Separation of Neutral Amino Acids with Ligand Exchange Resins

Four neutral amino acids (Gly, Ala,.Val and Leu) were separated with ligand exchange resins. The separation capacity of the ligand exchange resins is compared with that of common ion exchange resins. The effects of eluent, column temperature, and central metal ions of the support on the separation are studied. The relationship between matrix structure of resins and their separation capacity is analysed.

Exploring novel cell cryoprotectants based on neutral amino acids

Cryoprotectants play a key role in cell cryopreservation because they can reduce cryoinjuries to cells associated with ice formation.To meet the clinical requirements of cryopreserved cells,cryoprotectants should be biocompatible,highly efficient and easily removable from cryopreserved cells.However,integration of these properties into one cryoprotectant still remains challenging.Herein,three biocompatible neutral amino acids,includingβ-alanine,γ-aminobutyric acid andε-aminocaproic acid,are first reported to have the potential as such ideal cryoprotectants.The results demonstrate that they can inhibit ice formation and reduce osmotic stress to provide extracellular and intracellular protection,thereby ensuring high cryopreservation efficiency for both anuclear and nucleated cells.More importantly,due to the remarkable osmotic regulation ability,the neutral amino acids can be rapidly removed from cryopreserved cells via a one-step method without causing observable damage to cells,superior to the current state-of-the-art cryoprotectants—dimethyl sulfoxide and glycerol.This work provides a new perspective to develop novel cryoprotectants,which may have dramatic impacts on solvent-free cryopreservation technology to support the cell-based applications,such as cell therapy and tissue engineering,etc.

A selectively suppressing amino acid transporter: Sodium-coupled neutral amino acid transporter 2 inhibits cell growth and mammalian target of rapamycin complex 1 pathway in skeletal muscle cells

Sodium-coupled neutral amino acid transporter 2(SNAT2),also known as solute carrier family 38 member 2(SLC38 A2),is expressed in the skeletal muscle.Our research previously indicated that SNAT2 m RNA expression level in the skeletal muscle was modulated by genotype and dietary protein.The aim of this study was to investigate the key role of the amino acid transporter SNAT2 in muscle cell growth,differentiation,and related signaling pathways via SNAT2 suppression using the inhibitor a-methylaminoisobutyric acid(Me AIB).The results showed that SNAT2 suppression down-regulated both the m RNA and protein expression levels of SNAT2 in C2 C12 cells,inhibited cell viability and differentiation of the cell,and regulated the cell distribution in G0/G1 and S phases(P<0.05).Meanwhile,most of the intercellular amino acid content of the cells after Me AIB co-culturing was significantly lower(P<0.05).Furthermore,the m RNA expression levels of system L amino acid transporter 1(LAT1),silent information regulator 1,and peroxisome proliferator-activated receptor-gamma co-activator 1 alpha,as well as the protein expression levels of amino acid transporters LAT1 and vacuolar protein sorting 34,were all down-regulated.The phosphorylated protein expression levels of mammalian target of rapamycin(m TOR),regulatory-associated protein of m TOR,4 E binding protein 1,and ribosomal protein S6 kinase 1 after Me AIB treatment were also significantly down-regulated(P<0.05),which could contribute to the importance of SNAT2 in amino acid transportation and skeletal muscle cell sensing.In conclusion,SNAT2 suppression inhibited C2 C12 cell growth and differentiation,as well as the availability of free amino acids.Although the m TOR complex 1 signaling pathway was found to be involved,its response to different nutrients requires further study.