Hexapeptide-12 (val-gly-val-ala-pro-gly)

Hexapeptide-12 (Val-Gly-Val-Ala-Pro-Gly) contains alternating hydrophobic, flexible, and turn-inducing residues, favoring β-turn and extended-coil structures. The motif is frequently explored in dermal-matrix and extracellular-matrix interaction studies. Researchers evaluate its impact on collagen-related signaling and peptide-matrix adhesion. Applications include cosmetic-peptide research, biomaterial functionalization, and structural-motif analysis.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Hexapeptide-12 (val-gly-val-ala-pro-gly)(CAS 92899-39-3)

CAT No: R2589

CAS No:92899-39-3

Synonyms/Alias:92899-39-3;Chemotactic Domain of Elastin;Val-Gly-Val-Ala-Pro-Gly;H-Val-Gly-Val-Ala-Pro-Gly-OH;04V1QPJ5TW;2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-amino-3-methylbutanoyl]amino]acetyl]amino]-3-methylbutanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]acetic acid;Vgvapg;hexapeptide-12 (val-gly-val-ala-pro-gly);2-((S)-1-((S)-2-((S)-2-(2-((S)-2-Amino-3-methylbutanamido)acetamido)-3-methylbutanamido)Propanoyl)pyrrolidine-2-carboxamido)acetic acid;Val-gly-ala-pro-gly;UNII-04V1QPJ5TW;Valyl-glycyl-valyl-alanyl-prolyl-glycine;L-Glycine High;MFCD00133914;DERMAXYL;L-Glycine7407;L-Glycine High7408;SCHEMBL1404295;DTXSID50918909;HY-P4998;FC108662;CS-0675630;H-Val-Gly-Val-Ala-Pro-Gly-OH; H-VGVAPG-OH;Glycine, L-valylglycyl-L-valyl-L-alanyl-L-prolyl-;Q27247699;Chemotactic Domain of Elastin (H-L-Val-Gly-L-Val-L-Ala-L-Pro-Gly-OH);Glycine, N-(1-(N-(N-(N-L-valylglycyl)-L-valyl)-L-alanyl)-L-prolyl)-, (SP-4-2)-;N-[(1-{N-[2-({2-[(2-Amino-1-hydroxy-3-methylbutylidene)amino]-1-hydroxyethylidene}amino)-1-hydroxy-3-methylbutylidene]alanyl}pyrrolidin-2-yl)(hydroxy)methylidene]glycine;

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M.F/Formula
C22H38N6O7
M.W/Mr.
498.6
Sequence
One Letter Code:VGVAPG
Three Letter Code:H-Val-Gly-Val-Ala-Pro-Gly-OH

Hexapeptide-12 (val-gly-val-ala-pro-gly), also known as palmitoyl hexapeptide-12, is a synthetic peptide composed of a sequence of six amino acids. Engineered for its unique molecular structure, Hexapeptide-12 is widely recognized for its ability to interact with cellular processes related to extracellular matrix components and cell signaling pathways. Its amphiphilic nature allows for efficient integration into various research formulations, making it a versatile tool in biochemical studies and advanced material science. The peptide's sequence, derived from naturally occurring motifs, enables it to mimic certain biological activities, which has led to its adoption in a range of experimental applications. Researchers value Hexapeptide-12 for its stability, compatibility with diverse delivery systems, and its potential to facilitate investigations into cellular communication, tissue engineering, and biomimetic materials.

Cellular Signaling Research: Hexapeptide-12 is extensively utilized in cellular signaling studies to elucidate the mechanisms by which cells communicate and respond to external stimuli. By incorporating this peptide into cell culture models, scientists can observe its influence on the activation and regulation of specific signaling pathways, particularly those associated with extracellular matrix interactions. Its capacity to modulate cell behavior provides valuable insights into the molecular basis of tissue homeostasis and regeneration, supporting the development of new hypotheses regarding cell-matrix communication.

Extracellular Matrix Modeling: In the context of extracellular matrix (ECM) research, palmitoyl hexapeptide-12 serves as a model peptide for investigating peptide-matrix interactions. Its sequence allows it to mimic certain motifs found in natural ECM proteins, enabling researchers to study peptide-mediated effects on cell adhesion, migration, and matrix remodeling. By integrating this peptide into synthetic hydrogels or biomaterials, scientists can systematically analyze how such modifications influence the structural and functional properties of tissue constructs, driving innovation in the design of biomimetic scaffolds.

Biomaterials Development: The amphiphilic properties of Hexapeptide-12 make it a valuable additive in the development of novel biomaterials. It can be conjugated to polymers or incorporated into surface coatings to enhance biocompatibility and promote specific cell-material interactions. These modifications are especially relevant in the fabrication of tissue engineering scaffolds, where controlled cell attachment and proliferation are critical. By leveraging its functional attributes, materials scientists can tailor the biological performance of engineered constructs for a variety of research applications.

Wound Healing Models: In experimental wound healing models, palmitoyl hexapeptide-12 is applied to investigate its effects on cellular processes involved in tissue repair. Through in vitro and ex vivo studies, researchers examine how the peptide influences fibroblast migration, collagen synthesis, and matrix organization. These insights contribute to a deeper understanding of the molecular events underlying tissue regeneration and support the evaluation of new strategies for enhancing wound closure and recovery in laboratory settings.

Cosmetic Science Research: Hexapeptide-12 is also widely studied within the field of cosmetic science, where it is explored for its potential to modulate skin cell behavior and matrix composition. By incorporating it into experimental formulations, researchers can assess its impact on dermal fibroblast activity and extracellular matrix synthesis, providing a foundation for the development of advanced skincare prototypes. These studies advance the scientific understanding of peptide-based interventions aimed at supporting skin health and structural integrity.

Peptide-Protein Interaction Studies: The unique sequence of Hexapeptide-12 enables it to serve as a model system for probing peptide-protein interactions in a controlled research environment. By labeling or immobilizing the peptide, scientists can investigate its binding affinities with various extracellular matrix proteins or cell surface receptors, shedding light on the specificity and dynamics of peptide-mediated recognition events. These findings inform the rational design of peptide-based tools and materials for use in tissue engineering, regenerative medicine research, and molecular biology investigations, further expanding the utility of Hexapeptide-12 in scientific exploration.

InChI
InChI=1S/C22H38N6O7/c1-11(2)17(23)20(33)24-9-15(29)27-18(12(3)4)21(34)26-13(5)22(35)28-8-6-7-14(28)19(32)25-10-16(30)31/h11-14,17-18H,6-10,23H2,1-5H3,(H,24,33)(H,25,32)(H,26,34)(H,27,29)(H,30,31)/t13-,14-,17-,18-/m0/s1
InChI Key
RLCSROTYKMPBDL-USJZOSNVSA-N

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