1. Sequence-assisted peptide synthesis (SAPS)
B Due Larsen, A Holm J Pept Res. 1998 Dec;52(6):470-6. doi: 10.1111/j.1399-3011.1998.tb01251.x.
In solid-phase peptide synthesis (SPPS) the growing peptide chain may undergo chain aggregation which can cause serious synthetic problems. A number of investigations concerning this problem have been reported in the chemical literature. During a study of such "difficult sequences" using the Fmoc-protection strategy, we have observed that peptide-chain aggregation may be significantly reduced when certain amino acid sequences are incorporated C-terminally (1). Thus, synthesis of the difficult poly-alanine, (Ala)n, sequence (n < or = 20) has been investigated with (Lys(Boc))m (m < or = 6) and (Glu(tBu))m (m > or = 6) as pre-sequences. With m > or = 3, peptides are obtained as single, homogeneous products while a complex mixture of deletion peptides and corresponding Fmoc-protected peptides is formed (n > or = 6) without the pre-sequence. A mixed pre-sequence, (Lys(Boc)Glu(tBu))3, has a similar favorable effect on the synthetic results, but the positive effect seems confined to a rather narrow framework of amino acids and side-chain protecting groups in the pre-sequence as discussed in the article. Among other reputedly difficult sequences the synthesis of H-(Thr-Val)5-OH, H-Val-Asn-Val-Asn-Val-Gln-Val-Gln-Val-Asp-OH, the Acyl Carrier Protein (65-74) and the human insulin B-chain has been investigated. In all cases introduction of a pre-sequence gives rise to satisfactory synthetic results. In the latter case, the lysine pre-sequence may be cleaved enzymatically to give the desB30 insulin B-chain. NIR-FT Raman studies of the synthesis of the poly-alanine, (Ala)n, sequences have shown that the pre-sequence (Lys(Boc))6 shifts the conformation of the growing peptide chain from a beta-structure (n > or = 6) to a random coil conformation (1c). This result is in agreement with the general observation that SPPS proceeds optimally under random coil conditions.
2. A Simple & Convenient Solid Phase Synthesis of Bacterial Origin Octapeptide Sequence, Glu-Asp-Gly-Asn-Lys-Pro-Gly-Lys-OH
Riaz A Khan Int J Pept Res Ther. 2010 Mar;16(1):39-42. doi: 10.1007/s10989-010-9200-5. Epub 2010 Mar 3.
The repeating octapeptide sequence, Glu-Asp-Gly-Asn-Lys-Pro-Gly-Lys-OH derived from the glycoprotein found in Staphylococcus aureus cell wall is assembled by simple solid phase peptide synthesis methodology using a base labile linker.
3. Neurotensin: peptide for the next millennium
B M Tyler-McMahon, M Boules, E Richelson Regul Pept. 2000 Sep 25;93(1-3):125-36. doi: 10.1016/s0167-0115(00)00183-x.
Neurotensin is an endogenous tridecapeptide neurotransmitter (pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Try-Ile-Leu-OH) that was discovered by Carraway and Leeman in bovine hypothalami in the early 1970s. Since then this peptide has been the subject of a multitude of articles detailing discoveries related to its activity, receptors, localization, synthesis, and interactions with other systems. This review article does not intend to summarize again all the history of this fascinating peptide and its receptors, since this has been done quite well by others. The reader will be directed to these other reviews, where appropriate. Instead, this review attempts to provide a summary of current knowledge about neurotensin, why it is an important peptide to study, and where the field is heading. Special emphasis is placed on the behavioral studies, particularly with reference to agonists, antagonists, and antisense studies, as well as, the interaction of neurotensin with other neurotransmitters.
