Background reading on peptide classes, nomenclature and receptor pharmacology as described in the published literature.
VIP is 28 residues, amidated, and carries methionine, three asparagines, two aspartates and two tyrosines. A case study in why one named impurity never describes a chromatogram.
A 24-residue mitochondria-derived peptide with an unpaired cysteine and an N-terminal methionine. Why its purity figure is time-dependent in a way most are not.
A peptide that converts into a different stable molecule on its own, seventeen daltons lighter. Which form a certificate describes, and why the proportion is not fixed.
Argireline and SNAP-8 share six residues and differ by an alanine and an aspartate. What the terminal modifications, the methionine and the poor retention mean for analysis.
A Lys-Pro-Val tripeptide that barely retains on a C18 column, has no aromatic residue and lands in a noisy region of the mass spectrum. What confirms it instead.
A 37-residue fragment of human cathelicidin carrying a net charge near plus six. Why it tails, why it adsorbs, and why the solvent changes how it folds.
A 28-residue acetylated sequence containing no tryptophan, tyrosine or phenylalanine. Why that makes 280 nm detection useless and what has to be used instead.
Hexarelin differs from GHRP-6 by fourteen daltons on a single indole ring. Easy to see on a mass spectrum, easy to miss on a chromatogram run too steeply.
Two synthetic hexapeptides separated by 55 daltons and one unnatural residue. What that difference shows on a chromatogram, in a mass spectrum, and in the impurity profile.
A CAS Registry Number is a unique identifier assigned to a chemical substance. On a peptide certificate it is one of the few fields that is unambiguous…
A peptide chain has two ends, and both are frequently modified. The changes are small in mass and large in consequence…
Where a sequence contains two or more cysteines, the finished molecule is defined not only by the order of its residues but by which cysteines are joined to which.
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