferably between 10⁵% and 5%, by weight.

[0094] Non-limiting examples of dipeptides that can be used in the context of the present invention include Carnosine (|3-AH), YR, VW, NF, DF, KT, KC, CK, KP, KK, TT, PA, PM or PP.

[0095] Non-limiting examples of tripeptides include RKR, HGG, GHK, GKH, GGH, GHG, KFK, KAvaK, K[3AK, KAbuK, KAcaK, KPK, KMOK, KM02K, PPL, PPR, SPR, QPA, LPA or SPA. We can also cite non-limiting examples of tripeptides containing:

[0096] - a proline grafted onto lysine such as K(P)HG or K(P)GH; or

[0097] - a proglutamic acid grafted to a lysine such as K(Pyr)HG or K(Pyr)GH; or

[0098] - an acetylated lysine such as K(Ac)HG or K(Ac)GH.

[0099] Non-limiting examples of tetrapeptides are KTFK (SEQ ID NO: 6), RSRK (SEQ ID NO: 7), KTAK (SEQ ID NO: 8), KAYK (SEQ ID NO: 9), KFYK (SEQ ID NO: 10), TKPR (SEQ ID NO: 11), AVPG (SEQ ID NO: 12), VPGA (SEQ ID NO: 13), LKLE (SEQ ID NO: 14), ELED (SEQ ID NO: 15) or LLAN (SEQ ID NO: 16).

[0100] A non-limiting example of a pentapeptide is KTTKS (SEQ ID NO: 17) and KTSKS (SEQ ID NO: 18) and examples of hexapeptides are GKTTKS (SEQ ID NO: 19) and VGVAPG (SEQ ID NO: 20).

[0101] Other peptides usable within the framework of the present invention may be chosen from, without this list being limiting: lipophilic derivatives of peptides, preferably oleoyl, palmitoyl and myristoyl derivatives, and complexes with the metal ions mentioned above (for example: copper complex of the tripeptide HGG).

[0102] Preferred dipeptides include, for example, N-Palmitoyl-[3-Ala-His, N-Acetyl-Tyr-Arg-hexadecylester (Calmosensine™, Idealift™, Sederma), Pal-KT, Pal-RT, Pal-PP and Pal-PA (Sederma).

[0103] Preferred tripeptides include, in particular, the copper derivative of HGG (Lamin™, Sigma), Pal-GHK and Pal-GKH (Sederma), lipospondin (N-Elaidoyl-KFK) and its conservative substitution analogues, N-Acetyl-RKR-NH2(CK+ Peptide), Pal-KavaK, Pal-K[3AlaK, Pal-KAbuK, Pal-KAcaK, Pal-KMO2K (Matrixyl®synthe'6®, Sederma), Pal-KVK (Syn-Coll™ ' DSM), N-Biot-GHK (Sederma) and their derivatives.

[0104] Also relevant here are the anti-aging tripeptides of general formula X-Pro*-Pro*-Xaa-Y described in application WO2015 / 181688, with Xaa selected from Leu, Arg, Lys, Ala, Ser, and Asp at the N-terminal end, X selected from H, -CO-Ri, and -SO2-Ri at the C-terminal end, and Y selected from OH, ORi, NH2, NHRi, or NRi R2, Ri, and R2 being independently selected from an alkyl, aryl, aralkyl, alkylaryl, alkoxy, or aryloxy group, which may be linear, branched, cyclic, polycyclic, unsaturated, hydroxylated, carbonyl, phosphorylated, and / or sulfur-containing, said group having in its backbone a heteroatom, in particular O, S, and / or N, and Pro* corresponding to Proline, an analog, or a derivative thereof. ;including, for example, Myr-PPL-OH and Myr-PPR-OH. Also relevant here are the pro-pigmenting and / or pro-collagen dipeptides and tripeptides of general formula X-(Xaai)n-Pro*-Xaa2-Y described in application WO2014 / 080376, where n=0, 1 or 2, Xaai is a hydrophobic amino acid selected from Ala, Val, Met, Leu, Iso, Phe, Pro, and their analogues or derivatives; or a polar amino acid selected from Ser, Thr, Tyr, Asp, Glu, and their derivatives and analogues; and where n=2, the two Xaai amino acids may be identical or different; Xaa2 is a hydrophobic amino acid selected from Ala, Val, Met, Leu, Iso, Phe, and their analogues or derivatives; a basic amino acid chosen from Arg, Lys, His, and derivatives and analogues thereof; at the N-terminal end of the peptide, X is chosen from H, -CO-Ri and -SO2 -Ri;at the C-terminal end of the peptide, Y is chosen from OH, ORi, NH2, NHRi or NRiR2, Riet R2 being, independently of each other, chosen from an alkyl, aryl, aralkyl, alkylaryl, alkoxy, saccharide and aryloxy group, which may be linear, branched, cyclic, polycyclic, unsaturated, hydroxylated, carbonyl, phosphorylated and / or sulfur-containing, said group being able to possess in its skeleton a heteroatom in particular O, S and / or N; Pro* corresponding to Proline, an analogue or a derivative thereof; including for example the peptides Pal-SPR-OH, Pal-PPR-OH, Pal-QPA-OH, Pal-LPA-OH, Myr-SPA-OH, Pal-PM-OH, Pal-PA-OH and Pal-PP-OH.

[0105] Tetrapeptide derivatives that can be used in the context of the present invention include, but are not limited to, Ela-KTAK (SEQ ID NO: 21), Ela-KAYK (SEQ ID NO: 22), Ela-KFYK (SEQ ID NO: 23) or Pal-KTFK (SEQ ID NO: 24).

[0106] Usable pentapeptide derivatives include, but are not limited to, Pal-KTTKS (SEQ ID NO: 4) (MATRIXYL™, Sederma), Pal-KTSKS (SEQ IS NO: 5), Pal-YGGFXaa (SEQ ID NO: 25) with Xaa being Leu or Pro, or mixtures thereof.

[0107] Usable hexapeptide derivatives include, but are not limited to, Pal-HLDIIXaa (SEQ ID NO: 26) with Xaa being Trp, Phe, Tyr, Tic, 7-hydroxy-Tic or Tpi, Pal-GKTTKS (SEQ ID NO: 27), Pal-VGVAPG (SEQ ID NO: 28) (DERMAXYL™, marketed by Sederma).

[0108] The preferred compositions available commercially and offered by Sederma include:

[0109] - tripeptides or derivatives include: Biopeptide-CL™, Maxi-Lip™, or Procapil™ containing GHK;

[0110] - a tetrapeptide or derivative includes: Crystalide™, which contains Pal-KTFK (SEQ ID NO: 24) conveyed (solvated in microemulsion)

[0111] - pentapeptides or derivatives such as Matrixyl™ source of Pal-KTTKS (SEQ ID NO: 4).

[0112] We can also mention:

[0113] - the mixture Pal-GHK and Pal-GQPR (SEQ ID NO: 2) (Matrixyl™ 3000), and

[0114] - the mixture Pal-GHK and Pal-VGVAPG (SEQ ID NO: 27) (Biobustyl™).

