ABSTRACT
SUMMARY: The finger or thumb tip was used as a homodigital neurovascular island flap ('top-hat flap') to reconstruct 28 segmental defects of the distal phalanx, nailbed or pulp over a 7-year period with a minimum follow-up of 12 months. All flaps survived and all fractures united. 75% of patients achieved full range-of-motion at the distal interphalangeal joint, 71% achieved 2-point discrimination <6mm and 92% returned to their preinjury unrestricted job less than 3 months after injury. The average digit AMA5 impairment score was 19%. The top-hat flap is an option for the treatment of complex injuries of the finger or thumb tip where there is a segmental defect in the nailbed, distal phalanx or pulp and a neurovascularly intact finger or thumb tip.
Subject(s)
Informed Consent/standards , Medical Staff, Hospital/education , Patient Education as Topic/methods , Cross-Sectional Studies , Female , Health Knowledge, Attitudes, Practice , Humans , Informed Consent/ethics , Male , Medical Staff, Hospital/ethics , Patient Education as Topic/ethics , Patient Education as Topic/standards , Pregnancy , Surveys and QuestionnairesABSTRACT
The fluorescence of BODIPY and click-BODIPY dyes was found to substantially increase in the presence of bovine serum albumin (BSA). BSA acted as a solubilizer for dye aggregates, in addition to being a conventional binding scaffold for the click-BODIPY dyes, indicating that disaggregation of fluorophores should be considered when evaluating dye-protein interactions.
Subject(s)
Boron Compounds/metabolism , Serum Albumin, Bovine/metabolism , Animals , Boron Compounds/chemistry , Cattle , Click Chemistry , Fluorescent Dyes/chemistry , Fluorescent Dyes/metabolism , Protein Binding , Serum Albumin, Bovine/chemistry , Spectrometry, FluorescenceABSTRACT
Photophysical behaviour of a novel trimeric BODIPY rotor with a high extinction coefficient is reported. Steady state and time resolved fluorescence measurements established that the trimer could be used as a viscometer for molecular solvents, membrane-like environments and several cancer cell lines.
Subject(s)
Boron Compounds/chemistry , Polymers/chemistry , Triazines/chemistry , ViscosityABSTRACT
Clavicular fractures account for around 15% of fractures in children. Although nonunion is a recognized complication in adults, post-traumatic nonunion of the clavicle in children is extremely rare. To the best of our knowledge, post-traumatic nonunion of the clavicle in a child following repeated clavicular fracture has not yet been published in the English literature. Here, we report a case of a 9-year-old boy who presented with post-traumatic nonunion of his right clavicle following his third fracture after radiologically documented healing of the first two fractures. He underwent open reduction and internal fixation, supplemented with ipsilateral iliac crest bone graft, with resultant healing on follow-up radiographs.
Subject(s)
Clavicle/injuries , Fractures, Bone/surgery , Fractures, Ununited/surgery , Accidental Falls , Child , Humans , MaleABSTRACT
A symmetrical BODIPY-BODIPY dyad with a diyne linker was prepared in two steps; the lifetime decay of this rotor appeared to correlate with the viscosity of the media, thus making this dyad a suitable small molecule viscometer for molecular solvents. The potential of using the rotor to probe the viscosity of ionic liquids was also investigated.
ABSTRACT
Dye-binding assays, such as those utilizing Congo red and thioflavin T, are among the most widely used tools to probe the aggregation of amyloidogenic biomolecules and for the evaluation of small molecule inhibitors of amyloid aggregation and fibrillization. A number of recent reports have indicated that these dye-binding assays could be prone to false positive effects when assessing inhibitors' potential toward Aß peptides, species involved in Alzheimer's disease. Specifically, this review focuses on the application of thioflavin T for determining the efficiency of small molecule inhibitors of Aß aggregation and addresses potential reasons that might be associated with the false positive effects in an effort to increase reliability of dye-binding assays.
Subject(s)
Amyloid beta-Peptides/pharmacokinetics , Drug Discovery/methods , Fluorescent Dyes/pharmacokinetics , Thiazoles/pharmacokinetics , Alzheimer Disease/drug therapy , Amyloid beta-Peptides/antagonists & inhibitors , Benzothiazoles , Coloring Agents/pharmacokinetics , Congo Red/pharmacokinetics , False Positive Reactions , Humans , Reproducibility of ResultsABSTRACT
A straightforward functionalization of BODIPY dyes via incorporation of a triazole moiety produced fluorescent dyes that were capable of distinguishing between secondary structure conformations of soluble oligomeric species of Abeta1-42 peptide. Small concentrations of the dyes, relative to Abeta1-42, provided up to an 8-fold and 35-fold fluorescence increase in the presence of the unordered and ordered, beta-sheet-rich conformations of soluble Abeta1-42 oligomers, respectively. These triazole-containing dyes could prove to be useful probes for monitoring amyloid conformational transitions in vitro.
Subject(s)
Alzheimer Disease/metabolism , Amyloid beta-Peptides/chemistry , Boron Compounds/chemistry , Fluorescent Dyes/chemistry , Peptide Fragments/chemistry , Triazoles/chemistry , Humans , Protein ConformationABSTRACT
Amphotericin B has recently been suggested as an efficient inhibitor of amyloid peptide fibril formation; however its interactions with more neurotoxic, soluble forms of amyloid peptides have not been reported to date. Circular dichroism spectroscopy allowed for distinguishing between the binding and inhibition of aggregation events: amphotericin B distinctly interacts with both unordered and ordered, beta-structure-rich soluble oligomeric forms of Abeta1-42 peptide, yet amphotericin B has no measurable impact neither on the secondary structure nor on time-dependent aggregation profile of the amyloid peptide.
