Pro-Ser pairs a turn-inducing proline with polar serine to probe β-turn motifs and local structural rearrangements. The hydroxyl side chain engages in hydrogen bonding that shapes loop geometry. Researchers examine its conformational distribution by NMR and simulation. Applications include motif design, peptide-protein interface modeling, and SPPS optimization studies.
CAT No: R2567
CAS No:71835-80-8
Synonyms/Alias:Pro-Ser;71835-80-8;H-Pro-Ser-OH;L-Serine, N-L-prolyl-;CHEMBL209083;L-prolyl-L-serine;(2S)-3-hydroxy-2-[[(2S)-pyrrolidine-2-carbonyl]amino]propanoic acid;prolyl-serine;CHEBI:73648;prolylserine;L-Pro-L-Ser;MFCD00083811;SCHEMBL25365110;DTXSID70428595;BDBM50188510;AKOS010408212;DA-54089;FP108163;Q27143819;(2S)-3-hydroxy-2-{[(2S)-pyrrolidin-2-yl]formamido}propanoic acid;P-S;
Pro-Ser, also known as Prolyl-Serine, is a dipeptide composed of the amino acids proline and serine linked via a peptide bond. As a synthetic peptide, Pro-Ser serves as a valuable tool in biochemical and molecular biology research, enabling the exploration of peptide structure-function relationships and the development of peptide-based technologies. Its unique combination of a cyclic imino acid (proline) and a polar uncharged residue (serine) imparts distinct conformational properties, making it a useful model for studying peptide backbone flexibility, secondary structure motifs, and enzymatic processing. The presence of both a secondary amine and a hydroxyl side chain further enhances its relevance in investigations of peptide interactions, stability, and recognition by proteolytic enzymes.
Peptide synthesis: Pro-Ser is routinely employed as a building block in solid-phase peptide synthesis (SPPS) and solution-phase synthesis protocols. Its defined dipeptide structure allows for the efficient incorporation of proline-serine motifs into longer peptide chains, facilitating the assembly of biologically relevant sequences. The inclusion of this dipeptide can influence the local conformation of synthetic peptides, particularly in turn and loop regions, due to the conformational constraints imposed by proline and the hydrogen-bonding potential of serine. Researchers leverage these properties to design peptides with tailored structural and functional characteristics for use in biochemical assays, structural studies, and peptide-based material development.
Protein engineering: In the context of protein engineering, Pro-Ser serves as a model motif for investigating the effects of dipeptide composition on protein folding, stability, and function. The unique structural attributes of the proline-serine sequence enable researchers to probe the impact of backbone rigidity and side-chain polarity on secondary structure formation, such as β-turns and loops. Incorporation of this motif into recombinant proteins or synthetic analogs provides valuable insight into the determinants of conformational flexibility and the role of specific dipeptides in modulating protein architecture.
Enzymology research: The dipeptide is widely utilized in studies of protease specificity and mechanism. Owing to the distinct chemical environment created by the proline-serine bond, it serves as a substrate or inhibitor in enzymatic assays designed to elucidate the substrate preferences of peptidases and proteolytic enzymes. By analyzing the cleavage or resistance patterns of Pro-Ser-containing substrates, scientists can characterize enzyme active sites, map substrate recognition motifs, and advance the development of selective enzyme modulators.
Peptide transport and metabolism studies: Pro-Ser is instrumental in exploring the mechanisms of peptide uptake and metabolism in biological systems. As a representative dipeptide with both hydrophobic and hydrophilic features, it is used to assess the activity of peptide transporters, such as those in cellular membranes or epithelial tissues. Tracking the uptake, hydrolysis, or modification of this compound provides critical data on transporter specificity, metabolic pathways, and the regulation of peptide absorption in model organisms or cell-based systems.
Analytical method development: The compound is also valuable in the development and validation of analytical techniques for peptide detection and quantification. Its well-defined structure and physicochemical properties make it an ideal standard or calibration compound in chromatographic and mass spectrometric assays. Utilization of Pro-Ser in these contexts supports the accurate identification, separation, and quantification of dipeptides and related compounds in complex biological samples, thereby advancing the reliability and sensitivity of peptide analysis workflows.
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