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Alanylalanine

Alanylalanine is a dipeptide composed of two alanine amino acids.
It is involved in various biological processes and has potential applications in research and clinical settings.
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Most cited protocols related to «Alanylalanine»

1
Characterization of Alanylalanine by LCMS
Each sample in the previous section was diluted by water up to 10 µL. The final product, alanylalanine, was characterized by LCMS-2010EV electrospray mass spectrometry (Shimadzu, Kyoto, Japan) in positive-single ion monitoring (SIM) mode at m/z 199.20 using the analytical column Luna C8(2) 100 Å (150 mm × 4.6 mm, Phenomenex). The mobile phase consisted of 65% methanol. The flow rate was set at 0.2 mL/min and the injection volume was 8 µL. The column temperature was 60 °C. The peak area was calculated according to the protocol of the manufacturer (Shimadzu, Kyoto, Japan).
Kawabata M., Kawashima K., Mutsuro-Aoki H., Ando T., Umehara T, & Tamura K. (2022). Peptide Bond Formation between Aminoacyl-Minihelices by a Scaffold Derived from the Peptidyl Transferase Center. Life, 12(4), 573.
Full text: Click here
Publication 2022
alanylalanine Lincomycin Mass Spectrometry Methanol
2
Self-Dimerization and Alanylation Assay
1000 pmol of P1c2 or P1c2UGGU was dissolved in 2 µL of ACCA reaction buffer. After heating at 95 °C for 10 min, it was incubated on ice for 60 min to be self-dimerized. Then, 1000 pmol of alanyl-minihelixAla was added and placed at 4 °C for 24 h. The reaction product was treated with 0.22 µL of 250 mM KOH (pH of the solution was changed from 7.5 to pH 9.0) at room temperature for 45 min to liberate any alanylalanine that might form. As a negative control, 2 µL of ACCA reaction buffer was used instead of 2 µL of 1000 pmol of P1c2 or P1c2UGGU in the first step.
Kawabata M., Kawashima K., Mutsuro-Aoki H., Ando T., Umehara T, & Tamura K. (2022). Peptide Bond Formation between Aminoacyl-Minihelices by a Scaffold Derived from the Peptidyl Transferase Center. Life, 12(4), 573.
Full text: Click here
Publication 2022
alanylalanine Buffers
3
Immobilization of Photoreactive Peptides on Polypropylene Membranes
Not available on PMC !

EXAMPLE 1

The peptide to be immobilized H-Ala-Ala-OH was combined as the alanylalanine methyl ester hydrochloride 2 (7.2 g) with 10 g of L-N-Boc-2-(2-oxo-2-phenylethyl) glycine 1, i.e., with a linker compound of the general formula (I) (compare FIGS. 1, 3), with R1=phenyl, R2═OR4, R3=t-butoxycarbonyl (Boc) and R4═H, and 12 g of O-(benzotriazol-1-yl)-N,N, N′,N′-tetramethyluronium tetrafluoroborate in 300 ml of dichloromethane.

Ethyl diisopropylamine (1.3 ml) was slowly dripped into this suspension while stirring at 0° C. (ice cooling). The suspension was heated to room temperature and stirring was continued, until compound 1 could still be detected only in trace amounts, by thin-layer chromatography (silica gel 60 F254, mobile phase: dichloromethane/methanol 10:1) (approximately 2 h). The mixture was placed in a separatory funnel and the organic phase was extracted sequentially with 500 ml each of water, saturated tartaric acid solution and saturated sodium hydrogen carbonate solution. The organic phase was separated, dried with sodium sulfate, and the solvent was removed on the rotary evaporator. Approximately 15 g of a resin were obtained, which were purified on silica gel 60 (mobile phase: dichloromethane/methanol 5:1) by flash column chromatography. The yield of 2-[2-(2-tert-butoxycarbonylamino-4-oxo-4-phenyl-butyrylamino)propionylamino] propionic acid methyl ester 3 (Boc-BzAla-Ala-Ala-OMe) amounted to 13 g.

[Figure (not displayed)]

A polypropylene membrane (diameter 30 mm) was immersed for 30 minutes in a 0.1 M solution of 2-[2-(2-tert-butoxycarbonylamino-4-oxo-4-phenylbutyrylamino)propionylamino]propionic acid methyl ester 3, i.e., a photoreactive amino acid of the general formula (II) (compare FIG. 3), with R1=phenyl, and R3=t-butoxycarbonyl (Boc), and peptide H-Ala-Ala-OH bound to the N terminal as the methyl ester, as biomolecule M in dichloromethane, and then dried in high vacuum at 3·10−5 Torr for 30 minutes.

