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N-acetyl-S-farnesyl-L-cysteine

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

N-acetyl-S-farnesyl-L-cysteine is an inhibitor of the isoprenylated protein methyltransferase.

Category

L-Amino Acids

Catalog number

BAT-008095

CAS number

135304-07-3

Molecular Formula

C20H33NO3S

Molecular Weight

367.5

IUPAC Name

(2R)-2-acetamido-3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl]sulfanylpropanoic acid

Synonyms

AFC; Ac-Cys(farnesyl)-OH; (2R)-2-acetamido-3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl]sulfanylpropanoic acid

Appearance

Yellow-red oil

Purity

≥98%

Density

1.0±0.1 g/cm3

Boiling Point

566.1±50.0 °C at 760 mmHg

Storage

Store at-20 °C

InChI

InChI=1S/C20H33NO3S/c1-15(2)8-6-9-16(3)10-7-11-17(4)12-13-25-14-19(20(23)24)21-18(5)22/h8,10,12,19H,6-7,9,11,13-14H2,1-5H3,(H,21,22)(H,23,24)/b16-10+,17-12+/t19-/m0/s1

InChI Key

XTURYZYJYQRJDO-BNAHBJSTSA-N

Canonical SMILES

CC(=CCCC(=CCCC(=CCSCC(C(=O)O)NC(=O)C)C)C)C

N-acetyl-S-farnesyl-L-cysteine (AFC) is a unique biochemical compound derived from the modification of L-cysteine, an amino acid, through the addition of an acetyl group and a farnesyl group. This compound is particularly noted for its role in the post-translational modification of proteins, specifically in the prenylation process that influences the behavior and functionality of proteins within cellular membranes. As a lipidated form of cysteine, AFC exhibits increased hydrophobicity, allowing it to anchor effectively into lipid bilayers. This functionality is crucial in various biological pathways, contributing to its significance in both natural biological processes and therapeutic applications.

The first key application of N-acetyl-S-farnesyl-L-cysteine lies in the study of protein prenylation. This process is essential for the localization and proper functioning of proteins involved in numerous cellular activities, including signal transduction and cell division. By serving as a substrate analog, AFC aids researchers in delineating the mechanisms of prenylation and its effects on protein function. Experimental models utilizing AFC can thus unravel the intricacies of diseases like cancer, where aberrant protein prenylation is often a contributing factor. AFC’s ability to modulate protein prenylation makes it an invaluable tool in biochemical research and drug development aimed at targeting dysfunctional cellular pathways.

A second application is found in the development of therapeutic agents. AFC has been investigated for its potential to inhibit the activity of enzymes like farnesyltransferases, which are pivotal in the post-translational modification of oncogenic proteins such as Ras. By inhibiting these enzymes, AFC can potentially thwart the progression of cancers driven by these proteins. Inhibitors derived from or inspired by AFC are thus significant in creating novel anti-cancer therapies, offering a targeted approach to treating malignancies linked to dysregulated prenylation processes. The development of these inhibitors underscores AFC’s role in the advancement of precision medicine.

Additionally, AFC serves an important role in the cosmetic and dermatological sectors. Due to its effect on cellular signaling and protein modification, AFC has been examined for its potential to improve skin health and treat various skin disorders. Its ability to influence the molecular pathways connected to cell aging and growth makes it a candidate for formulations aimed at enhancing skin resilience and appearance. By modulating the effects of environmental stressors on skin cells, AFC-based products can contribute to skincare solutions that target aging, dermal distress, and even conditions like psoriasis or eczema, providing a biochemical basis for beauty and health products.

Finally, AFC’s utility extends to agriculture, particularly in the development of plant growth regulators. Through its involvement in signaling pathways, AFC can influence plant growth and development, offering possibilities for enhancing crop yields and resilience to environmental stresses. These applications not only provide insights into plant biology but also help in engineering crops that can withstand adverse conditions, thus contributing to food security and sustainable agriculture practices. AFC’s multifaceted applications highlight its versatility and potential impact across various domains, from human health to agricultural innovation.

1. Isoprenylcysteine carboxyl methyltransferase activity modulates endothelial cell apoptosis

Qing Lu, Julie Newton, Kristina Kramer, Robert Bellas, Elizabeth O Harrington, Sharon Rounds, Kerri L Sheahan Mol Biol Cell . 2003 Mar;14(3):848-57. doi: 10.1091/mbc.e02-07-0390.