[0115] The following commercial peptides may also be mentioned as additional active ingredients:

[0116] - Vialox™ (INCI name = Pentapeptide-3 (synthetic peptide comprising alanine, arginine, isoleucine, glycine and proline), Syn-ake™ (|3-Ala-Pro-Dab-NH-Bzl) or Syn-Coll™ (Pal-Lys-Val-Lys-OH) sold by Pentapharm,

[0117] - Argireline™ (Ac-Glu-Glu-Met-Gln-Arg-Arg-NH2 (SEQ ID NO: 29) (INCI Name = Acetyl hexapeptide-3), Leuphasyl™ (Tyr-D-Ala-Gly-Phe-Leu (SEQ ID NO: 30)), Aldenine™ (Gly-His-Lys), Trylagen™ (INCI Name = Pseudoalteromonas Ferment Extract, Hydrolyzed Wheat Protein, Hydrolyzed Soy Protein, Tripeptide-10 Citrulline (product of the reaction of citrulline and Tripeptide-10 (synthetic peptide made up of aspartic acid, isoleucine and lysine)), Tripeptide-1), Eyeseryl™ (Ac-[3-Ala-His-Ser-His (SEQ ID NO: 31)), Serilesine™ (Ser-Ile-Lys-Val-Ala-Val (SEQ ID NO: 32)) or Decorinyl™ (INCI name: Tripeptide-10 Citrulline = product of the reaction of Citrulline and Tripeptide-10 (synthetic peptide made up of aspartic acid, isoleucine and lysine) sold by the company Lipotec,

[0118] - Collaxyl™ (Gly-Pro-Gln-Gly-Pro-Gln (SEQ ID NO: 33)) or Quintescine™ (Cys-Gly) sold by the company Vincience,

[0119] - Cytokinol™LS (casein hydrolysate) sold by Laboratoires Serobiological / Cognis,

[0120] - Kollaren™ (Gly-His-Lys), TIP2000™ (Pal-Val-Tyr-Val) or Meliprene™ (INCI name = Monofluoroheptapeptide-1: product of the reaction of acetic acid and a synthetic peptide containing arginine, glycine, glutamic acid, histidine, norleucine, p-fluorophenylalanine and tryptophan) sold by the European Institute of Cell Biology;

[0121] - Neutrazen™ (Pal-His-D-Phe-Arg-NH2) sold by Innovations; or

[0122] - the B ONT-L-Peptide™ (INCI Name = Palmitoyl Hexapeptide-19: product of the reaction of palmitic acid and Hexapeptide-19 (synthetic peptide made up of asparagine, aspartic acid, lysine and methionine), Timp-Peptide™ (INCI name = Acetyl Hexapeptide-20: product obtained by acetylation of Hexapeptide-20 (synthetic peptide made up of alanine, glycine, lysine, valine and proline) or ECM Moduline™ (INCI name = Palmitoyl Tripeptide-28: product of the reaction of palmitic acid and Tripeptide-28 (synthetic peptide made up of arginine, lysine and phenylalanine) sold by the company Infinitec Activos.

[0123] It is also conceivable to combine the invention with one or more cyclic peptides in particular those extracted from linseed oil described in the Applicant's patent application WO2019 / 149450.

[0124] The peptide(s) according to the invention or the composition containing them may be combined with at least one additional hair care ingredient, preferably with at least one of the following compounds selected from surfactants, including non-ionic surfactants, amphoteric surfactants and cationic surfactants, vitamin B3 compounds, compounds such as niacinamide or tocopherol, retinoid compounds such as retinol, hexamidine, alpha-lipoic acid, resveratrol or DHEA, hyaluronic acid, peptides, including N-acetyl-Tyr-Arg-O-hexadecyl, Pal-VGVAPG (SEQ ID NO: 27), Pal-KTTKS (SEQ ID NO: 4), Pal-KTSKS (SEQ IS NO: 4), Pal-PP, Pal-GHK, Pal-KMO2K and the Pal-K(P)HG (MATRIXYLMorphomics™, marketed by Sederma) which are classic active ingredients used in topical cosmetic or dermo-pharmaceutical compositions.

[0125] According to yet another object, the present invention proposes the use of at least one peptide according to the invention as an active ingredient in the preparation of a cosmetic composition to preserve and / or improve the general condition of the hair and / or body hair.

[0126] A composition according to the invention can be applied to the face, body, décolletage, scalp, hair, eyelashes, body hair, in any form or vehicle known to those skilled in the art, in particular in the form of a solution, dispersion, emulsion, paste or powder, individually or premixed, or be delivered individually or premixed by vectors such as macrocapsules, microcapsules or nanocapsules, macrospheres, microspheres, or nanospheres, liposomes, oleosomes or chylomicrons, macroparticles, microparticles or nanoparticles, macrosponges, microsponges or nanosponges, microemulsions or nanoemulsions, sequestrants or adsorbed on powdered organic polymers, talcs, bentonites, spores or exines and other mineral or organic supports.

[0127] Hair care compositions may be in various forms, including hair conditioners, hair straightening formulations, smoothing and curling products, perms, hair shampoos, pre-shampoo conditioners, conditioners, lotions, leave-on shampoos, styling products, leave-in hair products, waterless products, emulsions, 2-in-1 foaming emulsions, creams, masks, aerosol or non-aerosol foams, sprayable emulsions, emulsifier-free products, aqueous or oily sprays, serums, gels, gentle sulfate-free formulations, silicone-free formulations, products containing pigments, shower products, or coloured cosmetics such as mascaras and colour formulations.

[0128] These hair care compositions comprising at least one peptide according to the invention may include various other ingredients known to those skilled in the art, such as, for example and without being exhaustive, cleansing agents, surfactants, revitalizing agents, styling agents, anti-dandruff agents, sequestering or complexing agents (EDTA and its salts), stabilizing agents, pearlescent and opacifying agents;plasticizers or coalescing agents, gelling agents, emollients, acidifying or alkalizing agents, hair growth promoters, anti-hair loss agents, perfumes, essential oils, polymers, proteins or derivatized proteins, silicones, ceramides, sun protection compounds (filters), pigments, moisturizers, antioxidants, co-emulsifiers, film-forming agents, alpha-hydroxy acids, hair dyes, detergents, thickening agents, coating agents, hair conditioning agents, texturizing agents, antiseptics, preservatives, and surfactants.

[0129] By “conditioning agent” is meant a hair care product for revitalizing hair by modifying the frictional and / or mechanical properties of hair.

[0130] Conditioning agents can be applied to hair when it is wet, for example during a shower, or when the hair is dry. Most often, the term refers to the former. Hair conditioning ingredients are generally applied from a formulation comprising the conditioning ingredients in combination with a number of lipophilic ingredients.

[0131] Hair care compositions are prepared according to methods known to those skilled in the art. The vehicle or excipient supporting the formulation may be water, oil, or a powder, depending on the final purpose of the formula: for example, if it is a shampoo, it may be water; for other formulations, an oil is preferred: such as vegetable oils (coconut, argan, jojoba, olive, sunflower, etc.), mineral oils, animal oils, or synthetic oils. Synthetic esters, such as C12-15 Alkyl Benzoate, may also be used as an excipient. Liquid fatty alcohols, liquid fatty esters, solid fats, and in particular waxes, solid fatty esters, and solid alcohols may also be used as a carrier.

[0132] The present invention covers a method of topical cosmetic, non-therapeutic treatment for the preservation and improvement of the appearance and general condition of hair, in particular to induce and / or stimulate the growth of hair, body hair, eyelashes, and eyebrows, protect their structure, slow their loss, prevent their depigmentation and / or induce their pigmentation, comprising the topical application to the hair, body hair, eyelashes and / or eyebrows, in a subject who needs it, of an effective amount of at least one peptide according to the invention or of a composition comprising it, the peptides being as defined above.

[0133] The present invention also proposes a hair treatment method comprising applying to the hair a composition comprising at least one peptide according to the invention and optionally rinsing this composition. The method consists of applying an effective amount of at least one peptide according to the invention to the hair and / or body hair requiring it.

[0134] The "effective" amount depends on various factors, such as age, the person's condition, the severity of the disorder, and the method of administration. An effective amount means a non-toxic quantity sufficient to achieve the desired effect.

[0135] According to other features, the cosmetic treatment process according to the invention can be associated with one or more other treatment processes targeting hair and body hair, such as light therapy, heat or aromatherapy treatments.

