Scrambling of sequence information in collision-induced dissociation of peptides
Scrambling of sequence information in collision-induced dissociation of peptides
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DOI：
10.1021/ja062440h
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发表时间：
2006-08-16
影响因子：
15
通讯作者：
Paizs, Bela
中科院分区：
文献类型：
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作者：
Harrison, Alex G.;Young, Alex B.;Paizs, Bela
质子化的YAGFL-NH 2的碰撞诱导解离（CID）导致不能直接从一级肽结构衍生的非直接序列碎片离子。实验和理论证据表明，完整肽的初级断裂导致具有C-末端恶唑酮环的线性YAGFLoxab 5离子，其被N-末端氨基攻击以诱导形成环状肽deb 5异构体。后者可以进行各种质子转移反应，并打开形成YAGFL-NH 2异构体以外的物质，导致质子化YAGFL-NH 2 CID中序列信息的混乱。
Collision-induced dissociation (CID) of protonated YAGFL-NH2leads tonondirect sequencefragment ions that cannot directly be derived from the primary peptide structure. Experimental and theoretical evidence indicate that primary fragmentation of the intact peptide leads to the linear YAGFLoxab5ion with a C-terminal oxazolone ring that is attacked by the N-terminal amino group to induce formation of a cyclic peptideb5isomer. The latter can undergo various proton transfer reactions and opens up to form something other than the YAGFLoxalinearb5isomer, leading to scrambling of sequence information in the CID of protonated YAGFL-NH2.