Isotachophoretic analysis of a synthetic dipeptide l-alanyl-l-glutamine

Stehle, Peter; Pfaendler, Peter; Fürst, Peter

doi:10.1016/s0021-9673(01)96174-6

Cited by 39 publications

(9 citation statements)

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“…(159) as con firmed for specific dipeptides containing glutamine (C-terminal), tyrosine, and cysteine, which are resistant to heat sterilization (186). Quality control tech niques such as high-performance liquid chromatography (HPLC), isotacho phoresis, nuclear magnetic resonance (NMR), and mass spectrometry (MS) have been applied to ensure purity (186,191). Protein hydrolysate toxicity and composition as well as peptide-chain length profile and composition have been determined by standard in vitro/in vivo testing (112, 206), amino acid analysis, Cu(lI)-sephadex chromatography ( …”

Section: General Considerations For Use Of Parenteral Peptidesmentioning

confidence: 99%

“…amounts cannot be given to fluid-restricted patients. Although hospital manufacturing pharmacies may formulate L-glutamine solutions sub ject to normal pharmaceutical safeguards (74), commercial solutions of termi nally sterilized, glutamine dipeptide-supplemented amino acids solutions with good long-term stability will eventually be made available (191).…”

Section: Glutamine Peptide Prodrugsmentioning

confidence: 99%

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The Significance of Peptides in Clinical Nutrition

Grimble

1994

Annu. Rev. Nutr.

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Section: General Considerations For Use Of Parenteral Peptidesmentioning

confidence: 99%

Section: Glutamine Peptide Prodrugsmentioning

confidence: 99%

The Significance of Peptides in Clinical Nutrition

Grimble

1994

Annu. Rev. Nutr.

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“…The intestine utilizes glutamine for the maintenance of the barrier function and in the regulation of the inflammation and apoptosis (Carneiro et al, 2006;Li and Neu, 2009;Hou et al, 2013). Glutamine is very poorly soluble and unstable during storage and heat sterilization, which limits its addition in the existing preparations (Stehle et al, 1984). However, these shortcomings can be overcome by employing a synthetic dipeptide containing glutamine, L-alanyl-L-glutamine (Ala-Gln) (Furst et al, 1987;Furst et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Protective Effects Oncorneal Endothelium During Intracameral Irrigation Using N-(2)-l-alanyl-l-Glutamine

Jin

Wang

et al. 2020

Front. Pharmacol.

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Corneal endothelial disease is a global sight-threatening disease, and corneal transplantation using donor corneas remains the sole therapeutic option. A previous work demonstrated that N (2)-alanyl-glutamine (Ala-Gln) protected against apoptosis and cellular stress, and maintained intestinal tissue integrity. In this pursuit, the present study aimed to examine the effect of Ala-Gln in the protection of the corneal endothelium and expand its range of potential clinical applications. Mice in the control group were intracamerally irrigated with Ringers lactate injection, whereas those in the experimental group were irrigated with Ringers lactate injection containing Ala-Gln. The mean intraocular pressure increased to 44 ± 3.5 mm Hg during intracameral irrigation (normal range 10.2 ± 0.4 mmHg). In vivo confocal microscopy results showed that the addition of Ala-Gln protected the morphology, structure, and density of the corneal endothelial cells. Optical Coherence Tomography (OCT) measurements showed that corneal thickness was not significantly different between the two groups, because of the immediate corneal edema after irrigation, but the addition of Ala-Gln obviously promoted the recovery of the corneal edema. Scanning electron microscopy indicated that the corneal endothelial cells were severely ruptured and exfoliated in the Ringer's group accompanied with cellular edema, when compared with the Ala-Gln group. The intracameral irrigation using Ala-Gln protected the structure and expression of cytoskeleton and Na-K-ATPase, which exhibited a regular distribution and significantly increased expression in comparison to Ringer's group. Furthermore, Ala-Gln maintained the mitochondrial morphology and increased the activity of mitochondria. Moreover, transmission electron microscopy showed that intracameral irrigation of Ala-Gln reversed the ultrastructural changes induced by the acute ocular hypertension in mice. Our study demonstrates that the intracameral irrigation of Ala-Gln effectively maintained the corneal endothelial pump function and barrier function by protecting the mitochondrial function and preventing the rearrangement of cytoskeleton in acute ocular hypertension in mice.

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“…l -Alanyl- l -glutamine (Ala-Gln) and glycyl- l -glutamine (Gly-Gln) are supposed to be two main types of glutamine-containing dipeptides in clinical practice [9]. Ala-Gln has been clinically selected as the most suitable alternative of Gln because of its high thermostability under heat sterilization, highly solubility (568 g/L), and higher decomposition rate [10, 11]. Beyond that, Ala-Gln will be rapidly removed from plasma after parenteral administration without accumulation in tissues and undetectable in urine [12].…”

Section: Introductionmentioning

confidence: 99%

Production of l-alanyl-l-glutamine by immobilized Pichia pastoris GS115 expressing α-amino acid ester acyltransferase

Gao

Pei

et al. 2019

Microb Cell Fact

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Backgroundl-Alanyl-l-glutamine (Ala-Gln) represents the great application potential in clinic due to the unique physicochemical properties. A new approach was developed to synthesize Ala-Gln by recombinant Escherichia coli OPA, which could overcome the disadvantages of traditional chemical synthesis. Although satisfactory results had been obtained with recombinant E. coli OPA, endotoxin and the use of multiple antibiotics along with toxic inducer brought the potential biosafety hazard for the clinical application of Ala-Gln.ResultsIn this study, the safer host Pichia pastoris was applied as an alternative to E. coli. A recombinant P. pastoris (named GPA) with the original gene of α-amino acid ester acyltransferase (SsAet) from Sphingobacterium siyangensis SY1, was constructed to produce Ala-Gln. To improve the expression efficiency of SsAet in P. pastoris, codon optimization was conducted to obtain the strain GPAp. Here, we report that Ala-Gln production by GPAp was approximately 2.5-fold more than that of GPA. The optimal induction conditions (cultivated for 3 days at 26 °C with a daily 1.5% of methanol supplement), the optimum reaction conditions (28 °C and pH 8.5), and the suitable substrate conditions (AlaOMe/Gln = 1.5/1) were also achieved for GPAp. Although most of the metal ions had no effects, the catalytic activity of GPAp showed a slight decrease in the presence of Fe3+ and an obvious increase when cysteine or PMSF were added. Under the optimum conditions, the Ala-Gln generation by GPAp realized the maximum molar yield of 63.5% and the catalytic activity of GPAp by agar embedding maintained extremely stable after 10 cycles.ConclusionsCharacterized by economy, efficiency and practicability, production of Ala-Gln by recycling immobilized GPAp (whole-cell biocatalyst) is represents a green and promising way in industrial.Electronic supplementary materialThe online version of this article (10.1186/s12934-019-1077-1) contains supplementary material, which is available to authorized users.

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Isotachophoretic analysis of a synthetic dipeptide l-alanyl-l-glutamine

Cited by 39 publications

References 14 publications

The Significance of Peptides in Clinical Nutrition

The Significance of Peptides in Clinical Nutrition

Protective Effects Oncorneal Endothelium During Intracameral Irrigation Using N-(2)-l-alanyl-l-Glutamine

Production of l-alanyl-l-glutamine by immobilized Pichia pastoris GS115 expressing α-amino acid ester acyltransferase

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