Dennison, Sarah R. team published research on Biochimica et Biophysica Acta, Biomembranes in 2022 | 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 lack the hydroxyl groups of alcohols. Without the strongly polarized O―H bond, ether molecules cannot engage in hydrogen bonding with each other. 73724-45-5, formula is C18H17NO5, Name is Fmoc-Ser-OH. Ethers do have nonbonding electron pairs on their oxygen atoms, however, and they can form hydrogen bonds with other molecules (alcohols, amines, etc.) that have O―H or N―H bonds. Application of C18H17NO5.

Dennison, Sarah R.;Reddy, Subrayal M.;Morton, Leslie H. G.;Harris, Frederick;Badiani, Kamal;Phoenix, David A. research published 《 PEGylation enhances the antibacterial and therapeutic potential of amphibian host defence peptides》, the research content is summarized as follows. Aurein 2.1, aurein 2.6 and aurein 3.1 are amphibian host defense peptides that kill bacteria via the use of lytic amphiphilic α-helical structures. The C-terminal PEGylation of these peptides led to decreased antibacterial activity (Min. Lethal Concentration (MLCs) ↓ circa one and a half to threefold), reduced levels of amphiphilic α-helical structure in solvents (α-helicity ↓ circa 15.0%) and lower surface activity (Δπ ↓ > 1.5 mN m-1). This PEGylation of aureins also led to decreased levels of amphiphilic α-helical structure in the presence of anionic membranes and zwitterionic membranes (α-helicity↓ > 10.0%) as well as reduced levels of penetration (Δπ ↓ > 3.0 mN m-1) and lysis (lysis ↓ > 10.0%) of these membranes. Based on these data, it was proposed that the antibacterial action of PEGylated aureins involved the adoption of α-helical structures that promote the lysis of bacterial membranes, but with lower efficacy than their native counterparts. However, PEGylation also reduced the haemolytic activity of native aureins to negligible levels (haemolysis ↓ from circa 10% to 3% or less) and improved their relative therapeutic indexes (RTIs ↑ circa three to sixfold). Based on these data, it is proposed that PEGylated aureins possess the potential for therapeutic development; for example, to combat infections due to multi-drug resistant strains of S. aureus, designated as high priority by the World Health Organization.

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