The membrane was irradiated for 30 minutes with the light of an HBO 500 at a distance of 20 cm with the use of a cutoff filter, which filters out light below 290 nm.

The membrane was then washed five times with a total of 150 ml of dichloromethane and dried for 30 minutes in high vacuum at 3·10−5 Torr.

The immobilization of the peptide according to formula (IV), in which the radicals R1 und R3 and the biomolecule M have the above-named meanings, was detected by comparison of the FT-IR spectra for the polypropylene membrane before and after treatment.

EXAMPLE 2

A polypropylene membrane (diameter 30 mm) was irradiated in a glass dish, filled with a 0.1 M solution of 2-[2-(2-tert-butoxycarbonylamino-4-oxo-4-phenylbutyrylamino)propionylamino]propionic acid methyl ester 3 (produced according to Example 1), i.e., a photoreactive amino acid of the general formula (II), with R1=phenyl and R3=t-butoxycarbonyl (Boc), and peptide H-Ala-Ala-OH bound to the N terminal as the methyl ester in benzene, for 60 minutes with the light of an HBO 500 at a distance of 20 cm with the use of a tilted mirror and a cutoff filter, which filters out light below 290 nm.

The membrane was then washed once with 50 ml of benzene and twice with 50 ml of dichloromethane and dried for 30 minutes in high vacuum at 3·10−5 Torr.

The immobilization of the peptide according to formula (IV), in which the radicals R1 and R3 have the above-named meanings, was detected by comparison of the FT-IR spectra for the polypropylene membrane before and after treatment.

US07514540B2. Functionalized carrier material containing covalently bound biomolecule via a linker (2009-04-07). Poly-An Gesellschaft zur Herstellung Von Polymeren Fuer Spezielle Anwendungen und Analytik mbH [DE]. Inventors: Pablo Wessig [DE], Jürgen Bendig [DE], Uwe Schedler [DE].
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Patent 2009
4
Two-dimensional Infrared Spectroscopy Setup
The two-dimensional infrared setup is based on 800 nm laser pulses (7 W, 35 fs, 1 kHz) from a regenerative amplifier laser system (Coherent, Astrella). In all, 2.7 W of the 800 nm pulses were used to pump an optical parametric amplifier Topas Prime (Coherent) to generate signal and idler pulses. Signal and idler pulses were used to generate infrared pules at ~6000 nm (18 µJ, 400 cm−1 FWHM) using non-collinear difference frequency generation (NDFG) Topas (Coherent). The IR beams are guided into a commercial 2D infrared spectrometer 2D Quick IR (Phasetech, Inc.).
In the spectrometer, a weak reflection90 (link),91 (link) from a wedged ZnSe window is used as probe beam. The transmitted IR light is guided to a pulse shaper, where it is diffracted from a grating (150 l/mm), collimated using a parabolic mirror, and guided to a Germanium-based acousto-optic modulator (AOM). The IR light is diffracted at the AOM and focused onto a second grating (150 l/mm). The shaped beam is reflected from a retroreflector on a translational stage to control the waiting time (T2) between the pump and the probe beams. After setting the polarization of the pump beam to 45° relative to the probe beam polarization, the pump and the probe beams are focused into the sample using an off-axis parabolic mirror. After the sample, the probe beam is re-collimated and split into polarization components, parallel and perpendicular relative to the pump beam with a polarizer. Both probe components are focused into an imaging spectrograph (SP2156 spectrograph, Princeton Instruments, 30 l/mm grating) and detected using a 128 × 128 pixel mercury cadmium telluride (MCT) array detector.
Frequency resolution on the pump axis is obtained in time domain, using the pulse shaper to generate two pump pulses delayed by 0 to 2555 fs at increments of 35 fs. To reduce data acquisition time we used a rotating frame at 1400 cm−1. Pump pulses were corrected for group-velocity dispersion, and the dispersion parameters were optimized using the transient signal generated from multi-photon absorption in a 0.5 mm thick Ge plate. Before transforming the thus determined free induction decays into the frequency domain, the time-domain data were zero-padded to 128 data points and filtered with a Hamming window.
Krevert C.S., Gunkel L., Haese C, & Hunger J. (2022). Ion-specific binding of cations to the carboxylate and of anions to the amide of alanylalanine. Communications Chemistry, 5, 173.
Full text: Click here
Publication 2022
Debility Epistropheus Eye Germanium Light mercury cadmium telluride Protein Biosynthesis Pulse Rate Pulses Reading Frames Regeneration Transients
5
Probing Peptide-Salt Interactions via Spectroscopy
Guanidinium chloride (GdmCl), LiCl, KCl, KSCN, KI, and l-alanyl-l-alanine (2Ala) were used without further purification. Solutions for DRS and NMR experiments were prepared using H2O with a specific resistivity >18 MΩcm−1 from a Millipore MILLI-Q purification unit or using D2O for infrared experiments. All samples were prepared by weighing the appropriate amount of salt and peptide into a 1 mL volumetric flask using an analytical balance. The peptide concentration was kept constant at 250 mM for all samples, while the salt concentration was varied from 0.05 M to 1.05 M for DRS and NMR experiments. For infrared experiments, we used salts concentrations of 1.05, 3, and 5 M.
For DRS experiments, 1 mL of each sample was brought in contact with the coaxial probes. For NMR experiments, 0.5 mL of the samples were placed in an NMR tube together with a capillary filled with DMSO-d6 for referencing. For all infrared experiments, solutions were contained between two CaF2 windows (2 mm thickness, 2.54 cm diameter) separated by a 25 µm Teflon spacer. The infrared absorption spectra were measured right before collecting the 2D-IR data.
Krevert C.S., Gunkel L., Haese C, & Hunger J. (2022). Ion-specific binding of cations to the carboxylate and of anions to the amide of alanylalanine. Communications Chemistry, 5, 173.
Full text: Click here
Publication 2022
alanylalanine, (L)-isomer Capillaries ECI2 protein, human Hydrochloride, Guanidine Peptides potassium thiocyanate Salts Sodium Chloride Sulfoxide, Dimethyl Teflon

