Bacteriophage-liposomal therapy in complex treatment of purulent wounds in patients with antibiotic allergy

В настоящее время возникла проблема альтернативной антибиотикотерапии для пациентов с аллергией на антибиотики. Одним из альтернативных методов лечения гнойной хирургической инфекции у данных пациентов является использование бактериофагов и липосом. В работе представлены результаты комплексного лечения больных с гнойными ранами мягких тканней и аллергией на антибиотики с использованием бактериофаголипосомальной терапии, которая может быть рекомендована в качестве метода выбора для лечения воспалительных и гнойных поражений мягких тканей у этих пациентов. Introduction. Nowadays there is a problem of alternative to antibiotic therapy for patients who have allergy to antibiotics. One of the alternative treatment of purulent surgical infection in patients with allergic reactions to antibiotics is the use of bacteriophages and liposomes. Aim. To improve the results of treatment of purulent wounds of soft tissues in patients with allergies to antibiotics using bacteriophages in treatment and liposomes. Material and methods. Clinical studies conducted in 140 patients with purulent-inflammatory diseases of soft tissues that were treated in Poltava District Central Hospital, City Clinical Hospital № 3 and Poltava Garrison Military Hospital. Conclusion. Using in the treatment of inflammatory lesions of purulent soft tissue bacteriophageliposomal therapy developed by our method leads to a statistically significant decrease in duration of pain and swelling tissue, accelerate wound cleansing and the emergence of active granulation and accelerates wound healing. Use bacteriophage-liposomal therapy in the treatment of septic wounds improves the above figures also in patients who have an allergic reaction to antibiotics and can be recommended as a method of choice for the treatment of inflammatory and purulent soft tissue lesions in these patient

Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro

This work investigated in vitro aggregation and amyloid properties of skeletal myosin binding protein-C (sMyBP-C) interacting in vivo with proteins of thick and thin filaments in the sarcomeric A-disc. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) found a rapid (5–10 min) formation of large (>2 μm) aggregates. sMyBP-C oligomers formed both at the initial 5–10 min and after 16 h of aggregation. Small angle X-ray scattering (SAXS) and DLS revealed sMyBP-C oligomers to consist of 7–10 monomers. TEM and atomic force microscopy (AFM) showed sMyBP-C to form amorphous aggregates (and, to a lesser degree, fibrillar structures) exhibiting no toxicity on cell culture. X-ray diffraction of sMyBP-C aggregates registered reflections attributed to a cross-β quaternary structure. Circular dichroism (CD) showed the formation of the amyloid-like structure to occur without changes in the sMyBP-C secondary structure. The obtained results indicating a high in vitro aggregability of sMyBP-C are, apparently, a consequence of structural features of the domain organization of proteins of this family. Formation of pathological amyloid or amyloid-like sMyBP-C aggregates in vivo is little probable due to amino-acid sequence low identity (<26%), alternating ordered/disordered regions in the protein molecule, and S–S bonds providing for general stability

Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro

This work investigated in vitro aggregation and amyloid properties of skeletal myosin binding protein-C (sMyBP-C) interacting in vivo with proteins of thick and thin filaments in the sarcomeric A-disc. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) found a rapid (5&ndash;10 min) formation of large (&gt;2 &mu;m) aggregates. sMyBP-C oligomers formed both at the initial 5&ndash;10 min and after 16 h of aggregation. Small angle X-ray scattering (SAXS) and DLS revealed sMyBP-C oligomers to consist of 7&ndash;10 monomers. TEM and atomic force microscopy (AFM) showed sMyBP-C to form amorphous aggregates (and, to a lesser degree, fibrillar structures) exhibiting no toxicity on cell culture. X-ray diffraction of sMyBP-C aggregates registered reflections attributed to a cross-&beta; quaternary structure. Circular dichroism (CD) showed the formation of the amyloid-like structure to occur without changes in the sMyBP-C secondary structure. The obtained results indicating a high in vitro aggregability of sMyBP-C are, apparently, a consequence of structural features of the domain organization of proteins of this family. Formation of pathological amyloid or amyloid-like sMyBP-C aggregates in vivo is little probable due to amino-acid sequence low identity (&lt;26%), alternating ordered/disordered regions in the protein molecule, and S&ndash;S bonds providing for general stability