Centocor Research & Development, Inc., 145 King of Prussia Rd., Radnor, PA 19087, USA.
J Mass Spectrom. 2011 Jul;46(7):677-88. doi: 10.1002/jms.1938.
This paper describes a method for the fast identification and composition of disulfide-bonded peptides. A unique fragmentation signature of inter-disulfide-bonded peptides is detected using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF)/TOF mass spectrometry and high-energy collision-induced dissociation (CID). This fragmentation pattern identifies peptides with an interconnected disulfide bond and provides information regarding the composition of the peptides involved in the pairing. The distinctive signature produced using CID is a triplet of ions resulting from the cleavage of the disulfide bond to produce dehydroalanine, cysteine or thiocysteine product ions. This method is not applicable to intra-peptide disulfide bonds, as the cleavage mechanism is not the same and a triplet pattern is not observed. This method has been successfully applied to identifying disulfide-bonded peptides in a number of control digestions, as well as study samples where disulfide bond networks were postulated and/or unknown.
本文介绍了一种快速鉴定和组成二硫键结合肽的方法。采用基质辅助激光解吸/电离（MALDI）飞行时间（TOF）/TOF 质谱和高能碰撞诱导解离（CID）技术，检测到二硫键结合肽的独特碎裂特征。这种碎裂模式可识别具有相互连接的二硫键的肽，并提供有关参与配对的肽组成的信息。CID 产生的独特特征是由二硫键断裂产生脱氢丙氨酸、半胱氨酸或硫代半胱氨酸产物离子的三离子对。该方法不适用于肽内二硫键，因为裂解机制不同，不会观察到三离子对模式。该方法已成功应用于鉴定许多对照消化物中的二硫键结合肽，以及假定和/或未知二硫键网络的研究样本。
