RESUMO
Relapsing polychondritis (RP) is a rare systemic autoimmune disease characterized by episodic, progressive inflammatory destruction of cartilage. It can occur as an overlap syndrome in patients with other rheumatologic conditions. The disease usually follows an indolent relapsing-remitting course, but occasionally it can progress rapidly and even cause death. Although auricular or nasal chondritis or peripheral arthritis without other significant organ involvement are usually treated with low-dose corticosteroids, other more severe disease manifestations may require treatment with high-dose corticosteroids or other immunosuppressive agents. Biological targeted therapies might prove to be effective treatments of this condition.
Assuntos
Artrite Reumatoide/epidemiologia , Síndromes Mielodisplásicas/epidemiologia , Policondrite Recidivante , Espondiloartropatias/epidemiologia , Vasculite/epidemiologia , Anticorpos Monoclonais/uso terapêutico , Anticorpos Monoclonais Humanizados/uso terapêutico , Comorbidade , Cartilagem da Orelha/patologia , Glucocorticoides/uso terapêutico , Humanos , Imunossupressores/uso terapêutico , Terapia de Alvo Molecular , Policondrite Recidivante/tratamento farmacológico , Policondrite Recidivante/epidemiologia , Policondrite Recidivante/patologiaRESUMO
Polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) was applied to investigate the interaction of bovine serum albumin (BSA) and fibrinogen with a biomedical-grade 316LVM stainless steel surface, in terms of the adsorption thermodynamics and adsorption-induced secondary structure changes of the proteins. Highly negative apparent Gibbs energy of adsorption values revealed a spontaneous adsorption of both proteins onto the surface, accompanied by significant changes in their secondary structure. It was determined that, at saturated surface coverages, lateral interactions between the adsorbed BSA molecules induced rather extensive secondary structure changes. Fibrinogen's two coiled coils appeared to undergo negligible secondary structure changes upon adsorption of the protein, while large structural rearrangements of the protein's globular domains occurred upon adsorption. The secondary structure of adsorbed fibrinogen was not influenced by lateral interactions between the adsorbed fibrinogen molecules. PM-IRRAS was deemed to be viable for investigating protein adsorption and for obtaining information on adsorption-induced changes in their secondary structures.
