Eyeliss is a cosmetic-research peptide blend associated with studies on microcirculation, extracellular-matrix interactions, and fluid homeostasis in skin models. Component peptides feature charged and lipophilic residues that modulate diffusion and binding to matrix proteins. Researchers evaluate its effects on capillary-mimetic systems and dermal cell cultures. Applications span cosmetic peptide screening, formulation optimization, and skin-biology research.
CAT No: R2722
CAS No:24292-52-2
Synonyms/Alias:Hesperidin methylchalcone;24292-52-2;Hesperidin methyl chalcone;EYELISS;hesperidine methylchalcone;EINECS 246-128-2;UNII-4T2GVA922X;4T2GVA922X;(E)-1-(4-((6-O-(6-Deoxy-alpha-L-mannopyranosyl)-beta-D-glucopyranosyl)oxy)-2-hydroxy-6-methoxyphenyl)-3-(3-hydroxy-4-methoxyphenyl)-2-propen-1-one;DTXSID90885262;(E)-3-(3-hydroxy-4-methoxyphenyl)-1-[2-hydroxy-6-methoxy-4-[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl]oxymethyl]oxan-2-yl]oxyphenyl]prop-2-en-1-one;HESPERIDIN METHYL CHALCONE [VANDF];HESPERIDIN METHYL CHALCONE [WHO-DD];2-Propen-1-one, 1-(4-((6-O-(6-deoxy-alpha-L-mannopyranosyl)-beta-D-glucopyranosyl)oxy)-2-hydroxy-6-methoxyphenyl)-3-(3-hydroxy-4-methoxyphenyl)-, (2E)-;2-Propen-1-one, 1-[4-[[6-O-(6-deoxy-.alpha.-L-mannopyranosyl)-.beta.-D-glucopyranosyl]oxy]-2-hydroxy-6-methoxyphenyl]-3-(3-hydroxy-4-methoxyphenyl)-, (2E)-;Chalcone, 2',3,4'-trihydroxy-4,6'-dimethoxy-, 4'-(6-O-(6-deoxy-alpha-L-mannopyranosyl)-beta-D-glucopyranoside);MFCD00010438;(E)-1-(4-((6-O-(6-DEOXY-.ALPHA.-L-MANNOPYRANOSYL)-.BETA.-D-GLUCOPYRANOSYL)OXY)-2-HYDROXY-6-METHOXYPHENYL)-3-(3-HYDROXY-4-METHOXYPHENYL)-2-PROPEN-1-ONE;(E)-3-(3-Hydroxy-4-methoxyphenyl)-1-(2-hydroxy-6-methoxy-4-((2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-((((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyltetrahydro-2H-pyran-2-yl)oxy)methyl)tetrahydro-2H-pyran-2-yl)oxy)phenyl)prop-2-en-1-one;2-PROPEN-1-ONE,1-(4-((6-O-(6-DEOXY-ALFA-L-MANNOPYRANOSYL)-.BETA.-D-GLUCOPYRANOSYL)OXY)-2-HYDROXY-6-METHOXYPHENYL)-3-(3-HYDROXY-4-METHOXYPHENYL)-, (E)-;hesperidin methyl chalone;(E)-1-[4-[[6-O-(6-Deoxy-alpha-L-mannopyranosyl)-beta-D-glucopyranosyl]oxy]-2-hydroxy-6-methoxyphenyl]-3-(3-hydroxy-4-methoxyphenyl)-2-propen-1-one;(E)-3-(3-hydroxy-4-methoxyphenyl)-1-(2-hydroxy-6-methoxy-4-((2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl)oxymethyl)oxan-2-yl)oxyphenyl)prop-2-en-1-one;SCHEMBL3452314;CHEMBL5435071;FDHNLHLOJLLXDH-JIYHLSBYSA-N;DTXCID401024653;STK801860;AKOS015895097;OH34622;HESPERIDIN METHYL CHALCONE [INCI]
Eyeliss is a proprietary peptide complex renowned in biochemical research for its multifaceted activity in modulating skin physiology and vascular function. Composed of a synergistic blend of bioactive peptides, including dipeptide-2, palmitoyl tetrapeptide-7, and hesperidin methyl chalcone, Eyeliss is designed to influence microcirculation, lymphatic drainage, and inflammatory pathways at the cellular level. Its unique peptide-driven mechanism has made it a subject of interest for studies focused on the molecular basis of tissue remodeling, capillary permeability, and peptide-mediated cellular signaling. The compound's relevance extends to investigations into the regulation of extracellular matrix components and the modulation of dermal and subdermal homeostasis, positioning it as a valuable tool in peptide science and advanced cosmetic research.
Peptide Mechanism Studies: Eyeliss serves as a robust model system for elucidating the biochemical mechanisms of action of synthetic peptides in human tissue. Researchers utilize it to investigate how peptide complexes interact with cellular receptors, modulate gene expression, and influence downstream signaling cascades. Its defined peptide composition enables the dissection of specific pathways involved in vascular tone, endothelial function, and the regulation of cytokine release, providing a foundation for understanding the broader roles of bioactive peptides in skin and vascular biology.
Vascular Permeability and Microcirculation Research: The peptide components of Eyeliss are frequently employed in studies exploring the regulation of capillary permeability and the dynamics of microvascular flow. By modulating key mediators involved in vascular stability and lymphatic drainage, the compound offers a controlled system for assessing the impact of peptide signaling on fluid homeostasis and tissue edema. Such research is critical for advancing knowledge of microcirculatory mechanisms and for developing peptide-based strategies to influence vascular health in non-clinical settings.
Inflammation Modulation Assays: The anti-inflammatory properties attributed to Eyeliss's peptide constituents make it a preferred choice for in vitro and ex vivo assays aimed at characterizing the suppression of pro-inflammatory mediators. Scientists utilize it to probe the influence of peptide complexes on the expression of interleukins, chemokines, and adhesion molecules, thereby shedding light on the molecular underpinnings of peptide-driven inflammation control. These studies are instrumental in mapping the interaction networks that govern immune cell recruitment and tissue response to environmental stressors.
Extracellular Matrix and Tissue Remodeling Studies: Eyeliss is widely used in research focused on the modulation of extracellular matrix (ECM) components, such as collagen and elastin, within dermal and subdermal models. By applying the peptide blend to cell cultures or tissue explants, investigators can monitor changes in matrix metalloproteinase activity, ECM synthesis, and tissue architecture. This application is particularly valuable for understanding the peptide-mediated regulation of tissue integrity, resilience, and repair processes in the context of skin biology.
Peptide Formulation Development: In the realm of formulation science, Eyeliss acts as a reference compound for the development and optimization of peptide-based delivery systems. Its stability, solubility, and bioactivity profiles make it suitable for evaluating encapsulation techniques, carrier compatibility, and peptide release kinetics. Formulators and researchers leverage these properties to design and test innovative delivery vehicles that maximize the functional utility of peptide complexes for research and industrial applications, while also gaining insights into the physicochemical behavior of multi-peptide systems.
By supporting a diverse range of experimental approaches, Eyeliss continues to play a pivotal role in advancing peptide research, from mechanistic studies to applied formulation science. Its multifactorial activity profile and well-characterized peptide composition provide an essential platform for scientific inquiry into the dynamic interplay between peptides, cells, and tissue microenvironments.
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