ATN-161 is a novel peptide antagonist of integrin α5β1. ATN-161 selectively binds to and blocks the receptor for integrin α5β1, thereby preventing integrin alpha5beta1 binding. This receptor blockade may result in inhibition of endothelial cell-cell interactions, endothelial cell-matrix interactions, angiogenesis, and tumor progression. It has potential antineoplastic activity.
CAT No: R0965
CAS No:262438-43-7
Synonyms/Alias:ATN-161;262438-43-7;ATN 161;Ac-PHSCN-NH2;ATN-161 free base;UNII-XW0H5LE42K;XW0H5LE42K;DTXSID60180877;L-Aspartamide, 1-acetyl-L-prolyl-L-histidyl-L-seryl-L-cysteinyl-;Acetyl-prolyl-histidyl-seryl-cysteinyl-asparaginamide;(2S)-2-(((2R)-2-(((2S)-2-(((2S)-2-(((2S)-1-ACETYLPYRROLIDINE-2-CARBONYL)AMINO)-3-(1H-IMIDAZOL-4-YL)PROPANOYL)AMINO)-3-HYDROXY-PROPANOYL)AMINO)-3-SULFANYL-PROPANOYL)AMINO)BUTANEDIAMIDE;(2S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-acetylpyrrolidine-2-carbonyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-hydroxypropanoyl]amino]-3-sulfanylpropanoyl]amino]butanediamide;(S)-2-((R)-2-((S)-2-((S)-2-((S)-1-Acetylpyrrolidine-2-carboxamido)-3-(1H-imidazol-4-yl)propanamido)-3-hydroxypropanamido)-3-mercaptopropanamido)succinamide;Ac-Pro-His-Ser-Cys-Asn-NH2;SCHEMBL2157375;CHEMBL4297456;SCHEMBL17262996;DTXCID00103368;GLXC-04869;ATN-161?;MKA43843;ATN-161 (Ac-PHSCN-NH2);262438-43-7 (free base);s8454;Alpha V Beta 1 Inhibitor ATN-161;AKOS030210988;AKOS040732486;CCG-270186;CS-3327;BS-16323;DA-71103;HY-13535;D83668;BRD-K00521308-019-01-9;(2S)-2-[(2R)-2-[(2S)-2-[(2S)-2-{[(2S)-1-acetylpyrrolidin-2-yl]formamido}-3-(1H-imidazol-4-yl)propanamido]-3-hydroxypropanamido]-3-sulfanylpropanamido]succinamide;(S)-2-((R)-2-((S)-2-((S)-2-((S)-1-acetylpyrrolidine-2-carboxamido)-3-(1H-imidazol-5-yl)propanamido)-3-hydroxypropanamido)-3-mercaptopropanamido)succinamide;
ATN 161 is a synthetic peptide derived from the synergy region of fibronectin, designed to specifically target integrin receptors, with particular affinity for integrin α5β1. As a peptide compound, ATN 161 has gained considerable attention in the biochemical research community for its ability to modulate cell adhesion, migration, and signaling pathways. Its unique sequence and integrin-binding properties make it a valuable tool for investigating extracellular matrix interactions, cellular communication, and the molecular mechanisms underlying tissue remodeling. The compound's specificity and functional activity have positioned it as a critical reagent in studies seeking to elucidate the roles of integrins in physiological and pathological processes.
Cell adhesion research: ATN 161 is widely utilized to study the molecular mechanisms of cell adhesion, particularly those mediated by fibronectin and integrin α5β1. By competitively inhibiting the binding of fibronectin to its integrin receptor, the peptide enables researchers to dissect the contribution of specific integrin-ligand interactions in cellular attachment and spreading. Such studies are fundamental for understanding how cells interact with their microenvironment, which has implications for tissue engineering, wound healing, and the regulation of cell motility.
Signal transduction studies: The peptide is an effective tool for probing integrin-mediated signaling cascades. By selectively blocking integrin engagement, ATN 161 allows for the investigation of downstream signaling events, such as focal adhesion kinase (FAK) activation, mitogen-activated protein kinase (MAPK) pathways, and cytoskeletal rearrangements. These insights are essential for mapping the complex networks that govern cell behavior, including proliferation, differentiation, and survival, in response to extracellular cues.
Angiogenesis modeling: In the context of angiogenesis research, ATN 161 serves as a functional inhibitor of endothelial cell migration and new vessel formation. Its integrin-targeting action provides a means to evaluate the role of specific cell-matrix interactions in vascular development and remodeling. Researchers employ the peptide in both in vitro and ex vivo systems to delineate the steps of endothelial cell recruitment, tube formation, and matrix invasion, contributing to a deeper understanding of the regulatory mechanisms controlling blood vessel growth.
Tumor microenvironment exploration: The use of ATN 161 extends to studies of the tumor microenvironment, where integrin-mediated signaling is known to influence cell invasion, stromal interactions, and matrix remodeling. By disrupting integrin function, the peptide allows for the assessment of how altered cell adhesion dynamics affect tumor cell behavior, tissue architecture, and the interplay between malignant and non-malignant cells. Such applications are instrumental in advancing knowledge of tumor biology and the cellular processes that drive disease progression.
Peptide-based assay development: ATN 161 is also employed in the design and validation of peptide-based assays aimed at quantifying integrin activity, screening for integrin-binding molecules, and evaluating the effects of candidate compounds on cell adhesion pathways. Its well-characterized binding specificity and functional effects make it a reliable positive control or reference standard in experimental protocols, thereby supporting the development of robust analytical and screening platforms for integrin research.
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