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SAMS peptide, a synthetic peptide substrate for AMPK based on the sequence around Ser79 on acetyl-CoA carboxylase, is more selective for the kinase than acetyl CoA carboxylase itself, and provides a convenient and sensitive assay for AMPK.

Peptide Inhibitors
Catalog number
CAS number
Molecular Formula
Molecular Weight
(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-(1H-imidazol-5-yl)propanoyl]amino]-4-methylsulfanylbutanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-hydroxypropanoyl]amino]propanoyl]amino]-4-methylsulfanylbutanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]-4-methylpentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-4-methylpentanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid
(Ser76, Arg86.87)-ACC-α (73-87) (dephosphorylated) (E.coli, rat); (Ser76, Arg86.87)-Acetyl-CoA Carboxylase 1 (73-87) (dephosphorylated) (E.coli, rat); (Ser77, Arg87.88)-ACC-α (74-88) (dephosphorylated) (bovine, ovine); (Ser77, Arg87.88)-Acetyl-CoA Carboxyla; H-His-Met-Arg-Ser-Ala-Met-Ser-Gly-Leu-His-Leu-Val-Lys-Arg-Arg-OH; L-histidyl-L-methionyl-L-arginyl-L-seryl-L-alanyl-L-methionyl-L-seryl-glycyl-L-leucyl-L-histidyl-L-leucyl-L-valyl-L-lysyl-L-arginyl-L-arginine
White or Off-white Lyophilized Powder
1.47±0.1 g/cm3
Store at -20°C
Soluble in Water, DMSO
InChI Key
Canonical SMILES
1.Interactions of zoospores of Ulva linza with arginine-rich oligopeptide monolayers.
Ederth T;Pettitt ME;Nygren P;Du CX;Ekblad T;Zhou Y;Falk M;Callow ME;Callow JA;Liedberg B Langmuir. 2009 Aug 18;25(16):9375-83. doi: 10.1021/la900688g.
We recently reported on the strong interactions of zoospores of the green alga, Ulva linza with an arginine-rich oligopeptide self-assembled monolayer (SAM) [Biofouling 2008, 24, 303-312], where the arginine-rich peptide induced not only high spore settlement, but also a form of abnormal settlement, or "pseudo-settlement", whereby a proportion of spores do not go through the normal process of surface exploration, adhesive exocytosis, and loss of flagella. Further, it was demonstrated that both the total number of settled spores and the fraction of pseudosettled spores were related to the surface density of the arginine-rich peptide. Here we present a further investigation of the interactions of zoospores of Ulva with a set of oligomeric, de novo designed, arginine-rich peptides, specifically aimed to test the effect of peptide primary structure on the interaction. Via variations in the peptide length and by permutations in the amino acid sequences, we gain further insight into the spore-surface interactions. The interpretation of the biological assays is supported by physicochemical characterization of the SAMs using infrared spectroscopy, ellipsometry, and contact angle measurements.
2.Holographic microscopy provides new insights into the settlement of zoospores of the green alga Ulva linza on cationic oligopeptide surfaces.
Vater SM;Finlay J;Callow ME;Callow JA;Ederth T;Liedberg B;Grunze M;Rosenhahn A Biofouling. 2015;31(2):229-39. doi: 10.1080/08927014.2015.1022534.
Interaction of zoospores of Ulva linza with cationic, arginine-rich oligopeptide self-assembled monolayers (SAMs) is characterized by rapid settlement. Some spores settle (ie permanently attach) in a 'normal' manner involving the secretion of a permanent adhesive, retraction of the flagella and cell wall formation, whilst others undergo 'pseudosettlement' whereby motile spores are trapped (attached) on the SAM surface without undergoing the normal metamorphosis into a settled spore. Holographic microscopy was used to record videos of swimming zoospores in the vicinity of surfaces with different cationic oligopeptide concentrations to provide time-resolved insights into processes associated with attachment of spores. The data reveal that spore attachment rate increases with increasing cationic peptide content. Accordingly, the decrease in swimming activity in the volume of seawater above the surface accelerated with increasing surface charge. Three-dimensional trajectories of individual swimming spores showed a 'hit and stick' motion pattern, exclusively observed for the arginine-rich peptide SAMs, whereby spores were immediately trapped upon contact with the surface.
3.Effect of a strong interfacial electric field on the orientation of the dipole moment of thiolated aib-oligopeptides tethered to mercury on either the N- or C-terminus.
Becucci L;Guryanov I;Maran F;Guidelli R J Am Chem Soc. 2010 May 5;132(17):6194-204. doi: 10.1021/ja100486y.
Four oligopeptides consisting of a sequence of alpha-aminoisobutyric acid (Aib) residues, thiolated at either the N- or C-terminus by means of a -(CH(2))(2)-SH anchor, were self-assembled on mercury, which is a substrate known to impart a high fluidity to self-assembled monolayers (SAMs). The surface dipole potential of these peptide SAMs was estimated in 0.1 M KCl aqueous solution at a negatively charged electrode, where the interfacial electric field is directed toward the metal. To the best of our knowledge, this is the first estimate of the surface dipole potential of peptide SAMs in aqueous solution. The procedure adopted consisted in measuring the charge involved in the gradual expansion of a peptide-coated mercury drop and then combining the resulting information with an estimate of the charge density experienced by diffuse layer ions. The dipole moment of the tethered thiolated peptides was found to be directed toward the metal, independent of whether they were thiolated at the C- or N-terminus. This result was confirmed by the effect of these SAMs on the kinetics and thermodynamics of the Eu(III)/Eu(II) redox couple. The combined outcome of these studies indicates that a strong interfacial electric field orients the dipole moment of peptide SAMs tethered to mercury, even against their "natural" dipole moment.

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