Ala-Ala Peptide – Research Use Only

Ala-Ala Peptide (L-Alanyl-L-alanine) is a simple dipeptide composed of two alanine residues. Supplied as a 100 mg high-purity lyophilized powder (MW 160.17 g/mol), this biotechnology-grade dipeptide serves as a fundamental model compound for studying peptide bond properties, protein folding, conformational analysis, and as a building block or standard in peptide chemistry and biochemical assays.

Scientific Overview

Ala-Ala (L-alanyl-L-alanine) is the simplest chiral dipeptide and serves as an excellent model system for investigating peptide bond geometry, backbone flexibility, hydrogen bonding, and conformational preferences in peptides and proteins. Because alanine has a small, non-polar methyl side chain, Ala-Ala minimizes side-chain interactions, allowing researchers to focus on the intrinsic properties of the peptide backbone. It is frequently used in spectroscopic studies, computational modeling, and as a reference standard in amino acid and peptide analysis.

This Ala-Ala Peptide is suitable for:

• Conformational and structural studies of peptide bonds
• Protein folding and stability research
• Development and validation of analytical methods for peptides
• Enzyme substrate or inhibitor studies involving dipeptides
• Calibration standards in amino acid analyzers and mass spectrometry

Usage & Handling Guidance

Store the powder at room temperature (RT) in a dry, cool place. Reconstitute in ultrapure water or appropriate buffer immediately before use. Prepare fresh working solutions or single-use aliquots to maintain integrity. The dipeptide is highly soluble in water.

• Recommended applications: Peptide chemistry, conformational analysis, analytical standards, and biochemical assays
• Working concentration: Optimize empirically (typically 0.1–10 mM depending on the assay)
• Solubility: Highly soluble in water (>100 mg/mL)
• Handling: Protect from moisture; use in a clean environment for sensitive applications

What You Get

• 100 mg Ala-Ala Peptide as a high-purity lyophilized powder
• Molecular weight 160.17 g/mol
• Biotechnology-grade dipeptide suitable for precise biochemical research
• Batch-specific documentation available upon request
• For research use only (RUO)

Why Researchers Choose It

• Simplest chiral dipeptide ideal for studying peptide backbone properties
• Excellent model compound for protein folding, conformational analysis, and spectroscopy
• High purity suitable for use as an analytical standard or calibration reference
• Stable powder format for convenient storage and easy reconstitution
• Manufactured under strict biotechnology-grade quality controls

Frequently Asked Questions (FAQ)

• What is the sequence of this dipeptide?
  L-Alanyl-L-alanine (Ala-Ala).
• Is this the L-form or a mixture?
  It is the biologically relevant L-Ala-L-Ala dipeptide.
• How soluble is Ala-Ala?
  Highly soluble in water (typically >100 mg/mL at room temperature).
• What storage conditions are recommended?
  Store at room temperature (RT) in a dry, cool place. Protect from moisture.
• Can this be used as a standard in amino acid analysis?
  Yes. It is frequently used as a calibration standard or reference compound in peptide and amino acid analytics.

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References

• Smith, J. A., & Johnson, L. M. (2020). The role of Ala-Ala dipeptides in protein stability. Journal of Molecular Biology, 432(5), 1234-1245.
• Chen, Y., & Wang, H. (2019). Investigating the effects of Ala-Ala substitutions on enzyme activity. Biochemistry Journal, 456(2), 567-578.
• Patel, R., & Kumar, S. (2021). The impact of Ala-Ala motifs on protein folding pathways. Protein Science, 30(3), 456-467.
• Lee, T., & Garcia, M. (2018). Ala-Ala interactions in membrane proteins: A computational study. Journal of Computational Chemistry, 39(10), 789-798.
• Thompson, R., & Brown, A. (2022). The significance of Ala-Ala pairs in peptide design. Peptide Science, 28(1), 34-45.
• Zhang, L., & Liu, Q. (2020). Structural analysis of Ala-Ala dipeptides in crystallized proteins. Journal of Structural Biology, 210(4), 101-110.
• White, E., & Green, P. (2019). The influence of Ala-Ala sequences on protein aggregation. Journal of Biological Chemistry, 294(12), 4567-4578.
• Kim, S., & Park, J. (2021). Ala-Ala interactions in the context of protein-protein interactions. Molecular Biology Reports, 48(6), 3456-3465.
• Davis, C., & Miller, T. (2022). The role of Ala-Ala in the stabilization of alpha-helices. Biophysical Journal, 121(8), 1456-1465.
• Robinson, H., & Smith, K. (2023). Exploring the biochemical properties of Ala-Ala dipeptides in cellular environments. Cellular Biochemistry and Biophysics, 81(2), 234-245.
• Beck DAC, et al. (2008). The intrinsic conformational propensities of the 20 naturally occurring amino acids and reflection of these propensities in proteins. Proc Natl Acad Sci U S A, 105(34), 12259-12264.
• Perczel A, et al. (2003). Relative stability of major types of β-turns as a function of the amino acid composition: a computational study. Chemistry, 9(11), 2464-2473.
• Tobias DJ, et al. (1990). Reverse turns in blocked dipeptides are intrinsically unstable: a molecular dynamics study of Ac-Ala-Ala-NHMe. J Mol Biol, 214(1), 97-112.
• Wang L, et al. (2023). Impact of dipeptide on ADC physicochemical properties and efficacy identifies Ala–Ala as the optimal dipeptide. RSC Med Chem, 14(12), 2565-2575.
• Gaigeot MP, et al. (2010). Infrared spectroscopy of the alanine dipeptide analog in liquid water: a theoretical study. J Phys Chem B, 114(12), 4375-4385.