[0136] According to the invention, it is possible to propose multi-compartment devices or kits intended for the implementation of the process described above, and which could include, by way of example, and without limitation, in a first compartment the active ingredient according to the invention and in a second compartment an additional excipient and / or active ingredient, the compositions contained in said first and second compartments being considered herein as a combination composition for simultaneous, separate or spread-out use in particular in one of the treatments defined above.

[0137] By way of example, for a cosmetic facial treatment, the European Cosmetics Directive has set a standard application quantity of 2.72 mg / cm² / day / person for a cream and 0.5 mg / cm² / day / person for a body lotion. DETAILED DESCRIPTION

[0138] The present invention will be better understood in the light of the following description of an example of embodiment and in vitro and ex vivo tests.

[0139] 1. Example of the preparation of an active ingredient according to the invention and of a composition including

[0140] The peptides according to the invention can be obtained, for example:

[0141] - by conventional chemical synthesis, in solid phase or in homogeneous liquid phase,

[0142] - by enzymatic synthesis from the constituent amino acids or their derivatives,

[0143] - by fermentation of a bacterial strain, modified or not by genetic engineering, To produce the desired sequences or their various fragments, either by extraction of proteins of animal or plant origin, preferably plant, followed by controlled hydrolysis which releases, among other peptide fragments, H-(AA)n-Pro-Arg-OH or H-Arg-Pro-(AA)n-OH. Gentle purification of the resulting hydrolysate will then allow collection of the desired peptide.

[0144] - by a biotechnological route, via a microorganism capable of producing it at less partially.

[0145] To carry out the invention, it is possible either to extract the proteins concerned first and then hydrolyze them, or to perform the hydrolysis first on a crude extract and then purify the peptide fragments. The hydrolysate can also be used without extracting the peptide fragments in question, provided, however, that the enzymatic hydrolysis reaction is stopped in time and that the presence of the peptides in question is determined by appropriate analytical means (radioactive tracing, immunofluorescence or immunoprecipitation with specific antibodies, etc.).

[0146] Other simpler or more complex processes, leading to cheaper or purer products, are easily conceivable by a person skilled in the art who knows the business of extracting and purifying proteins and peptides.

[0147] The tetrapeptide Pal-GQPR-OH (SEQ ID NO: 2) is prepared by peptide synthesis. A protected arginine derivative is attached by its side and N-terminal groups via its C-terminal acid group to a resin. The N-terminal amine group of this compound is then deprotected to react with a proline derivative in the presence of a coupling agent (e.g., DCC (diclyclohexylcarbodiimide) / NHS (N-hydroxysuccinimide) or HBTU (2-(1H-benzotriazole-1-yl)-1,1,3,3- tetramethyluronium hexafluorophosphate) / HOBT (1-hydroxybenzotriazole), then the same deprotection and coupling steps are repeated to add glutamine, glycine, and palmitic acid. The fully protected peptide is then cleaved in an acidic medium, and after precipitation, washing, and drying, the solid product palmitoyl-glycyl-glutamyl-prolyl-arginine is obtained.

[0148] To obtain the active ingredient according to the invention, approximately 500 ppm of the peptide obtained is solubilized using a surfactant, for example steareth-20, in a matrix, for example a mixture of water and glycerin. Optionally, the active ingredient can be preserved, for example with potassium sorbate and / or chlorhexidine digluconate. 2. Examples of cosmetic formulas

[0149] Various cosmetic formulations are described below, containing the ingredient according to the invention, in particular as formulated in the active ingredient described in point 1 above.

[0150] In the examples of cosmetic formulas described below, the active ingredient according to the invention is RIGIN™ (marketed by Sederma) comprising Pal-GQPR-OH (SEQ ID NO: 2) according to the invention with a surfactant and a water-glycerin matrix.

[0151] This ingredient is recommended in a composition at a concentration of 1% to 10%, preferably between 1% and 5%, and even more preferably at 3%. It is understood that these concentrations could vary without departing from the scope of the present invention, depending on the desired effects, whether more or less pronounced.

[0152] Examples of formulation are described below. Additional active ingredients may support and / or complement the activity of the active ingredient according to the invention. These ingredients may be of any category depending on their function(s), the area of ​​application (body, face, neck, chest, hands, etc.), the desired end effect, and the target consumer. Example 1#: Shampoo

[0153] [Tables 1] Raw Materials % Name INC! Phase A Aqua QSP Water Potassium Sorbate MO Potassium sorbate Phase B Sodium laureth sulfate 8 AO Sodium laureth sulfate Microcee® Emettent DCP 5.00 Pentylene Glycol (and) Caprylic / Capric Triglyceride (and) Decyfene Glycol Crucdatera™ CAB 30 1.50 Aqua (and) Coesimdol Betaine Phase C Water 1.50 Aqua / Water Lactic Acid 0.50 Lactic Acid Phase D Active ingredient as indicated 3.00 Aqua (and) Qb / cerin (and) Steareth-20 (and) Paimitoÿl TeSrapep8d&-7 Phase E Sodium Chloride 3.00 Sodium Chloride Operating procedure

[0154] Weigh phase A and homogenize. Add the ingredients of phase B one after the other to phase A while stirring. Homogenize. Weigh phase C and homogenize. Add phase C to phase A+B while stirring. Add phase D to phase A+B+C while stirring. Add phase E to phase A+B+C+D while stirring. Examples of additional active ingredients#:

[0155] Apiscalp™: active ingredient marketed by Sederma, to combat itching, dryness and hyperseborrhea of ​​the irritated scalp (added to part D).

[0156] Zinc Pyrithione: anti-dandruff agent (added to part A). Example 2#: Stimulating hair oil

[0157] [Tables2] Raw materials % Name INCI Phase A OP QSP Ethylhexyi Patate Crodanjd™ A8 10.00 C12-15 Alkyl Benzoate Crodairoi™ STS 5.G0 PFG-3 Benzyi Ether Croda^ JPiS 5.00 Isopropyi issstesrate Phenoxyethsnci 8.8 PhenoxyethanQl Di Alpha Toœpheroi 0.2 Di Alpha Tocopheroi Phase B 10GTIS 15.00 PEG-20 Glyceryl Thisostearate •Pentyfené Glycd 3.G0 PsWfene Glycd Artasoive^ DM1 PC 2.50 Dimethyl issKarbide active ingredient according to i'imenfon 3.G0 Aqua (and) Glycem (and) Steareth-20 (and) Palmiioyl Tetrapeptide-7 Operating procedure

[0158] Weigh phase A and homogenize. Weigh phase B and homogenize. Add phase B to phase A while stirring, and homogenize. Add part C to part A+B and homogenize. Examples of additional active ingredients#:

[0159] Crodabond™ CSA (INCI: Hydrogenated Castor Oil / Sebacic Acid Copolymer): active ingredient sold by Croda, which seals raised cuticles (outermost layer of the hair shaft) and repairs split ends (added to part B).

[0160] Phytolea™ Baobab EC (INCI: Adansonia Digitata Seed Oil): active ingredient sold by Crodarom, regenerating and antioxidant thanks to its content of fatty acids and vitamins E and A.

[0161] Seatons Coconut Oil (INCI: Cocos Nucifera (Coconut) Oil): active ingredient marketed by Croda, for immediate hair hydration with a smooth and silky feel (added to phase A).

