ABSTRACT
Fluorescence imaging in the near-infrared II (NIR-II, 1000-1700 nm) region opens up new avenues for biological systems due to suppressed scattering and low autofluorescence at longer-wavelength photons. Nonetheless, the development of organic NIR-II fluorophores is still limited mainly due to the shortage of efficient molecular design strategy. Herein, we propose an approach of designing Janus NIR-II fluorophores by introducing electronic donors with distinct properties into one molecule. As a proof-of-concept, fluorescent dye 2 TT-m, oC6B with both twisted and planar electronic donors displayed balanced absorption and emission which were absent in its parent compound. The key design strategy for Janus molecule is that it combines the merits of intense absorption from planar architecture and high fluorescence quantum yield from twisted motif. The resulting 2 TT-m, oC6B nanoparticles exhibit a high molar absorptivity of 1.12 ⨯104 M-1 cm-1 at 808 nm and a NIR-II quantum yield of 3.7%, displaying a typical aggregation-induced emission (AIE) attribute. The highly bright and stable 2 TT-m, oC6B nanoparticles assured NIR-II image-guided cancer surgery to resect submillimeter tumor nodules. The present study may inspire further development of molecular design philosophy for highly bright NIR-II fluorophores for biomedical applications.
ABSTRACT
Aggregation greatly boosts emission efficiency of the silole, turning it from a weak luminophor into a strong emitter.
ABSTRACT
A simple process for fast fabrication of thin films with biomimetic morphological structures from a group of linear homopolymers is developed. Natural evaporation of tetrahydrofuran, chloroform, and hexane-dichloromethane solutions of poly(phenylacetylene)s that contain amino acid and ethylene glycol moieties under ambient conditions instantly produces three-dimensional porous films with structural patterns reminiscent of honeycombs and radiolarian shells. Morphological analysis by optical and electronic microscopy suggests that vesicles of the amphiphilic polymers serve as building blocks in the self-organization to the biomimetic structures.
Subject(s)
Acetylene/analogs & derivatives , Acetylene/chemistry , Biomimetic Materials/chemical synthesis , Biomimetics/methods , Crystallization/methods , Nanotechnology/methods , Polymers/chemistry , Biomimetic Materials/chemistry , Chloroform/chemistry , Furans/chemistry , Hexanes/chemistry , Macromolecular Substances , Membranes, Artificial , Microscopy, Electron , Microscopy, Electron, Scanning , Molecular Conformation , Polyynes , Porosity , Solutions/chemistry , Surface Properties , Surface-Active Agents/chemistry , VolatilizationSubject(s)
Adjuvants, Immunologic/administration & dosage , Antiviral Agents/administration & dosage , Hepatitis B virus/isolation & purification , Hepatitis B, Chronic/drug therapy , Interferon-alpha/administration & dosage , Thymosin/analogs & derivatives , Thymosin/administration & dosage , Adolescent , Adult , Alanine Transaminase/blood , DNA, Viral/analysis , Follow-Up Studies , Hepatitis B e Antigens/blood , Hepatitis B virus/genetics , Humans , Middle Aged , ThymalfasinSubject(s)
Adjuvants, Immunologic/administration & dosage , Antiviral Agents/administration & dosage , Hepatitis B, Chronic/drug therapy , Interferon-alpha/administration & dosage , Thymosin/analogs & derivatives , Thymosin/administration & dosage , Adolescent , Adult , Antiviral Agents/adverse effects , Humans , Interferon-alpha/adverse effects , Middle Aged , Thymalfasin , Treatment OutcomeABSTRACT
A gene coding for the 5 S rRNA-binding protein (YL3) in yeast (Saccharomyces cerevisiae) was isolated using a polymerase chain reaction-amplified gene probe. The DNA sequence contains no introns and codes for a 297 amino acid (Mr = 33,741) protein. Although the protein is just 1 residue longer than in rat, unlike the high sequence homology in the 5 S rRNAs from the same organisms, only about 45% of the amino acid residues are conserved with surprisingly little homology in the carboxyl-terminal end. Nevertheless, comparative studies indicate that a number of structural features are conserved including small repeats in the primary structure and a number of helical estimates in the higher order structure. One of the sequence repeats also appears to be present in the carboxyl-terminal end of the eukaryotic transcription factor TFIIIA suggesting an evolutionary relationship in these 5 S RNA-binding proteins.
