Muranov K O, Dizhevskaia A K, Boldyrev A A, Karpova O E, Sheremet N L, Polunin G S, Avetisov S E, Ostrovskiĭ M A
Vestn Oftalmol. 2008 Mar-Apr;124(2):3-6.
Aggregation ofcrystallins, the lens proteins, is one of the basic stages of cataract formation. Among the protein aggregation models used to study the molecular mechanisms of the initial stages of lenticular opacity, UV-induced aggregation of betaL-crystallin is most close to the in vivo conditions. The carnosine derivative N-acetyl carnosine has been shown to be effective in inhibiting the UV-induced aggregation of betaL-crystallin. Examination of the accumulation kinetics of carbonyl groups in betaL-crystallin under UV irradiation has indicated that neither carnosine nor N-acetyl carnosine fails to affect this parameter--an indicator of oxidative protein damage. By taking into account also the fact that N-acetyl carnosine is not an antioxidant, it can be believed that the molecular mechanism of action of this compound on UV-induced aggregation of betaL is unassociated with its antioxidative properties. The authors hypothesize that the molecular chaperon-like properties similar to those of alpha-crystallin underlie the mechanism of action of the acetyl derivative carnosine. The prospects for searching anticataract agents of a new chaperon-like class are discussed.
晶状体蛋白（即晶体蛋白）的聚集是白内障形成的基本阶段之一。在用于研究晶状体混浊初始阶段分子机制的蛋白质聚集模型中，紫外线诱导的βL-晶体蛋白聚集最接近体内情况。已证明肌肽衍生物N-乙酰肌肽可有效抑制紫外线诱导的βL-晶体蛋白聚集。对紫外线照射下βL-晶体蛋白中羰基积累动力学的研究表明，肌肽和N-乙酰肌肽均未影响该参数——蛋白质氧化损伤的指标。同时考虑到N-乙酰肌肽不是抗氧化剂这一事实，可以认为该化合物对紫外线诱导的βL聚集的作用分子机制与其抗氧化特性无关。作者推测，类似于α-晶体蛋白的分子伴侣样特性是乙酰肌肽衍生物作用机制的基础。文中还讨论了寻找新型分子伴侣样抗白内障药物的前景。