[0162] Apiscalp™ (INCI: Caprylic / Capric Triglyceride (and) Apium Graveolens (Celery) Seed Extract): active ingredient marketed by Sederma, to combat itching, dryness and hyperseborrhea of ​​the irritated scalp. Example 3#: Hair Tonic

[0163] [Tables3] Raw materials % Name JNCI Phase A Deionized water q.s. Aqua / Water Akwi 20.00 Alcohol Phase B Butylene Glycol 200 Butylene Glycol Phenoxyethanol q.s. Phenoxyethanol Phase C Tween7** 20 1.50 Pdysorbate 20 Phase D Active ingredient according to Bweafcn Aqua (and) Glycel (and) Steareth-20 (and) Pat Mytoyl Tetrapeptide-7 Operating procedure

[0164] Weigh phase A. Weigh and melt phase B. Add phase B to phase A while stirring and homogenize. Add part C to part A+B and homogenize. Add part D to part A+B+C while stirring. Homogenize. Example 4#: Sulfate-free solid shampoo

[0165] [Tableaux4] Matières premières % Nom INC! Phase A Crodastâc® LS30 2£W (and) Sodium Lauro^ Sarcosinsré Phytofoam™ 5,00 Aqua (and) Acacia Concinrsa Fruit Extract (and) Balanites Aegyptiaca Fruit Extract (and) Gypsophite Panicuiata Roct Extraets Peréytene Glycoi 3,00 Pentytene Glycoi .Ahas^ve”* DM! PC 2.50 Dirée&yi isosorbide Ph ase B OrodacGr"* CS90 TO.QO Céteary! Aîtaol Crodazoscft7'* DBQ 2,00 Quateenium-Sf (and) Cetrimonium Mettaulfete (and) Ceteary! Afeohoi Syncrows*™ HRC 2,00 Titehemn Phase C ingrédient actif séton F invention 3,00 Aqüa (and) Glycerin (and) Sfea:reth-20 (and) Patmilo^ Tefepeptide-7 Phase D Kaoün QSP Kaolin Mode opératoire

[0166] Weigh phase A and homogenize. Heat phase A to 75°C in a water bath. Weigh phase B. Heat phase B to 75°C in a water bath. Add phase C to phase A while stirring, still in the water bath. Add phase B to phase A+C while stirring. Add phase D to phase A+B+C and homogenize. Pour into the mold immediately. Examples of additional active ingredients#:

[0167] Matcha Tea Extract™ (INCI: Glycerin (and) Water (and) Camellia Sinensis Leaf Extract): active ingredient sold by Crodarom, antioxidant and purifying (added to part C).

[0168] Hairspa™ (INCI: Glycerin (and) Lactitol (and) Xylitol): active ingredient sold by Sederma, calming and moisturizing for the scalp, based on lactitol and xylitol (added to part C). Example 5#: Energizing Wax

[0169] [Tables5] Raw materials % Name INC! Phase À Crodarfi^581 AS QSP 012-15 Aikyt Benzoate OeocraftTM LP-20 17> Poksmide-8 CrodamoF' jPiS 5.00 Isopropd Isnstearate CtodarnoP” ML 4.00 Mynstyj Lactafe SpsnTM 12S 2.00 Sorbtar? isostearate CmdamaP” STS 1.00 PPG-3 Benzyl Ether Myristafe CrodazosoftTM 8DQ 1.00 Quatemium-9t (and) Cebimonium Mediumsulfate (and)Oeteaiyl; Ateohoi Phase B Pentyphene Glycoe 3.00 Pentylene Glycote ArtasdveTM DMÎ PC 2.50 Disrsethyl Is&ssrbide ■Phenoxye^æ©! 0.40 Phenoxyethane! Phase C CWolTM WTiS 15.00 PEG-20 Glyceryl Triisostearate active ingredient according to Onventon- 3.00 Aqaa (and) Giycenn (and) Steareth-20 (and) Paimitoyl Te&apepfafe-7 Operative mode

[0170] Weigh phase A and heat to 80°C in a water bath. Add phase B to phase A while stirring and without heating. Weigh phase C and mix thoroughly. When the temperature of A+B is 55°C, add phase C to A+B and mix thoroughly. Weigh and add phase D to A+B+C. When the temperature of A+B+C+D is 45°C, pour into the jars. Examples of additional active ingredients#:

[0171] NG Unsaponibialbes of Shea Butter™ (INCI: Butyrospermum Parkii (Shea) Butter (and) Butyrospermum Parkii (Shea) Butter Unsaponifiables): active ingredient sold by Sederma, restores barrier function and improves hydration (added to phase A).

[0172] Phytolea™ Cranberry EC (INCI: Vaccinium Macrocarpon (Cranberry) Seed Oil): active scalp moisturizing ingredient sold by Crodarom (added to phase A). Example 6#: Regenerating and nourishing mask

[0173] [Tableauxô] Raw materials % ta INCt Phase A Eaü defe^isée CSP Aqua / Water Potassium Sorbafe Ci a Potassium Sorbafe Phase B Ctodaœl™ CS90 460 Ceiear^ AidoM STS 460 PPG-3 Benzyi Ether htyristaie 'C^P, 100 BRO Behertrâwiwn Methosdfate (æ?d) Cl 0-40 Etaulfate (and) Cetyi atahd Crodazosofi™ DBG 7 77 Quaîemium-91 (and) Gefem&nium Me&csu&afe Z,t J t and} CetearyS .Acdhol Ceramide, 20 T Esty Phase Phase; Periyiene G^ 1$3 Periyiene Glyod Arlasdve™ M PC 2.50 ümethyl isos-stède Phenoxÿefcand Phenoxyethanoi Phase D Urâcett YeBcw 8S005-J sototon 0.1% 0.15 Aqua fend) Cl 194 Eau déwise Phase 153' Aqua / Water Sodium Hydroxide 30% 0;15 Sodium Hydroxide Phase G Mgràdiefe atif selon Firwenta 3.00 Aqua (and) Glyæhri (and) Steareth-2û (and) Pstofoyl Tetrapephde-7 Operating Mode

[0174] Weigh phase A and heat to 85°C in a water bath. Weigh phase B and heat to 90°C in a water bath. Weigh phase C and homogenize. Add phase C to phase A while stirring. Disperse phase B in phase A+C while stirring and homogenize. Add phase D to phase A+B+C while stirring, at approximately 40°C. Add phase E to phase A+B+C+D and homogenize. Add phase F to phase A+B+C+D+E and homogenize. Add phase G to phase A+B+C+D+E+F and homogenize. Examples of additional active ingredients#:

[0175] Procapil™ (INCI: Butylene Glycol (and) Water (and) PPG-26-Buteth-26 (and) PEG-40 Hydrogenated Castor Oil (and) Apigenin (and) Oleanolic Acid (and) Biotinoyl Tripeptide-1) active ingredient sold by Sederma, preventing hair loss (added to phase D).

[0176] Crodarom® Manuka Honey (INCI: Water (and) Glycerin (and) Honey Extract) active ingredient sold by Crodarom, repairer of damaged hair and fur (added to phase D).

[0177] Ceramide HO3 (INCI: Trihydroxypalmitamidohydroxypropyl Myristyl Ether): active ingredient sold by Sederma, helps repair damaged hair and promotes hydration (added to phase B).

[0178] Example 7: No-rinse infrared protective spray

[0179] [Tables7] Raw Bavaria: % NomIHCI Phase A Deionized Ea CSP Aqual Water Pdasson Serbia 039 Potassium Sorbaie Viscatess™ HPD 1 ±9 Po^uatemiurn-3? (and) Hydrogenated Pdydecene (and} Tndeceth-S fard) Aqua 1.59 Polyquatemium-70 (and) Diprapyfene Glycol Phase 8 Alcohol 5.09 Akai®) Wardrobe Glyœt 3.09 Wardrobe Glycal Ariasotee^ OMI PC 2.59 ESmethÿl Isosorbide Tween™ 20 w FWysorbate 20 Pherîaxyeihanûl w Phenaxyetharioi Phase C Deionized water Aqua / Water Scftïm oxide 30% 030 Sottes Hydroxide Phase D Vofateis™ 100 Ethyftrimoftea. Chtafe È&thacry&te / HydKJiyzed Wheat Protein oopolymer Phase E Ingredient acid' according to hnveo&n 3.00 Aqua (and) GEycedn (and) Steareth-20 (aad) Palrmtoyl Tetspeptide-7 Operating procedure

[0180] Weigh phase A. Weigh phase B. Add phase B to phase A while stirring. Weigh and add phase C to phase A+B while stirring. Add phase D to the Mix phase A+B+C while stirring. Add phase E to phase A+B+C+D while stirring, and homogenize. Examples of additional active ingredients#:

[0181] Phytessence™ Hazel Leaf (INCI: Glycerin (and) Water (and) Corylus Avellana Leaf extract): active ingredient sold by Crodarom, restoring vitality and tone to the scalp (added to phase D).

