Capture of carbon monoxide using a heme protein model: from biomimetic chemistry of heme proteins to physiological and therapeutic applications
Capture of carbon monoxide using a heme protein model: from biomimetic chemistry of heme proteins to physiological and therapeutic applications
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DOI：
10.1038/s41428-021-00591-y
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发表时间：
2021-11
期刊：
影响因子：
2.8
通讯作者：
Hiroaki Kitagishi;Qiyue Mao
中科院分区：
文献类型：
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作者：
Hiroaki Kitagishi;Qiyue Mao
血红蛋白（Hb）和肌红蛋白（Mb）是血红素蛋白，在生物体中捕获和运输分子氧（O2）。虽然使用合成铁卟啉模拟Hb和Mb的O2结合功能已经被广泛研究了40多年，但在体内或100%水溶液中模拟Hb/Mb的功能的研究最少。因此，使用5，10，15，20-四（4-磺酸基苯基）卟啉铁（II）（FeIITPPS）与具有吡啶接头的全-O-甲基化β-环糊精二聚体（Py 3CD）的1：1包合物构建了称为“hemoCD 1”的超分子复合物作为水合成Hb/Mb模型。选择性体内一氧化碳（CO）耗竭有利于研究内源性CO作为气体信号信使的生理作用。HemoCD 1在环境温度下可逆结合水溶液中的O2和CO。因此，由于其对CO的极高结合亲和力，hemoCD 1被用作体内选择性CO清除剂。此外，hemoCD 1被用于定量器官/组织中内源性和外源性CO的蓄积。最后，将hemoCD 1用作动物CO中毒的解毒剂。因此，最近的事态发展，在hemoCD 1已经揭示，水仿生血红素蛋白模型具有显着的生理和治疗应用潜力。
Hemoglobin (Hb) and myoglobin (Mb) are heme proteins that capture and transport molecular oxygen (O2) in living organisms. Although mimicking the O2-binding function of Hb and Mb using synthetic iron-porphyrin has been extensively studied for over 40 years, mimicking the function of Hb/Mb in vivo or 100% aqueous solutions has been minimally studied. Hence, a supramolecular complex termed “hemoCD1” was constructed as the aqueous synthetic Hb/Mb model using a 1:1 inclusion complex of 5,10,15,20-tetrakis(4-sulfonatophenyl)porphinatoiron(II) (FeIITPPS) with a per-O-methylated β-cyclodextrin dimer with a pyridine linker (Py3CD). Selective carbon monoxide (CO) depletion in vivo is beneficial for studying the physiological roles of endogenous CO as a gaseous signal messenger. HemoCD1 reversibly binds O2and CO in aqueous solution at ambient temperature. Hence, hemoCD1 was used as a selective CO scavenger in vivo due to its extremely high binding affinity to CO. In addition, hemoCD1 was utilized to quantify the accumulation of endogenous and exogenous CO in organs/tissues. Finally, hemoCD1 was employed as an antidote for CO poisoning in animals. Thus, recent developments in hemoCD1 have revealed that the aqueous biomimetic heme protein model has significant physiological and therapeutic application potential.