Fmoc-PNA-T-OH

Description:

Fmoc-PNA-T-OH is a specialized monomer used in the synthesis of Peptide Nucleic Acids (PNAs). This monomer is designed for automated DNA synthesizers but can be adapted for other synthetic chemistry instruments, including microwave-assisted peptide synthesizers.

Key Features:

1. High-Affinity Binding: PNAs, including those synthesized with this monomer, exhibit higher binding affinity to DNA strands than DNA itself, allowing for effective use in shorter oligomer lengths of 12-15 units.

2. Aggregation Control: It's recommended to limit purine content, especially G-rich sequences, to prevent aggregation. Incorporating lysine or multiple AEAA linkers can improve solubility and handling.

3. Labelling Flexibility: Fmoc-PNA-T-OH allows for the labeling of PNA with various groups like fluorescein and biotin. Labels can be attached either to the resin before cleavage or in solution after cleavage, depending on their acid sensitivity.

4. Solid Support Compatibility: Suitable for use with solid supports like PAL-PEG-PS and XAL-PEG-PS, which are cleavable in acid and compatible with Fmoc chemistry.

5. Optimized Synthesis Protocol: The synthesis involves a repetitive cycle of deblocking, activation/coupling, and capping, typically conducted on a 2?mol scale.

Applications:

• Synthesis of short, high-affinity PNAs for DNA binding studies.
• Research in molecular biology, especially in areas requiring specific DNA sequence recognition and binding.

Fmoc-PNA-T-OH is a 3-residue synthetic peptide with the sequence Pro-Asn-Ala. These sequence-derived properties describe the reagent chemically; no specific receptor, enzyme, pathway, disease association, or biological activity is assigned without product-specific experimental evidence.

• LC-MS/HPLC analytical method development
• sequence-specific assay controls

Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions.