FAQs
Technical
- What are pseudoproline amino acids and what advantage do they have in peptide synthesis?
- What are the typical contaminants associated with peptide synthesis?
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What is the difference between peptide purity and peptide yield?
Peptide purity is determined using analytical methods such as RP-HPLC and MS analysis. It provides a percentage of the sample which is detected using UV absorbance of certain chemical moieties (for HPLC) or charged species in the case of MS. It does not identify the contribution of water and salts in the sample, for example.
Amino Acid Analysis is used to calculate the yield or actual amount of peptide only in the peptide sample. In this way, the moles of peptide can be calculated and the difference between the weighed mass (before AAA) and the measured result (after AAA) is normally attributable to water and salts.
- What are the typical salts associated with my peptide?
- If I have biotin in my peptide, do I need a spacer between the biotin group and the peptide sequence and if so which spacer should I use?
- What can I do to increase the cell permeability of a peptide?
- How do I solubilize my peptides?
- How do I characterize batches of my "drug candidate" peptide, which contains a D-amino acid?
- How do you calculate hydrophobicity?