Selank is a synthetic linear heptapeptide with the amino acid sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro. The chain consists of a naturally occurring tetrapeptide motif (Thr-Lys-Pro-Arg) to which the tripeptide Pro-Gly-Pro is attached at the C-terminus. The compound bears CAS number 129954-34-3 and has the molecular formula C33<\/sub>H57<\/sub>N11<\/sub>O9<\/sub> and a molecular mass of approximately 751.9 Da (PubChem CID 11765600).<\/p>\n With three proline residues at seven positions, Selank is a distinctly proline-rich sequence. Proline limits the rotational freedom of the backbone, and the proline-glycine-proline sequence at the C-terminal end increases the rigidity of that end, thereby limiting attack by exopeptidases; under laboratory conditions, this makes the chain measurably more stable than the unextended tetrapeptide motif, which degrades rapidly in defined buffer systems. Furthermore, two strongly basic residues\u2014lysine and arginine\u2014give the molecule a high isoelectric point and a distinctly hydrophilic character, while the chain contains no aromatic residues whatsoever. Consequently, detection relies not on absorption at 280 nm, but on the peptide bond itself around 210\u2013220 nm. This combination of chain rigidity, high hydrophilicity, and the absence of a chromophore makes Selank an instructive model compound in comparative peptide research and in the development of analytical methods.<\/p>\n Within peptide chemistry and analytical work, Selank is involved in the following in vitro research areas, among others:<\/p>\nApplications in a laboratory context<\/h2>\n
\n
Specifications<\/h2>\n