Ethers can again be classified into two varieties: if the alkyl or aryl groups are the same on both sides of the oxygen atom, 73724-45-5, formula is C18H17NO5, Name is Fmoc-Ser-OH. Then it is a simple or symmetrical ether, whereas if they are different, the ethers are called mixed or unsymmetrical ethers. Reference of 73724-45-5.
Babych, Margaryta;Nguyen, Phuong Trang;Cote-Cyr, Melanie;Kihal, Nadjib;Quittot, Noe;Golizeh, Makan;Sleno, Lekha;Bourgault, Steve research published 《 Site-specific alkylation of the islet amyloid polypeptide accelerates self-assembly and potentiates perturbation of lipid membranes》, the research content is summarized as follows. The accumulation of insoluble amyloids in the pancreatic islets is a pathol. hallmark of type II diabetes and correlates closely with the loss of β-cell mass. The predominant component of these amyloid deposits is the islet amyloid polypeptide (IAPP). The factors contributing to the conversion of IAPP from a monomeric bioactive peptide hormone into insoluble amyloid fibrils remain partially elusive. In this study, we investigated the effect of the oxidative non-enzymic post-translational modification induced by the reactive metabolite 4-hydroxynonenal (HNE) on IAPP aggregation and cytotoxicity. Incubation of IAPP with exogenous HNE accelerated its self-assembly into β-sheet fibrils and led to the formation of a Michael adduct on the His-18 side chain. To model this covalent modification, the imidazole N(π) position of histidine was alkylated using a close analog of HNE, the octyl chain. IAPP lipidated at His-18 showed a hastened random coil-to-β-sheet conformational conversion into fibrillar assemblies with a distinct morphol., a low level of binding to thioflavin T, and a high surface hydrophobicity. Introducing an octyl chain on His-18 enhanced the ability of the peptide to perturb synthetic lipid vesicles, to permeabilize the plasma membrane, and to induce the death of pancreatic β-cells. Alkylated IAPP triggered the self-assembly of unmodified IAPP by prompting primary nucleation and increased its capacity to perturb the plasma membrane, indicating that only a small proportion of the modified peptide is necessary to shift the balance toward the formation of proteotoxic species. This study underlines the importance of studying IAPP post-translational modifications induced by oxidative metabolites in the context of pancreatic amyloids.
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., Reference of 73724-45-5
Referemce:
Ether – Wikipedia,
Ether | (C2H5)2O – PubChem