131509-64-3Relevant academic research and scientific papers
Synthesis and NMR Characterization of the Prenylated Peptide, a-Factor
Bader, Taysir K.,Rappe, Todd M.,Veglia, Gianlugi,Distefano, Mark D.
, p. 207 - 238 (2019)
Protein and peptide prenylation is an essential biological process involved in many signal transduction pathways. Hence, it plays a critical role in establishing many major human ailments, including Alzheimer's disease, amyotrophic lateral sclerosis (ALS), malaria, and Ras-related cancers. Yeast mating pheromone a-factor is a small dodecameric peptide that undergoes prenylation and subsequent processing in a manner identical to larger proteins. Due to its small size in addition to its well-characterized behavior in yeast, a-factor is an attractive model system to study the prenylation pathway. Traditionally, chemical synthesis and characterization of a-factor have been challenging, which has limited its use in prenylation studies. In this chapter, a robust method for the synthesis of a-factor is presented along with a description of the characterization of the peptide using MALDI and NMR. Finally, complete assignments of resonances from the isoprenoid moiety and a-factor from COSY, TOCSY, HSQC, and long-range HMBC NMR spectra are presented. This methodology should be useful for the synthesis and characterization of other mature prenylated peptides and proteins.
Highly efficient synthetic method on pyroacm resin using the boc SPPS protocol for C-terminal cysteine peptide synthesis
Juvekar, Vinayak,Kim, Kang-Tae,Gong, Young-Dae
, p. 54 - 62 (2017)
A very effective process on Pyroacm resin was developed for solid-phase peptide synthesis (SPPS) of C-terminal cysteine and cysteine ester peptides. The process uses cysteine side chain anchoring to the Pyroacm resin and the Boc protocol for SPPS. The Pyroacm resin showed remarkable stability under standard trifluoromethanesulfonic acid (TFMSA) cleavage condition. TFMSA cleavage of protecting groups generates a peptide-linked resin, which can be subjected to peptide modification reactions. Finally, the peptide can be cleaved from the resin using methoxycarbonylsulfenyl chloride. The utility of this protocol was demonstrated by its applications to the synthesis of model peptides, key intermediates in the preparation of natural products riparin 1.2 and a-factor.
EPIMERIZATION-FREE N TO C SOLID-PHASE PEPTIDE SYNTHESIS
-
Paragraph 0060; 0157, (2020/03/09)
The present disclosure provides a method of solid-phase peptide synthesis from the N terminus to C terminus without detectable epimerization of the C-terminal amino acid.
Synthesis of peptides containing C -terminal methyl esters using trityl side-chain anchoring: Application to the synthesis of a-factor and a-factor analogs
Diaz-Rodriguez, Veronica,Mullen, Daniel G.,Ganusova, Elena,Becker, Jeffrey M.,Distefano, Mark D.
supporting information, p. 5648 - 5651 (2013/01/15)
A new cysteine anchoring method was developed for the synthesis of peptides containing C-terminal cysteine methyl esters. This method consists of attachment of Fmoc-Cys-OCH3 to either 2-ClTrt-Cl or Trt-Cl resins (via the side-chain thiol) followed by preparation of the desired peptide using Fmoc-based SPPS. We applied this method to the synthesis of the mating pheromone a-factor and a 5-FAM labeled a-factor analog. The peptides were obtained with high yield and purity and were shown to be bioactive in a growth arrest assay.
Synthesis of a-factor peptide from Saccharomyces cerevisiae and photoactive analogues via Fmoc solid phase methodology
Mullen, Daniel G.,Kyro, Kelly,Hauser, Melinda,Gustavsson, Martin,Veglia, Gianluigi,Becker, Jeffery M.,Naider, Fred,Distefano, Mark D.
experimental part, p. 490 - 497 (2011/02/27)
a-Factor from Saccharomyces cerevisiae is a farnesylated dodecapeptide involved in mating. The molecule binds to a G-protein coupled receptor and hence serves as a simple system for studying the interactions between prenylated molecules and their cognate
