Tran, Kien team published research in Journal of Medicinal Chemistry in 2021 | 73724-45-5

73724-45-5, Fmoc-Ser-OH, also known as Fmoc-Ser-OH, is a useful research compound. Its molecular formula is C18H17NO5 and its molecular weight is 327.3 g/mol. The purity is usually 95%.
Fmoc-L-Ser-OH is a synthetic peptide that belongs to the group of glycopeptides. It is used as a model for such compounds and has been shown to have antimicrobial activity in vitro against gram-positive bacteria, especially Staphylococcus epidermidis. This compound was synthesized from 3-mercaptopropionic acid and chloride in the presence of hydroxyl groups and epidermal growth factor. The synthetic pathway can be divided into three steps: (1) condensation of 3-mercaptopropionic acid with hydrochloric acid to yield 3-mercaptoacrylic acid; (2) esterification of 3-mercaptoacrylic acid with glycine to form Fmoc-L-Ser; and (3) deprotection of Fmoc protecting group., Application of C18H17NO5

Ethers do have nonbonding electron pairs on their oxygen atoms, 73724-45-5, formula is C18H17NO5, Name is Fmoc-Ser-OH. The ability to form hydrogen bonds with other compounds makes ethers particularly good solvents for a wide variety of organic compounds and a surprisingly large number of inorganic compounds. Application of C18H17NO5.

Tran, Kien;Van Den Hauwe, Robin;Sainsily, Xavier;Couvineau, Pierre;Cote, Jerome;Simard, Louise;Echevarria, Marco;Murza, Alexandre;Serre, Alexandra;Theroux, Lea;Saibi, Sabrina;Haroune, Lounes;Longpre, Jean-Michel;Lesur, Olivier;Auger-Messier, Mannix;Spino, Claude;Bouvier, Michel;Sarret, Philippe;Ballet, Steven;Marsault, Eric research published 《 Constraining the Side Chain of C-Terminal Amino Acids in Apelin-13 Greatly Increases Affinity, Modulates Signaling, and Improves the Pharmacokinetic Profile》, the research content is summarized as follows. Side-chain-constrained amino acids are useful tools to modulate the biol. properties of peptides. In this study, we applied side-chain constraints to apelin-13 (Ape13) by substituting the Pro12 and Phe13 positions, affecting the binding affinity and signaling profile on the apelin receptor (APJ). The residues 1Nal, Trp, and Aia were found to be beneficial substitutions for Pro12, and the resulting analogs displayed high affinity for APJ (Ki 0.08-0.18 nM vs Ape13 Ki 0.7 nM). Besides, constrained (D-Tic) or α,α-disubstituted residues (Dbzg; D-α-Me-Tyr(OBn)) were favorable for the Phe13 position. Compounds 47 (Pro12-Phe13 replaced by Aia-Phe, Ki 0.08 nM) and 53 (I) (Pro12-Phe13 replaced by 1Nal-Dbzg, Ki 0.08 nM) are the most potent Ape13 analogs activating the Gα12 pathways (53, EC50 Gα12 2.8 nM vs Ape13, EC50 43 nM) known to date, displaying high affinity, resistance to ACE2 cleavage as well as improved pharmacokinetics in vitro (t1/2 5.8-7.3 h in rat plasma) and in vivo.

73724-45-5, Fmoc-Ser-OH, also known as Fmoc-Ser-OH, is a useful research compound. Its molecular formula is C18H17NO5 and its molecular weight is 327.3 g/mol. The purity is usually 95%.
Fmoc-L-Ser-OH is a synthetic peptide that belongs to the group of glycopeptides. It is used as a model for such compounds and has been shown to have antimicrobial activity in vitro against gram-positive bacteria, especially Staphylococcus epidermidis. This compound was synthesized from 3-mercaptopropionic acid and chloride in the presence of hydroxyl groups and epidermal growth factor. The synthetic pathway can be divided into three steps: (1) condensation of 3-mercaptopropionic acid with hydrochloric acid to yield 3-mercaptoacrylic acid; (2) esterification of 3-mercaptoacrylic acid with glycine to form Fmoc-L-Ser; and (3) deprotection of Fmoc protecting group., Application of C18H17NO5

Referemce:
Ether – Wikipedia,
Ether | (C2H5)2O – PubChem