Most recents protocols related to «Alanylalanine»

1
Quantification of Amino Acids and Nucleobases

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2024
2
Metabolomic Analysis of Bacterial Vaginosis
Not available on PMC !
The metabolite list from the study by Srinivasan et. al. (2015) reported 108 metabolites with their KEGG annotations and was used for our comparison (28) . From the MMIP predicted list of significant metabolites, 52 overlapped with their list and 21 of those 52 metabolites depicted the same trend as reported in the study. We provide a relative value that signifies the capacity of that community to consume or accumulate a particular metabolite. Like for example cadaverine, in the study they showed that the BV+ samples had a higher amount of this compound; in our prediction we showed that compared to that of BV-(or H) group, the relative capacity of cadaverine being accumulated in the BV+ samples is significantly higher than that of BVsamples. With regards to amino acids, we correctly predicted the lowering of amino acids in BV+ samples. The study reported that 18 out 19 amino acids that they found in the samples, were lower in amount in BV+ samples compared to that of BV-or healthy samples; there is an increase in amino acid catabolites in BV+ samples. The amino acids that lowered in our prediction included alanine, cysteine, histidine, tryptophan, phenylalanine etc. and the dipeptide, alanylalanine. Also, the compounds that are involved in amino acid metabolism pathways like spermine and glutathione, were also found to be low in BV+ and matched with that of the study. While drawing a biological inference from this result we can say, an increase in the number of bacterial taxa and not just Lactobacillus, probably cause an increased usage of amino acids since they are essential during cell growth; correlating to this pattern we can also say that this should also increase the amount of amino acid catabolites, and this too is confirmed by our prediction. Thus, the increase in amino acid catabolites and decrease of amino acids in BV+ samples with increased bacterial diversity.
Focusing on the carbohydrate metabolism associated metabolites, the study reported lowering of simple sugars in BV+ environment, and the same is observed in our results too; maltose being one of them, that overlap with them and follow the correct trend. Also, glucose-6-phosphate, and sugar alcohols like sorbitol and mannitol are other reported carbohydrate metabolism metabolites that are correctly predicted and maintain the trend of being present in lower amounts in BV+ cases. The same explanation that justified our amino acids metabolite prediction could also justify the case for carbohydrate metabolism metabolites; while the simple sugars and intermediate metabolites are being used up, the carbohydrate catabolites tend to accumulate in BV+ samples with the growing diversity of microbes.
They also reported lowering of glycerol, ethanolamine and glycerophosphorylcholine (GPC), all of which are associated with lipid metabolism, in BV+ samples and they too were correctly predicted.
Gautam A., Bhowmik D., Basu S., Zeng W., Lahiri A., Huson D.H., & Paul S. (2023). Microbiome Metabolome Integration Platform (MMIP): a web-based platform for microbiome and metabolome data integration and feature identification.
Publication 2023
3
Characterization of Alanylalanine by LCMS
Each sample in the previous section was diluted by water up to 10 µL. The final product, alanylalanine, was characterized by LCMS-2010EV electrospray mass spectrometry (Shimadzu, Kyoto, Japan) in positive-single ion monitoring (SIM) mode at m/z 199.20 using the analytical column Luna C8(2) 100 Å (150 mm × 4.6 mm, Phenomenex). The mobile phase consisted of 65% methanol. The flow rate was set at 0.2 mL/min and the injection volume was 8 µL. The column temperature was 60 °C. The peak area was calculated according to the protocol of the manufacturer (Shimadzu, Kyoto, Japan).
Kawabata M., Kawashima K., Mutsuro-Aoki H., Ando T., Umehara T, & Tamura K. (2022). Peptide Bond Formation between Aminoacyl-Minihelices by a Scaffold Derived from the Peptidyl Transferase Center. Life, 12(4), 573.
