Okamoto Hideyuki, Murano Shuko Amber, Ikekawa Kaoru, Katsuyama Masahiro, Konno Sho, Taguchi Akihiro, Takayama Kentaro, Taniguchi Atsuhiko, Hayashi Yoshio
Department of Medicinal Chemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences Hachioji Tokyo 192-0392 Japan
Department of Environmental Biochemistry, Kyoto Pharmaceutical University 5 Misasaginakauchi-cho, Yamashina Kyoto 607-8414 Japan.
RSC Med Chem. 2023 Jan 3;14(2):386-392. doi: 10.1039/d2md00425a. eCollection 2023 Feb 22.
Inhibition of myostatin is an attractive strategy for the treatment of muscular atrophic diseases such as muscular dystrophy. For the efficient inhibition of myostatin, functionalized peptides were developed by the conjugation of a 16-mer myostatin-binding d-peptide with a photooxygenation catalyst. These peptides induced myostatin-selective photooxygenation and inactivation under near-infrared irradiation, and were associated with little cytotoxicity or phototoxicity. The peptides are resistant to enzymatic digestion due to their d-peptide chains. These properties could contribute to the use of photooxygenation-based inactivation strategies targeting myostatin.
抑制肌肉生长抑制素是治疗诸如肌肉萎缩症等肌肉萎缩性疾病的一种有吸引力的策略。为了有效抑制肌肉生长抑制素,通过将一种16聚体肌肉生长抑制素结合d肽与一种光氧化催化剂偶联来开发功能化肽。这些肽在近红外照射下诱导肌肉生长抑制素选择性光氧化和失活,并且几乎没有细胞毒性或光毒性。由于其d肽链,这些肽对酶消化具有抗性。这些特性可能有助于基于光氧化的针对肌肉生长抑制素的失活策略的应用。