H-Ala-Ala-Ala-Ala-Ala-OH is a homooligopeptide composed entirely of alanine residues, offering a minimalistic model for α-helix formation. Its uniform side-chain environment simplifies analysis of steric and hydrogen-bond patterns. Researchers use it to explore folding dynamics and peptide-solvent interactions. Applications include structural calibration, helix-nucleation studies, and computational model benchmarking.
CAT No: R2397
CAS No:10183-34-3
Synonyms/Alias:H-Ala-Ala-Ala-Ala-Ala-OH;10183-34-3;Penta-alanine;Ala-Ala-Ala-Ala-Ala;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-aminopropanoyl]amino]propanoyl]amino]propanoyl]amino]propanoyl]amino]propanoic acid;alanyl-alanyl-alanyl-alanyl-alanine;Penta-L-alanine; AAAAA (peptide); Alanine, N-[N-[N-(N-L-alanyl-L-alanyl)-L-alanyl]-L-alanyl]- (6CI,7CI); Alanine, N-[N-[N-(N-L-alanyl-L-alanyl)-L-alanyl]-L-alanyl]-, L- (8CI); L-Alanine, N-[N-[N-(N-L-alanyl-L-alanyl)-L-alanyl]-L-alanyl]-; L-Alanyl-L-alanyl-L-alanyl-L-alanyl-L-alanine;MFCD00080980;CHEMBL328980;SCHEMBL23733547;XXAUOPDVAKGRPR-WYCDGMCDSA-N;HY-P4623;DA-53818;FA108401;CS-0655419;(2S,5S,8S,11S,14S)-14-amino-2,5,8,11-tetramethyl-4,7,10,13-tetraoxo-3,6,9,12-tetraazapentadecan-1-oic acid;
H-Ala-Ala-Ala-Ala-Ala-OH is a synthetic peptide composed of five consecutive alanine residues, commonly referred to as a polyalanine pentapeptide. As a model oligopeptide, it is widely valued in biochemical research for its simplicity, defined sequence, and lack of side-chain complexity beyond methyl groups. The structural uniformity and physicochemical properties of this peptide make it an ideal substrate for exploring peptide behavior, secondary structure formation, and sequence-dependent interactions. Its relevance extends across peptide chemistry, protein folding studies, and the development of analytical methodologies, underscoring its significance as a versatile tool in both academic and industrial research settings.
Peptide structure-function analysis: As a homopolymeric alanine peptide, H-Ala-Ala-Ala-Ala-Ala-OH serves as a benchmark for investigating the relationship between primary sequence and secondary structure in peptides. Researchers utilize it to examine helix formation, β-sheet propensity, and random coil behavior in solution or solid state, providing fundamental insights into the folding mechanisms of larger polypeptides and proteins. Its uniform side-chain composition allows for controlled studies on backbone conformation and the intrinsic properties of peptide chains.
Analytical method development: The defined sequence and physicochemical stability of this pentapeptide make it an excellent standard for calibrating and validating peptide analytical techniques. It is frequently employed as a reference material in high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. By offering predictable retention times and fragmentation patterns, the peptide aids in optimizing separation protocols and instrument sensitivity for peptide and protein analysis.
Peptide synthesis optimization: H-Ala-Ala-Ala-Ala-Ala-OH is often used as a test substrate in the development and evaluation of solid-phase peptide synthesis (SPPS) methodologies. Its straightforward sequence enables the assessment of coupling efficiency, resin performance, and deprotection strategies without the complications introduced by bulky or reactive side chains. This application is particularly valuable for laboratories seeking to refine synthesis protocols or benchmark new reagents and technologies in peptide manufacturing.
Protein engineering and design: The pentapeptide provides a minimalistic model for studying sequence-driven aggregation, self-assembly, and intermolecular interactions relevant to protein engineering. By incorporating polyalanine motifs into larger constructs or studying them in isolation, scientists can elucidate the effects of repetitive sequences on structural stability, aggregation propensity, and material properties. These studies inform the rational design of novel peptides and protein-based biomaterials.
Biophysical characterization: H-Ala-Ala-Ala-Ala-Ala-OH is frequently employed in spectroscopic and thermodynamic investigations to probe peptide-solvent interactions, hydrogen bonding patterns, and conformational dynamics. Techniques such as circular dichroism (CD), nuclear magnetic resonance (NMR), and infrared (IR) spectroscopy benefit from the peptide's well-defined structure, enabling detailed analysis of folding transitions and environmental influences on peptide conformation. Such studies contribute to a broader understanding of peptide behavior in diverse biophysical contexts.
4. Cationic cell-penetrating peptides are potent furin inhibitors
5. Myotropic activity of allatostatins in tenebrionid beetles
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More