Understanding the interaction between light and chiral nanostructures is of fundamental importance, yet the principles governing chiral interactions have remained largely phenomenological. In this work, we present a chiral field-mode (FM) matching model to quantify the circular dichroism (CD) and helical dichroism (HD) of chiral plasmonic nanostructures interacting with beams of different spin-orbit states. The chiral FM matching model posits that among the inherent resonance modes within the nanostructure, the most efficiently excited mode is the one that matches the external field structure by possessing one more node along the vibration direction, with the field structure itself being determined by the interaction between the geometric phase and dynamic phase through a Doppler-like effect.
View Article and Find Full Text PDFBackground: This study aimed to investigate the clinical characteristics of gastric cancer (GC) patients with dermatomyositis (DM) and summarize the perioperative outcomes.
Methods: The clinical and pathological data of five patients diagnosed with co-occurring DM and GC (DM-GC group) were retrospectively analyzed, who were admitted to the Department of Gastrointestinal Surgery at Ren ji Hospital, Shanghai Jiao Tong University, between January 2012 and April 2023. Their data were compared with 618 GC patients (GC-1 group) from September 2016 to August 2017 and 35 GC patients who were meticulously screened from 14,580 GC cases from January 2012 and April 2023.
Spectrochim Acta A Mol Biomol Spectrosc
February 2023
Based on the classical Schiff base reaction, fluorescent probe dimethyl 5-((pyren-1-ylmethylene)amino)isophthalate (PAI) is designed and synthesized through introducing Schiff base structure to pyrene unit for structural modification. The structure of the synthesized probe PAI is determined and characterized by FT-IR, H NMR, C NMR and HRMS. PAI is a type of "turn-on" probe which can specifically recognize Al ion with high selectivity.
View Article and Find Full Text PDFAppl Environ Microbiol
September 2017
Proteins with high catalytic efficiency and selectivity under mild conditions have long been appreciated by industrial and medicinal fields. These proteins, which are commonly multimeric, often possess low stability, impeding wider application. Currently, strategies to improve the stability of multimeric proteins concentrate on enhancing the interaction at internal interface of the subunits.
View Article and Find Full Text PDFHalohydrin dehalogenases (HHDHs) are biocatalytically interesting enzymes due to their ability to form C-C, C-N, C-O, and C-S bonds. One of most important application of HHDH was the protein engineering of HheC (halohydrin dehalogenase from Agrobacterium radiobacter AD1) for the industrial manufacturing of ethyl (R)-4-cyano-3-hydroxybutanoate (HN), a key chiral synthon of a cholesterol-lowering drug of atorvastatin. During our development of an alternative, more efficient and economic route for chemo-enzymatic preparation of the intermediate of atorvastatin, we found that the HheC2360 previously reported for HN manufacture, had insufficient activity for the cyanolysis production of tert-butyl (3 R,5 S)-6-cyano-3,5-dihydroxyhexanoate (A7).
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