[0182] Venuceane™ (INCI: Thermus Termophillus Ferment (and) Glycerin): active ingredient sold by Sederma, preventing damage caused by UV and IR radiation (added to phase D). Example 8: Anti-graying serum

[0183] [Tables8] Raw Materials % Name JHCt Phase A Deionized Water QSP Carbomer 0.25 Carbomer Phase B Potassium Sorbate 0.40 Potassium Sorbate Phase C Deionized Water 2.00 Aqua / Water Sodium Hydroxide 30% 0.29 Sodium Hydroxide Phase D Alcohol 5.00 Alcohol Pentyfene Glycol Pentyfene Glycol AiasoEæ™ Eye PC 2.50 Dimethyl IsQsorbsde Pherroxyethanol 0.20 Pliensxyethanüi Phase E Ingredient achf .selon finverto Aqua (and) Glycen (and) Sfeareth-20 (and) ■pdmethyl Tetfapeptide-7 Operating procedure

[0184] Sprinkle the carbomer into the water and let it swell for 30 minutes. Weigh phase B. Add phase B to phase A while stirring. Weigh and add phase C to phase A+B while stirring. Add phase D to phase A+B+C while stirring. Add phase E to phase A+B+C+D and homogenize. Example of additional active ingredients#:

[0185] Neroli Floral Water™ (INCI / Water (and) Citrus Aurantium Amara (Bitter Orange) Flower Water): active ingredient sold by Crodarom, possessing calming and regenerating properties (added to phase E).

[0186] Silverfree™ (INCI: Glycerin (and) Aqua (and) Palmitoyl-dipeptide-52): active ingredient sold by Sederma, for a long-lasting hair repigmenting effect (added to phase E). 3. In vitro studies

[0187] The peptide according to the invention exhibits a number of remarkable effects, which are described below. The product tested in vitro comprises the tetrapeptide Pal-GQPR-OH (SEQ ID NO: 2) prepared according to point 1 above, dissolved in an excipient. It has shown activities that are described below.

[0188] 3.1. Protection of hair follicle stem cells 3.1.1. Collagen Protection XVII Protocol

[0189] Human HaCaT keratinocytes are cultured and then exposed to the product according to the invention. The cells are then treated with elastase in the presence of the product according to the invention. The cells are fixed and labeled with a primary antibody recognizing collagen XVII. Labeling is performed using a fluorescent secondary antibody and photographs captured under a microscope. An estimation of the cell count by DNA staining using Hoechst 33258 reagent allows for normalization of the results. Results

[0190] Variation in the amount of collagen XVII in keratinocytes. Effect of the product according to the invention compared to the control (n=18):

[0191] [Tables9] CoBagêæ.Xyil Vaisfcst (%); ssgïs^atMté Case cscontrol ffference Seat Case cantete + seat -872¾; .Relations to VSG elA >jase 15 ppm of PakGQPR + elastase +844%, p<0;85

[0192] * UAF: Arbitrary Fluorescence Units.

[0193] The results show that elastase significantly degrades collagen XVII in keratinocytes and that the product according to the invention counteracts this effect. No toxicity was observed at the tested concentrations. Conclusion

[0194] By reducing the proteolytic activity of elastase, the product according to the invention ensures the protection of collagen XVII. Collagen XVII is involved in the niche of Hair stem cells. The loss of collagen XVII causes miniaturization of the follicle, leading to hair loss.

[0195] 3.1.2. Protection from the formation of HFDPCs spheres Protocol

[0196] HFDPCs are seeded in a hanging-drop manner and stressed with interferon-γ in the presence of the product according to the invention. The drops are then transferred into the wells of a new plate. The spheres are then fixed and their sizes are determined by image analysis. Results

[0197] Variation in the diameter of HFDPC spheres stressed by interferon-γ. Effect of the product according to the invention (n>10):

[0198] [TableauxlO] Dssasèîfe des sphères de HFDPCs Variata (%) ;"signfaMé Casœnfâe Æ&ëreæcé son stressé Cas contrôle + -63.4% 1 p <ü,oi sêferesœ stressée par 29 ppm de pal-gpqr * hfehêiw-y +76,2% ;

[0199] The results show that interferon-γ inhibits the formation of HFDPC spheres, with the spheres having a smaller diameter. The results also show that the product according to the invention protects cells from the effect of interferon-γ by significantly increasing the diameter of the HFDPC spheres. No toxicity was observed at the tested concentrations. Conclusion

[0200] In the presence of a pro-inflammatory stress such as interferon-γ which induces the catagen phase, the product according to the invention has a protective effect on the formation of the spherical structure of HFDPCs, more particularly on the diameter of the spheres of the HFDPCs, allowing the proper development of hair follicles. 3.2. Hair growth and morphogenesis 3.2.1. Proliferation of HFDPCs Protocol

[0201] HFDPCs are seeded in their growth medium. After 24 hours, the culture medium is changed to a test medium, and the cells are incubated for 24 hours to acclimate to this new medium. The product according to the invention and the EdU probe are brought into contact with the cells for 24 hours. Following this contact, the cells were rinsed with a PBS solution, fixed, and then permeabilized. The EdU detection reagent was added for 30 minutes.

[0202] An estimation of the number of cells by DNA staining method using Hoechst 33258 reagent allowed the results to be normalized. Results

[0203] Variation in the proliferation of HFDPCs. Effect of the product according to the invention compared to the control case (n=4):

[0204] [Tableauxll] ProSérafon des HFDPCs Vacation Case control Wp mdePafGPQR +9.7¾; dns 15 pp m of F^-GPQR +23 J%; p<0.01 29 ppm of PafGPQR +51..8¾;

[0205] The results show that the product according to the invention significantly increases the proliferation of HFDPCs and that there is a dose effect. No toxicity was observed at the concentrations tested. 3.2.2. Hyaluronic Acid Protocol

[0206] HFDPCs are cultured until confluence is achieved in their culture medium. The cells are then brought into contact with the product according to the invention. Following this contact, the culture supernatants are quantified for their hyaluronic acid content. The cell mats are observed under a microscope to verify the absence of toxicity. A survival test and an estimation of the cell quantity using the DNA staining method with Hoechst 33258 reagent normalized the results. Results

[0207] Variation in hyaluronic acid production by HFDPCs. Effect of the product according to the invention compared to the control (n=5):

[0208] [Tables 12] Hyatafic acid Vaidion (%); signal fat content Control case of Pal-GPQR +20% dns 15 ppm of PafGPQR +34% 39 ppm of Psi-GPQR +309%; p <g,q1

[0209] The results show that the product according to the invention significantly increases hyaluronic acid synthesis by HFDPCs and that there is a dose-response effect. No toxicity was observed at the tested concentrations. 3.2.3. Gene Expression Protocol

[0210] HFDPCs are seeded in their growth medium. After 24 hours, a purge is performed in serum-free medium, and then the product according to the invention is contacted for 6 hours and 24 hours. Following this contact, the cells are lysed and their RNA extracted. After quantification of the RNA by NanoDrop spectrophotometry, reverse transcription followed by qPCR is performed to determine the expression levels of the genes of interest HAPLN1 and TGF-

[32] . The data are normalized using a housekeeping gene. The levels of expression modification relative to the solvent controls are expressed as a ratio and are calculated according to the formula: -(Ct target gene-Ct housekeeping gene) treated product target gene-Ct housekeeping gene) control t 3.2.3.1. HAPLN1 Results

