Guanidination of Soluble Lysine-Rich Cyanophycin Yields a Homoarginine-Containing Polyamide

Frommeyer, Maja; Bergander, Klaus; Steinbüchel, Alexander

doi:10.1128/aem.04013-13

Cited by 18 publications

(10 citation statements)

References 52 publications

(85 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Because of the limited degree of conversion of the reaction and the low amount of citrulline side chains, changes in the properties of the polymer are expected to be marginal. A test to determine a possible change in the solubilization temperature of the modifi ed polymer in water, which is usually the most altered property of modifi ed CGP, [ 7,8,11 ] showed only a rather small decrease which was still within the standard deviation of the unmodifi ed polymer and was therefore considered insignifi cant (data not shown). The effect of the citrulline on the solubilization temperature is most likely suppressed by the high amount of lysine in the polymer, which itself has a strong infl uence on the solubilization of CGP.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, the chemical modifi cation of CGP was shown for the fi rst time. [ 12 ] By using a guanidination reaction, it was possible to replace 100% of the lysine side chains in CGP by homoarginine. This showed that modifi cations of CGP can also be obtained by modifying the polymer itself.…”

Section: Introductionmentioning

confidence: 99%

“…[ 4 ] An important part of CGP research focusses on the development of novel variants of CGP, both in its composition and in its characteristics. Alternative constituents can be generated by several different strains that synthesize CGP with relevant amounts of lysine, [ 7 ] ornithine, [ 8 ] or citrulline [ 8,9 ] replacing the arginine side-chains. Soluble CGP was also an interesting variation, since "conventional" CGP, which is composed of an aspartic acid backbone and L -arginine side chains, is insoluble at pH 6-8 and 20 °C, while soluble CGP did not precipitate under these conditions.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Enzymatic Modification of Soluble Cyanophycin Using the Type II Peptidyl Arginine Deiminase from Oryctolagus cuniculus

Wiefel

Steinbüchel

2016

Macromolecular Bioscience

Self Cite

View full text Add to dashboard Cite

An increased structural variety expands the number of putative applications for cyanophycin (multi-l-arginyl-poly-[l-aspartic acid], CGP). Therefore, structural modifications of CGP are of major interest; these are commonly obtained by modification and optimization of the bacterial producing strain or by chemical modification. In this study, an enzymatic modification of arginine side chains from lysine-rich CGP is demonstrated using the peptidyl arginine deiminase from Oryctolagus cuniculus, purified from Escherichia coli after heterologous expression. About 10% of the arginine side chains are converted to citrulline which corresponds to 4% of the polymer's total side chains. An inhibition of the reaction in the presence of small amounts of l-citrulline is observed, thereby explaining the low conversion rate. CGP dipeptides can be modified with about 7.5 mol% of the Asp-Arg dipeptides being converted to Asp-Cit. These results show that the enzymatic modification of CGP is feasible, opening up a whole new area of possible CGP modifications for further research.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Enzymatic Modification of Soluble Cyanophycin Using the Type II Peptidyl Arginine Deiminase from Oryctolagus cuniculus

Wiefel

Steinbüchel

2016

Macromolecular Bioscience

Self Cite

View full text Add to dashboard Cite

show abstract

“…However, in recent years, two novel procedures using chemical or enzymatic in vitro modification of the CGP were successfully applied. The first chemical modification of CGP was reported by Frommeyer et al (2014) by the guanidinylation of a lysine-rich CGP with O-methylisourea. This reaction completely converted the lysine residues of CGP to homoarginine (Frommeyer et al 2014).…”

Section: Introductionmentioning

confidence: 99%

“…The first chemical modification of CGP was reported by Frommeyer et al (2014) by the guanidinylation of a lysine-rich CGP with O-methylisourea. This reaction completely converted the lysine residues of CGP to homoarginine (Frommeyer et al 2014). The feasibility of enzymatic CGP modification was demonstrated by Wiefel and Steinbüchel (2016) using a peptidyl arginine deiminase from Oryctolagus cuniculus, which normally introduces post-translational modifications on several proteins, to catalyze the conversion of arginine residues to citrulline.…”

Section: Introductionmentioning

confidence: 99%

In Vitro Modification of Bacterial Cyanophycin and Cyanophycin Dipeptides Using Chemical Agents Towards Novel Variants of the Biopolymer

et al. 2019

Self Cite

View full text Add to dashboard Cite

Variations of the composition of cyanophycin (CGP) have been investigated since the early 2000s. Modifications of the polymer are of academical interest, but also expand the number of putative applications for CGP and its dipeptides in fields like food supplementations, and medical and cosmetic applications. Until recently variations of the composition occurred only in vivo. However, in the last years, two procedures using chemical or enzymatic in vitro modification were successfully applied. Since chemical treatments were more effective and reached higher conversion rates, a search for reagents and their applicability to conduct reactions with CGP was done. The reaction of CGP with methyl isocyanate resulted in the conversion of 50% of the lysine residues, while only 3% of the arginine residues were modified. However, using digested CGP dipeptides, the conversion rates of lysine increased slightly to 72%, while the conversion of arginine reached 96%. Using formaldehyde, CGP could be methylated with a conversion rate of 84% for lysine and 15% for arginine. Acetylation of lysine residues was obtained using acetic anhydride, reaching a conversion rate of 100% for a single acetylation, where 63% of the residues were acetylated twice. Arginine residues could be acetylated at a rate of 89%. Diacetyl could be added to 80% of all arginine residues, while lysine was not targeted by the compound. Other agents were also tested, but showed lesser or no conversion and/or inconclusive results. Overall, the tested reactions confirm the viability of chemical CGP modification for future approaches.

show abstract

Recombinant Multi‐l‐Arginyl‐Poly‐l‐Aspartate (Cyanophycin) as an Emerging Biomaterial

Tseng

Fang

2023

Macromolecular Bioscience

View full text Add to dashboard Cite

Multi‐l‐arginyl‐poly‐l‐aspartate (MAPA) is a non‐ribosomal polypeptide which synthesis is directed by cyanophycin synthetase, and its production can be achieved using recombinant microorganisms carrying the cphA gene. Along its poly‐aspartate backbone, arginine or lysine links to each aspartate via an isopeptide bond. MAPA is a zwitterionic polyelectrolyte full of charged carboxylic, amine, and guanidino groups. In aqueous solution, MAPA exhibits dual thermal and pH responses similar to those stimuli‐responsive polymers. Being biocompatible, the films containing MAPA can support cell proliferation and elicits minimal immune response in macrophages. Dipeptides from MAPA after enzymatic treatments can provide nutritional benefits. In light of the increasing interest in MAPA, this article focuses on the recent discovery of the function of cyanophycin synthetase and the potentials of MAPA as a biomaterial.

show abstract

Guanidination of Soluble Lysine-Rich Cyanophycin Yields a Homoarginine-Containing Polyamide

Cited by 18 publications

References 52 publications

Enzymatic Modification of Soluble Cyanophycin Using the Type II Peptidyl Arginine Deiminase from Oryctolagus cuniculus

Enzymatic Modification of Soluble Cyanophycin Using the Type II Peptidyl Arginine Deiminase from Oryctolagus cuniculus

In Vitro Modification of Bacterial Cyanophycin and Cyanophycin Dipeptides Using Chemical Agents Towards Novel Variants of the Biopolymer

Recombinant Multi‐l‐Arginyl‐Poly‐l‐Aspartate (Cyanophycin) as an Emerging Biomaterial

Contact Info

Product

Resources

About