Extracellular ATP, adenosine (Ado), and adenosine plus homocysteine (Ado/HC) cause apoptosis of cultured pulmonary artery endothelial cells through the enhanced formation of intracellular S-adenosylhomocysteine and disruption of focal adhesion complexes. Because an increased intracellular ratio of S-adenosylhomocysteine/S-adenosylmethionine favors inhibition of methylation, we hypothesized that Ado/HC might act by inhibition of isoprenylcysteine-O-carboxyl methyltransferase (ICMT). We found that N-acetyl-S-geranylgeranyl-L-cysteine (AGGC) and N-acetyl-S-farnesyl-L-cysteine (AFC), which inhibit ICMT by competing with endogenous substrates for methylation, caused apoptosis. Transient overexpression of ICMT inhibited apoptosis caused by Ado/HC, UV light exposure, or tumor necrosis factor-alpha. Because the small GTPase, Ras, is a substrate for ICMT and may modulate apoptosis, we also hypothesized that inhibition of ICMT with Ado/HC or AGGC might cause endothelial apoptosis by altering Ras activation. We found that ICMT inhibition decreased Ras methylation and activity and the activation of the downstream signaling molecules Akt, ERK-1, and ERK-2. Furthermore, overexpression of wild-type or dominant active H-Ras blocked Ado/HC-induced apoptosis. These findings suggest that inhibition of ICMT causes endothelial cell apoptosis by attenuation of Ras GTPase methylation and activation and its downstream antiapoptotic signaling pathway.

2. Identification of prenylcysteine carboxymethyltransferase in bovine adrenal chromaffin cells

H M De Busser, A R Lagrou, G A Van Dessel Int J Biochem Cell Biol . 2000 Sep;32(9):1007-16. doi: 10.1016/s1357-2725(00)00036-4.

Chromaffin cells from bovine adrenal medulla were examined for the presence of a specific prenylcysteine carboxymethyltransferase by using N-acetyl-S-farnesyl-L-cysteine and N-acetyl-S-geranylgeranyl-L-cysteine as artificial substrates and a crude cell homogenate as the enzyme source. From Michaelis-Menten kinetics the following constants were calculated: K(m) 90 microM and V(max) 3 pmol/min per mg proteins for N-acetyl-S-farnesyl-L-cysteine; K(m) 52 microM and V(max) 3 pmol/min per mg proteins for N-acetyl-S-geranylgeranyl-L-cysteine. Both substrates were methylated to an optimal extent at the pH range 7. 4-8.0. Methylation activity increased linearly up to 20 min incubation time and was dose dependent up to at least 160 microg of protein. Sinefungin and S-adenosylhomocysteine both caused pronounced inhibition, as also to a lesser extent did farnesylthioacetic acid, deoxymethylthioadenosine and 3-deaza-adenosine. Effector studies showed that the methyltransferase activity varied depending on the concentration and chemical nature of the cations present. Monovalent cations were slightly stimulatory, while divalent metallic ions displayed diverging inhibitory effects. The inhibition by cations was validated by the stimulatory effect of the chelators EDTA and EGTA. Sulphydryl reagents inhibited methylation but to different degrees: Hg(2+)-ions: 100%, N-ethylmaleimide: 30%, dithiothreitol: 0% and mono-iodoacetate: 20%. Due to the hydrophobicity of the substrates dimethyl sulfoxide had to be included in the incubation mixture (<4%; still moderate inhibition at more elevated concentrations). The detergents tested affected the methyltransferase activity to a varying degree. The membrane bound character of the methyltransferase was confirmed.

3. Topical N-acetyl-S-farnesyl-L-cysteine inhibits mouse skin inflammation, and unlike dexamethasone, its effects are restricted to the application site

Joel S Gordon, Maxwell B Stock, Jeffry B Stock, Peter M Wolanin, Karl Rouzard, Eduardo Perez, David A Fela, Gopal Sarngadharan, Arnold V Gonzalez J Invest Dermatol . 2008 Mar;128(3):643-54. doi: 10.1038/sj.jid.5701061.

N-acetyl-S-farnesyl-L-cysteine (AFC), a modulator of G protein and G-protein coupled receptor signaling, inhibits neutrophil chemotaxis and other inflammatory responses in cell-based assays. Here, we show topical AFC inhibits in vivo acute inflammation induced by 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and arachidonic acid using the mouse ear model of inflammation. AFC inhibits edema, as measured by ear weight, and also inhibits neutrophil infiltration as assayed by direct counting in histological sections and by measuring myeloperoxidase (MPO) activity as a neutrophil marker. In addition, AFC inhibits in vivo allergic contact dermatitis in a mouse model utilizing sensitization followed by a subsequent challenge with 2,4-dinitrofluorobenzene. Unlike the established anti-inflammatories dexamethasone and indomethacin, AFC's action was restricted to the site of application. In this mouse model, both dexamethasone and indomethacin inhibited TPA-induced edema and MPO activity in the vehicle-treated, contralateral ear. AFC showed no contralateral ear inhibition for either of these end points. A marginally significant decrease due to AFC treatment was seen in TPA-induced epidermal hyperplasia at 24 hours. This was much less than the 90% inhibition of neutrophil infiltration, suggesting that AFC does not act by directly inhibiting protein kinase C.