[0211] Variation in HAPLN1 gene expression in HFDPCs. Effect of the product according to the invention compared to the control (n=3):

[0212] [Tables 13] HA Rats R at 24 hours Ca 5 connotes xi ,01 - Rêjw / æe 20 □pm of PsFGQPR xl.50; p<0.01

[0213] The results show that the product according to the invention significantly increases HAPLN1 gene expression in HFDPCs compared to the control. No toxicity was observed at the tested concentrations. 3.2.3.2. TGF-02 Results

[0214] Variation in TGF-

[32] gene expression in HFDPCs. Effect of the product according to the invention compared to the control (n=3):

[0215] [Tables 14] TGFf2 Ra§o R at 6 o'clock Rats R at 24 o'clock Cascoft^cié xf.OO - Réfew xî ,00 Rêfêhwe ^5- ppm of P^-GQPR xi ,48 ; p<0.05 xl,34 ; p<0.05 20 ppm of PafôQPR xl,50 ; p<0;01 xl.81 ; p<0;î)1

[0216] The results show that the product according to the invention significantly increases, compared to the control, the expression of the TGF-

[32] gene in HFDPCs. No toxicity was observed at the tested concentrations. 3.2.4. Metabolic Signaling Pathways Protocol

[0217] HFDPCs are brought into contact with the product according to the invention. Following this contact, the intracellular quantity of phosphorylated AKT and ERK proteins (denoted respectively pAKT and pERK) is evaluated using the ELIS A method.

[0218] An estimation of the total protein quantity by a BCA quantification method made it possible to normalize the results. Results

[0219] Variation in AKT and ERK phosphorylation in HFDPCs cells after 24 hours of contact. Effect of the product according to the invention compared to the control case (n=4):

[0220] [Tables 15] Replacement (%) ; sgRfcafeiiè Cas curàfèfe 15 ppin de Pai-GQPR +23% ; in 20 ppm of Paî-GQPR +46%;p <f95 3.2.5. Conclusion

[0221] The product according to the invention improves hyaluronic acid synthesis by HFDPCs, thereby ensuring good hydration of the hair follicle and scalp. Hyaluronic acid, by binding to CD44, induces phosphorylation of the AKT protein to activate the corresponding metabolic pathway.

[0222] The product according to the invention also makes it possible to induce the expression of the HAPLN1 and TGF-

[32] genes, which are linked respectively to protection against the degradation of hyaluronic acid and to the induction of phosphorylation of the ERK protein which activates the corresponding metabolic pathway.

[0223] Activating the ERK and AKT metabolic pathways allows the induction of the proliferation of HFDPCs responsible for hair growth and morphogenesis.

[0224] 3.3. Protection of hair against different types of stress

[0225] Hair follicles are exposed daily to aggressions such as psychological, inflammatory, hormonal, and oxidative stressors, etc. These stressors directly or indirectly impact their metabolism and cause hair growth and loss problems. Hair growth is arrested by induction of the catagen phase and / or by shortening of the anagen phase. These events are also correlated with a decrease in HFDPC proliferation.

[0226] Psychological stress, here represented by stress on HFDPCs caused by hydrocortisone (cortisol) or dexamethasone (a synthetic glucocorticoid), decreases HFDPC proliferation and inhibits hair growth. Furthermore, the Dexamethasone decreases the cell viability of HFDPCs and induces the catagen phase in HFDPCs.

[0227] Inflammatory stress, here represented by stress on HFDPCs by interferon-γ, induces the catagen phase in HFDPCs.

[0228] Oxidative stress, here represented by stress on HFDPCs by H2O2, causes damage to DNA, proteins and lipids, leading to graying and hair loss.

[0229] Hormonal stress, here represented by stress on HFDPCs by dihydrotestosterone, induces a shortening of the anagen phase in HFDPCs. 3.3.1. Psychological stress 3.3.1.1. Hydrocortisone 3.3.1.1.1. Proliferation of HFDPCs Protocol

[0230] HFDPCs are seeded in their growth medium. After 24 hours, the culture medium is changed to a test medium, and the cells are incubated for 24 hours to acclimate to this new medium. Then, hydrocortisone, the product according to the invention, and the EdU probe are in contact with the cells for 24 hours. The cells are rinsed with a PBS solution, fixed, and then permeabilized. The EdU detection reagent was added for 30 minutes.

[0231] An estimation of the number of cells by DNA staining method using Hoechst 33258 reagent allowed the results to be normalized. Results

[0232] Variation in the proliferation of hydrocortisone-stressed HFDPCs. Effect of the product according to the invention compared to the control case (n=4):

[0233] [Tables 16] Mïératios des HFDPCs VanatÉsn; sjgrôlrôatDitê ; sigafcafeiié Control case Refers,'^ nœ susses Control case * hydrocortwræ -29.9%; pot R'etawse stressed at 10 ppm of PaFGQPR * hytoudisons; p< û 01 15 ppm of Psl-GQPR * hj^Qcorôsone +3897%: 3.3.1.1.2. Hyaluronic acid Protocol

[0234] A protocol equivalent to that described in point 3.2.2. is carried out with some modifications: when the product according to the invention was brought into contact with the HFDPCs cells, the cells also received hydrocortisone. Results

[0235] Variation in hyaluronic acid production by hydrocortisone-stressed HFDPCs. Effect of the product according to the invention compared to the control (n=5):

[0236] [Tables 17] Hyalsawsqae acid (sg / W^eth Vasafen (%); ssgrsScaLity Variation {%): sjgnfcafeitê Case œo&Ss. Reference good susses Case control + hytacrfisone. -5S%; pOAL Reference stressed at f / îydtaætrscrîe 20 ppm of Pal-GQPR + hydrocoriisorse

[0237] The results show that the product according to the invention significantly increases hyaluronic acid synthesis by HFDPCs when stressed by hydrocortisone. No toxicity was observed at the tested concentrations. 3.3.1.2. Dexamethasone 3.3.1.2.1. Proliferation of HFDPCs Protocol

[0238] The protocol is equivalent to that above for hydroxycortisone (see paragraph 3.3.1.1.1.), only the stress molecule used is different: hydroxycortisone is replaced by dexamethasone. Results

[0239] Variation in the proliferation of dexamethasone-stressed HFDPCs. Effect of the product according to the invention compared to the control case (n=4):

[0240] [Tables 18] Differentiation of HFDPCs Variation; sensitivity Control case Stressed reference Case against dexamethasone. -30.3% Stressed reference to dexamethasone W ppm of P-GQPR + dexamethasone +86.9%; p<0.00; 45 ppm of P-GQPR + dexamethasone +138.5%; p <w1

[0241] The results show that the product according to the invention significantly increases the proliferation of HFDPCs when stressed by dexamethasone and that a dose-response effect exists. No toxicity was observed at the tested concentrations. 3.3.2. Inflammatory stress 3.3.2.1. Interferon-γ 3.3.2.1.1. Proliferation of HFDPCs Protocol

[0242] The protocol is equivalent to that above for hydroxycortisone (see paragraph 3.3.1.1.1.), only the stress molecule used is different: hydroxycortisone is replaced by interferon-γ. Results

[0243] Variation in the proliferation of HFDPCs stressed by interferon-γ. Effect of the product according to the invention compared to the control case (n=4):

[0244] [Tables 19] Pfcærafon des HFDPCs Variation (%) ; significance Variafcn ; significance Control case Reference rmsfessée Control case + Ènîesféron-y -40..9%, p <û,0l revers® stressée à w ppm de p^-gqpr + +146,5% ; 15 * +322,6% p<6,01

[0245] The results show that the product according to the invention significantly increases the proliferation of HFDPCs when stressed by interferon-γ and that a dose-response effect exists. No toxicity was observed at the tested concentrations. 3.3.2.1.2. Hyaluronic acid Protocol

