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1.
Otolaryngol Head Neck Surg ; 170(2): 405-413, 2024 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-37702155

RESUMO

OBJECTIVE: This study sought to analyze the efficacy and safety of postoperative prednisone to reduce reliance on opioids in adult benign oropharyngeal surgery. STUDY DESIGN: Prospective cohort study. SETTING: Single tertiary-care facility. METHODS: Patients undergoing tonsillectomy (T), tonsillectomy and adenoidectomy (T&A), and/or modified uvulopalatopharyngoplasty (UPPP) from December 2020 to January 2023 received the standard of care postoperative management. A prednisone taper was dependent on surgeon preference. Cohorts were based on the prescription of postoperative steroids. Patients completed a survey to assess opioid usage, pain scores, and steroid compliance. RESULTS: Seventy-two patients were included. The nonsteroid cohort (N = 29) received an average of 467 ± 94.1 morphine milligram equivalents (MME), and the steroid cohort (N = 43) received an average of 285 ± 128 MME (P < 0.001). The nonsteroid cohort consumed 1.62 times more opioids than the steroid cohort (P < 0.002). There were no significant differences in complication or refill rates between treatment groups. There were no significant differences in pain scores on the day of surgery or postoperative days 1, 5, or 10 (P = 0.34, P = 0.66, P = 0.62, and P = 0.22, respectively). Patients undergoing T&A (p = 0.019) or who had current psychiatric medication use (P < 0.006) consumed significantly more opioids. Patients who received a total opioid prescription of >300 MME (40 5-mL doses of 5 mg/5 mL liquid oxycodone) consumed 2.27 times more postoperative opioids than patients with opioid prescriptions ≤300 MME (P < 0.001). CONCLUSION: Patients who did not receive steroids consumed 1.62 times more postoperative opioids compared to those who completed a steroid taper. Corticosteroid use was not associated with changes in pain scores, refill rates, or complication rates and may be considered in a multimodal approach to pain management in adults undergoing benign oropharyngeal surgery, although further study is warranted.


Assuntos
Analgésicos Opioides , Endrin/análogos & derivados , Transtornos Relacionados ao Uso de Opioides , Adulto , Humanos , Analgésicos Opioides/uso terapêutico , Prednisona/uso terapêutico , Dor Pós-Operatória/tratamento farmacológico , Dor Pós-Operatória/etiologia , Estudos Prospectivos , Estudos Retrospectivos , Padrões de Prática Médica
2.
Chem Rev ; 119(17): 9915-9949, 2019 09 11.
Artigo em Inglês | MEDLINE | ID: mdl-31045350

RESUMO

The α-helix is the most commonly found natural secondary structure in proteins and is intrinsic to many protein-protein interactions involved in important biological functions. Novel peptides designed to mimic helices found in nature employ a variety of methods to control their structure. These approaches are significant due to potential applications in developing new therapeutic agents and materials. Over the years, many strategies have emerged to influence, initiate, and propagate helical content in short, synthetic peptides. Early innovations used the natural macrocycle tether of disulfide bond formation, metal-mediated or lactam group addition as a means to prompt helical formation. These examples have been applied to a host of peptides as inhibitors toward relevant diseases including cancer, viral and bacterial infection. In the most recent decades, hydrocarbon bridges to "staple" peptides across side chains or hydrogen bond surrogates in the backbone of peptides have been effective in producing biologically functional, helical peptidomimetics with non-natural elements, increased protease resistance and potency in vitro and in vivo. Modern methods expand and elaborate these, with applications of functional peptides from both synthetic and recombinant origins. Overall, efforts persist using these strategies to create peptides with great biological potential and a better understanding of the control of helical structure in protein folding.


Assuntos
Peptídeos/química , Proteínas/química , Alcenos/síntese química , Alcenos/química , Sequência de Aminoácidos , Animais , Antineoplásicos/química , Antineoplásicos/farmacologia , Bactérias/química , Ciclização , Fungos/química , HIV-1/química , Humanos , Lactamas/síntese química , Lactamas/química , Metais Pesados/química , Peptídeos/farmacologia , Conformação Proteica em alfa-Hélice/efeitos dos fármacos , Domínios Proteicos
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