Succinimidyl esters of fatty acids for amino acid acylations

Paquet, Alenka

doi:10.1139/v76-106

Cited by 41 publications

(15 citation statements)

References 7 publications

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“…Preparation of Monomethylarginine (-N G -Monomethylarginine)-Conversion of Fmoc-OCOCl to Fmoc-OSu was performed as described (28,29). HOSu (0.633 g, 5.5 mmol) was added to a solution of FmocOCOCl (1.29 g, 5.0 mmol) in dioxane (12.5 ml) in a 50-ml roundbottomed flask with a magnetic stirrer.…”

Section: Methodsmentioning

confidence: 99%

PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine

Lee

Cook

Yang

et al. 2005

Journal of Biological Chemistry

185

153

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The cDNA for PRMT7, a recently discovered human protein-arginine methyltransferase (PRMT), was cloned and expressed in Escherichia coli and mammalian cells. Immunopurified PRMT7 actively methylated histones, myelin basic protein, a fragment of human fibrillarin (GAR) and spliceosomal protein SmB. Amino acid analysis showed that the modifications produced were predominantly monomethylarginine and symmetric dimethylarginine (SDMA). Examination of PRMT7 expressed in E. coli demonstrated that peptides corresponding to sequences contained in histone H4, myelin basic protein, and SmD3 were methylated. Furthermore, analysis of the methylated proteins showed that symmetric dimethylarginine and relatively small amounts of monomethylarginine and asymmetric dimethylarginine were produced. SDMA was also formed when a GRG tripeptide was methylated by PRMT7, indicating that a GRG motif is by itself sufficient for symmetric dimethylation to occur. Symmetric dimethylation is reduced dramatically compared with monomethylation as the concentration of the substrate is increased. The data demonstrate that PRMT7 (like PRMT5) is a Type II methyltransferase capable of producing SDMA modifications in proteins.

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Section: Methodsmentioning

confidence: 99%

PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine

Lee

Cook

Yang

et al. 2005

Journal of Biological Chemistry

185

153

View full text Add to dashboard Cite

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“…21 The N ␣ -Zprotected L-(␣Me)Nva residue was synthesized from Z-OSu[N-(benzyloxycarbonyl)succinimide]. 35,36 L-(␣Me)Nva methylester hydrochloride was prepared by treatment of the free amino acid with thionyl chloride in methanol. The fully protected heptapeptide 7 was synthesized by solution methods.…”

Section: Peptide Synthesismentioning

confidence: 99%

The complete chirospectroscopic signature of the peptide 3₁₀‐helix in aqueous solution

et al. 2004

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We synthesized by solution methods a water-soluble, terminally blocked heptapeptide based on five markedly helicogenic, C(alpha)-tetrasubstituted alpha-amino acids C(alpha)-methyl-L-norvalines and two strongly hydrophilic 2-amino-3-[1-(1,4,7-triazacyclononane)]-L-propanoic acid residues at positions 2 and 5. A Fourier transform infrared absorption and NMR analysis in deuterated chloroform and aqueous solutions of the heptapeptide and two side-chain protected synthetic precursors confirmed our working hypothesis that all oligomers are folded in the 3(10)-helical conformation. Based on these findings, we exploited this heptapeptide as a chiral reference compound for detailed electronic CD, vibrational CD, and Raman optical activity characterizations of the 3(10)-helix in aqueous solution.

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“…Surfactants have a variety of applications in detergency, solubilization, emulsification, and preservation of biomaterials. Studies on surface-active properties of different types of surfactants derived from lauroyl and palmitoyl derivatives of glycine and alanine have been reported (1). Critical micelle concentration (CMC) and foaming ability can serve to characterize the physicochemical nature of any surfactant molecule.…”

mentioning

confidence: 99%

Preparation, characterization, and surface and biological properties of N‐stearoyl amino acids

Sivasamy

Krishnaveni

Rao

2001

J Americ Oil Chem Soc

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Several lipoamino acids were synthesized, in which n-octadecanoic acid (stearic acid) was coupled with the α-amino group of an amino acid. The products were characterized and their identities confirmed by advanced analytical techniques like Fourier transform infrared, 1 H nuclear magnetic resonance spectroscopy, and differential scanning calorimetry. Their surface properties, such as critical micelle concentration (CMC) and foaming properties, biodegradability, and antimicrobial activity were also evaluated. The N-stearoyl amino acids (NSA) had low CMC values, and some of them showed good foaming properties. They were screened for antimicrobial activity against the gram-positive bacteria Staphylococcus aureus, Micrococcus luteus, and Bacillus cerceus, the gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa, and the yeast Candida albicans. All the compounds inhibited at least one of these organisms. N-Stearoyl proline was the most effective, the order of antimicrobial activity being aromatic NSA > acidic NSA > basic NSA. However, the effective inhibition by all the compounds indicates the desirability of more thorough investigation and suggests that some of these compounds may have potential utility as biostatic additives in commercial products. All NSA are highly biodegradable and can readily be removed under conditions of normal secondary sewage treatment.Paper no. J9653 in JAOCS 78, 897-902 (September 2001).

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Succinimidyl esters of fatty acids for amino acid acylations

Cited by 41 publications

References 7 publications

PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine

PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine

The complete chirospectroscopic signature of the peptide 3₁₀‐helix in aqueous solution

Preparation, characterization, and surface and biological properties of N‐stearoyl amino acids

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Succinimidyl esters of fatty acids for amino acid acylations

Cited by 41 publications

References 7 publications

PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine

PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine

The complete chirospectroscopic signature of the peptide 310‐helix in aqueous solution

Preparation, characterization, and surface and biological properties of N‐stearoyl amino acids

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Product

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The complete chirospectroscopic signature of the peptide 3₁₀‐helix in aqueous solution