[0246] A protocol equivalent to that described in point 3.2.2. is carried out with some modifications: when the product according to the invention was brought into contact with the HFDPCs cells, the cells also received interferon-γ. Results

[0247] Variation in hyaluronic acid production by interferon-γ-stressed HFDPCs. Effect of the product according to the invention compared to the control (n=5):

[0248] [Tables20] Adde hy^üKsniçje [sg / liMh Vacation (¾) : sgnfefcité Væiata ; signicafoité Cas œntràle Ré^rerse ssesséa Cas contrôle ♦ interferon-γ -35%; pO.Of Reference stressed at γhwérefi-γ 29 ppm of Pai-GQPR + interferon-γ +72% ; pWi

[0249] The results show that the product according to the invention significantly increases hyaluronic acid synthesis by HFDPCs when stressed by interferon-γ. No toxicity was observed at the tested concentrations. 3.3.2.1.3. TGF-02 Protocol

[0250] A protocol equivalent to that described in point 3.2.3 is carried out with some modifications: when the product according to the invention is brought into contact with the HFDPCs cells, the cells also receive interferon-γ. Results

[0251] Variation in TGF-γ2 gene expression in interferon-γ-stressed HFDPCs after 6 hours (n=4) and 24 hours (n=4) of contact. Effect of the product according to the invention compared to the control:

[0252] [Tables21] TGF-R RMæ R after S hours ■Ratio R ^Hês 24 hours Stressed control case Stressed control case + irderSæn-y »0.18 ; Stressed reference xô.43 ; Stressed reference 10 ppm of Pal-GQPR xi.38..; pOXH xi.35 ; p <ü;d5

[0253] The results show that the product according to the invention significantly increases TGF-

[32] gene expression in HFDPCs when they are stressed by interferon-γ. This counteracts the effect of inflammatory stress, which inhibits TGF-

[32] gene expression in HFDPCs. No toxicity was observed at the tested concentrations. 3.3.3. Oxidative Stress 3.3.3.1. Proliferation of HFDPCs Protocol

[0254] The protocol is equivalent to that above for hydroxycortisone (see paragraph 3.3.1.1.1.), only the stress molecule used is different: hydroxycortisone is replaced by H2O2. Results

[0255] Variation in the proliferation of HFDPCs stressed by H2O2. Effect of the product according to the invention compared to the control case (n=4):

[0256] [Tables22] of HFDPCs Vadato (%) ; 5igr <æafeité variait f%) ; sigæitatmié casconiral-e règre îc® non stressée cas confrôte * ha référence à wa 10 ppm.de p^-gqpr +151,1% ;p<01 15 ppm de p®i-gqpr +322,8% p<û1

[0257] The results show that the product according to the invention significantly increases the proliferation of HFDPCs when stressed by H2O2 and that a dose-response effect exists. No toxicity was observed at the tested concentrations. 3.3.4. Hormonal stress 3.3.4.1. Proliferation of HFDPCs Protocol

[0258] The protocol is equivalent to that above for hydroxycortisone (see paragraph 3.3.1.1.1.), only the stress molecule used is different: hydroxycortisone is replaced by dihydrotestosterone. Results

[0259] Variation in the proliferation of HFDPCs stressed by dihydrotestosterone. Effect of the product according to the invention compared to the control case (n=4):

[0260] [Tables23] Prdfetos of HFDPCs Vagftn; signtatMîé Variation Side case no stressed Side case + -25.3%; pO.OI Weresæ Ceased at 10 ppm of Pai-GQPR * dshydrûfestosterone +144.5%: p <g,q1 15 pptrs de psfgqpr + +271,6% ; po,û1

[0261] The results show that the product according to the invention significantly increases the proliferation of HFDPCs when stressed by dihydrotestosterone and that a dose-response effect exists. No toxicity was observed at the tested concentrations. 3.3.5. Conclusion

[0262] The product according to the invention protects the hair follicle from the various stresses encountered daily by significantly increasing the proliferation of HFDPCs, the gene expression of TGF-

[32] and the synthesis of hyaluronic acid in HFDPCs, all responsible for the growth and morphogenesis of hair and / or scalp hair. 3.4. Protection of the extracellular matrix 3.4.1. Fibroblasts Protocol

[0263] Normal human fibroblasts are cultured to confluence and then brought into contact with the product according to the invention. Following this contact, the culture supernatants and cell mats are analyzed for their collagen, hyaluronic acid, fibronectins and laminins were analyzed using ELISA-type kits. An estimation of the cell quantity using the DNA staining method with Hoechst 33258 reagent was used to normalize the results. 3.4.1.1. Collagen I and Collagen IV Results

[0264] Variation in the production of collagen I (n=5) and collagen IV (n=5) by fibroblasts. Effect of the product according to the invention compared to the control:

[0265] [Tables24] Cotagen 1 Vata (%); siccativity Collagen IV (ngWcetl) Vanato (%); stgnteWé Case control Ré-Srejx» 12 ppm of Psi-GQPR *67%; 15 ppm of P^-GQPR +113%; p <ds31 +39% ;

[0266] The results show that the product according to the invention significantly increases the synthesis of collagen I and collagen IV by fibroblasts, essential components of the ECM, and that there is a dose-response effect. No toxicity was observed at the concentrations tested. 3.4.1.2. Hyaluronic acid Results

[0267] Variation in hyaluronic acid production by fibroblasts. Effect of the product according to the invention compared to the control (n=5):

[0268] [Tables25] Hyaliswsqye acid (rçg / Vanahon (¾); ssgptetMîé Cas control 12 ppm of Pel-GQPR 15 ppm of Pai-GQPR

[0269] The results show that the product according to the invention significantly increases the synthesis of hyaluronic acid by fibroblasts and that there is a dose-response effect. No toxicity was observed at the concentrations tested. 3.4.1.3. Fibronectin Results

[0270] Variation in fibronectin production by fibroblasts. Effect of the product according to the invention compared to the control (n=5):

[0271] [Tables26] Fsbonecfee Vasistas (%); sgn^cafeilé Control case Refers to 12 ppm of P^-GQPR +37%; 15 ppm 'of PafGQFR +63%;

[0272] The results show that the product according to the invention significantly increases fibronectin synthesis by fibroblasts and that there is a dose-response effect. No toxicity was observed at the tested concentrations. 3.4.1.4. Laminates Results

[0273] Variation in laminin production by fibroblasts. Effect of the product according to the invention compared to the control (n=5):

[0274] [Tables27] Blade? (n^Wcelfj; ssg^iUcsfeité Confeôle case 12 ppm of PafQQFR +45%; 15 ppm of PafGQPR +47%: pO.0-1

[0275] The results show that the product according to the invention significantly increases the synthesis of laminins by fibroblasts. No toxicity was observed at the concentrations tested. 3.4.2. Keratinocytes Protocol

[0276] Normal human keratinocytes are cultured until a confluent mat is obtained. At this stage, they are exposed to the product according to the invention for 24 hours, then the mats are irradiated with UVB and exposed again to the product according to the invention for 24 hours. The amount of IL-6 synthesized is measured in the culture supernatants by ELISA assay.