Full text: Click here
Publication 2022
alanylalanine Lincomycin Mass Spectrometry Methanol
4
Self-Dimerization and Alanylation Assay
1000 pmol of P1c2 or P1c2UGGU was dissolved in 2 µL of ACCA reaction buffer. After heating at 95 °C for 10 min, it was incubated on ice for 60 min to be self-dimerized. Then, 1000 pmol of alanyl-minihelixAla was added and placed at 4 °C for 24 h. The reaction product was treated with 0.22 µL of 250 mM KOH (pH of the solution was changed from 7.5 to pH 9.0) at room temperature for 45 min to liberate any alanylalanine that might form. As a negative control, 2 µL of ACCA reaction buffer was used instead of 2 µL of 1000 pmol of P1c2 or P1c2UGGU in the first step.
Kawabata M., Kawashima K., Mutsuro-Aoki H., Ando T., Umehara T, & Tamura K. (2022). Peptide Bond Formation between Aminoacyl-Minihelices by a Scaffold Derived from the Peptidyl Transferase Center. Life, 12(4), 573.
Full text: Click here
Publication 2022
alanylalanine Buffers
5
Two-dimensional Infrared Spectroscopy Setup
The two-dimensional infrared setup is based on 800 nm laser pulses (7 W, 35 fs, 1 kHz) from a regenerative amplifier laser system (Coherent, Astrella). In all, 2.7 W of the 800 nm pulses were used to pump an optical parametric amplifier Topas Prime (Coherent) to generate signal and idler pulses. Signal and idler pulses were used to generate infrared pules at ~6000 nm (18 µJ, 400 cm−1 FWHM) using non-collinear difference frequency generation (NDFG) Topas (Coherent). The IR beams are guided into a commercial 2D infrared spectrometer 2D Quick IR (Phasetech, Inc.).
In the spectrometer, a weak reflection90 (link),91 (link) from a wedged ZnSe window is used as probe beam. The transmitted IR light is guided to a pulse shaper, where it is diffracted from a grating (150 l/mm), collimated using a parabolic mirror, and guided to a Germanium-based acousto-optic modulator (AOM). The IR light is diffracted at the AOM and focused onto a second grating (150 l/mm). The shaped beam is reflected from a retroreflector on a translational stage to control the waiting time (T2) between the pump and the probe beams. After setting the polarization of the pump beam to 45° relative to the probe beam polarization, the pump and the probe beams are focused into the sample using an off-axis parabolic mirror. After the sample, the probe beam is re-collimated and split into polarization components, parallel and perpendicular relative to the pump beam with a polarizer. Both probe components are focused into an imaging spectrograph (SP2156 spectrograph, Princeton Instruments, 30 l/mm grating) and detected using a 128 × 128 pixel mercury cadmium telluride (MCT) array detector.
Frequency resolution on the pump axis is obtained in time domain, using the pulse shaper to generate two pump pulses delayed by 0 to 2555 fs at increments of 35 fs. To reduce data acquisition time we used a rotating frame at 1400 cm−1. Pump pulses were corrected for group-velocity dispersion, and the dispersion parameters were optimized using the transient signal generated from multi-photon absorption in a 0.5 mm thick Ge plate. Before transforming the thus determined free induction decays into the frequency domain, the time-domain data were zero-padded to 128 data points and filtered with a Hamming window.
Krevert C.S., Gunkel L., Haese C, & Hunger J. (2022). Ion-specific binding of cations to the carboxylate and of anions to the amide of alanylalanine. Communications Chemistry, 5, 173.
Full text: Click here
Publication 2022
Debility Epistropheus Eye Germanium Light mercury cadmium telluride Protein Biosynthesis Pulse Rate Pulses Reading Frames Regeneration Transients

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L-alanine is an amino acid that serves as a building block for proteins. It is a white, crystalline powder that is commonly used in various laboratory applications. The core function of L-alanine is to provide a source of nitrogen and carbon for biochemical reactions and processes.

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