[0277] An estimation of the cell quantity by the DNA staining method using Hoechst 33258 reagent allowed for normalization of the results. Results

[0278] Variation in IL-6 production by UVB-irradiated and non-irradiated keratinocytes. Effect of 15 ppm Pal-GQPR compared to control (n=2):

[0279] [Tables28] Certainly not irradiated O(p§ / Wcea) CeButes irradiated with UVB ILS (pg / eye) Control case Reference Radiated Reference to irradiated Variation (%) compared to the control case 27% 48%

[0280] The results show that the product according to the invention strongly reduces IL-6 production by UVB-irradiated and non-irradiated keratinocytes. No toxicity was observed at the tested concentration. 3.4.3. Melanocytes 3.4.3.1. Melanin Protocol

[0281] Normal human cutaneous melanocytes (NHM) are cultured and in contact with the product according to the invention for 10 days. Following this contact, the cell mats are broken down and the melanin is extracted from the cells. The amount of melanin is evaluated by spectrophotometry at 490 nm, using a standard curve previously established from a melanin solution. A protein assay using the bicinchoninic acid (BCA) method is used to estimate the number of cells in order to homogenize the data obtained. Results

[0282] Variation in melanin production by melanocytes. Effect of the product according to the invention compared to the control (n=4):

[0283] [Tables29] 1 Weli) Variates; sigs fefefité Joint case Reference 15 pptn of Psl-GQPR +18%; p<0.01 23 ppm of Paf GQPR +31%;p<(Wi 30 ppm of P^-GQPR +45^:.^.01

[0284] The results show that the product according to the invention significantly and in a dose-dependent manner increases melanin synthesis by melanocytes. No toxicity was observed at the concentrations tested. 3.4.3.2. Tyrosinase activity Protocol

[0285] Normal human cutaneous melanocytes (NHM) are cultured and contacted for 10 days with the product according to the invention. At the end of the contact period, the cell mats are broken down and tyrosinase is extracted from the cells. Its dopa-oxidase activity is evaluated using the substrate L-DOPA at 37°C. The absorbance due to dopaquinone production is measured at 490 nm and converted to units activity is assessed using a pre-established range. A protein assay using the Bicinchoninic Acid (BCA) method allows for the estimation of the number of cells and thus for the homogenization of the data obtained. Results

[0286] Variation in tyrosinase activity in melanocytes. Effect of the product according to the invention compared to the control (n=4):

[0287] [Tables 30] TyKæinâse (p^WIC^cel^ Væiîto; signicsüdié Cascofi&cfe Regress 15 ppm of Psi-GQPR *is% / p <aûi 20 ppm de p^-gqpr 30 psâ-gqpr *20% :

[0288] The results show that the product according to the invention significantly increases tyrosinase activity in melanocytes. No toxicity was observed at the concentrations tested. 3.4.4. Conclusion

[0289] The product according to the invention induces the synthesis of ECM proteins in fibroblasts, allowing for better anchoring and growth of hair and / or body hair, a reduction in hair loss, and the preservation and / or improvement of the overall condition of the hair and / or body hair. The product according to the invention reduces basal or UVB-induced inflammation responsible for the early induction of the catagen phase of the hair cycle, during which the hair follicle is no longer nourished and the hair and / or body hair falls out. The product according to the invention counteracts this effect.

[0290] The product according to the invention also induces the production of melanin and tyrosinase activity in melanocytes, demonstrating pro-pigmenting activity and the resulting cosmetic use, for example, an anti-greying use of hair and / or body hair. 4. Ex vivo study

[0291] 4.1. Growth of hairs from hair follicles Protocol

[0292] Hair follicles obtained from Philpott facelift surgeries are incubated for 7 days with the product according to the invention. The medium is renewed on the second and fifth days. The length of the hair from the follicle is measured by image analysis of photographs taken on days 0, 2, 5, and 7. Results

[0293] Variation in the length of the hair emerging from the hair follicle between JO and J7. Effect of the product according to the invention compared to the control (n=12):

[0294] [Tables31] Vacation (%) ; Syndics Cas tæn&Ôte 15 de FaLGQPR +32% ; p<05

[0295] The results show that the product according to the invention significantly stimulates the hair growth originates from the hair follicle.

Claims

Demands

1. Use of at least one peptide of formula X-(Xaa)nGQPR(Xaa)mZ, wherein: - Xaa is an amino acid selected from proline (P, Pro), glycine (G, Gly), alanine (A, Ala), valine (V, Val), leucine (L, Leu) and isoleucine (I, Ile), the Xaa being selected independently of each other, with n and m being integers which may be equal or different from 0 to 5; - at the N-terminal end X is selected from H, CO-Ri, or SO2-R!; - at the C-terminal end Z is selected from OH, ORi, NH2, NHRb or NRiR2; - Ri and R2 being, independently of each other, chosen from an alkyl, aryl, aralkyl, alkylaryl, alkoxy and aryloxy group, which may be linear, branched, cyclic, polycyclic, unsaturated, hydroxylated, carbonyl, phosphorylated and / or sulfurized, said group having from 1 to 24 carbon atoms and being able to possess in its skeleton one or more heteroatoms O, S and / or N;for non-therapeutic cosmetic treatment of hair and / or body hair, including eyelashes and eyebrows.;

2. Use according to claim 1, characterized in that the hair treatment is suitable for: - Protecting the structure of hair and / or body hair, including eyelashes and eyebrows; and / or - Slowing down the loss of hair and / or body hair, including eyelashes and eyebrows; - Inducing and / or stimulating the growth of hair and / or body hair, including eyelashes and eyebrows; - Preventing depigmentation and / or inducing pigmentation of hair and / or body hair, including eyelashes and eyebrows.

3. Use according to claim 1 or 2, characterized in that the treatment is adapted to protect the stem cells of the hair follicle.

4. Use according to any one of the preceding claims, characterized in that the treatment is suitable for protecting the dermal papillae of the hair follicles.

5. Use according to any one of the preceding claims, characterized in that the treatment is suitable for preventing dry, rough, brittle, dull and / or split ends.

6. Use according to any one of the preceding claims, characterized in that Ri and / or R2 are lipophilic chains of 6 to 24 C atoms.

7. Use according to any one of the preceding claims, characterized in that X is a CO-Rp acyl group

8. Use according to any one of the preceding claims, characterized in that the group X is an acyl selected independently from among an octanoyl (C8), decanoyl (C10), lauroyl (C12), myristoyl (C14), palmitoyl (C16), stearoyl (C18), biotinoyl, elaidoyl, oleoyl and lipoyl.

9. Use according to any one of the preceding claims, characterized in that Z is chosen independently of each other from an OH or NH2 group.

10. Use according to any one of the preceding claims, characterized in that the peptide is Pal-GQPR-OH or Pal-gqpr-nh2.

11. Use according to any one of the preceding claims, characterized in that the peptide is combined with optionally one or more additional active ingredients in a physiologically acceptable medium.

12. Hair care composition comprising at least one peptide of formula X-(Xaa)nGQPR(Xaa)mZ, wherein: - Xaa is an amino acid selected from proline (P, Pro), glycine (G, Gly), alanine (A, Ala), valine (V, Val), leucine (L, Leu) and isoleucine (I, Ile), the Xaa being selected independently of each other, with n and m being integers which may be equal or different from 0 to 5; - at the N-terminal end X is selected from H, CO-Ri, or SO2-R!;

13.

14.

15.

16. - at the C-terminal end Z is chosen from OH, ORh NH2, NHRb or NRiR2; - Ri and R2 being, independently of each other, chosen from an alkyl, aryl, aralkyl, alkylaryl, alkoxy and aryloxy group, which may be linear, branched, cyclic, polycyclic, unsaturated, hydroxylated, carbonyl, phosphorylated and / or sulfurized, said group having from 1 to 24 carbon atoms and being able to possess in its skeleton one or more O, S and / or N heteroatoms; and a physiologically acceptable environment. Composition according to claim 12, further comprising at least one additional hair care ingredient. Composition according to claim 13, wherein the additional hair care ingredient is: one or more surfactant(s), vitamin B3 compounds, niacinamide, tocopherol, retinol, hexamidine, alpha-lipoic acid, resveratrol, DHEA, hyaluronic acid, ceramides, one or more peptides. Composition according to claim 14, wherein the peptide(s) may be Pal-GHK and / or Pal-PP. Composition according to claim 14, wherein the surfactant is selected from a non-ionic surfactant, an amphoteric surfactant and a cationic surfactant.