Collision-induced dissociation (CID) with ESI-MS was used to obtain structural information on early-stage aggregation of hIAPP (human islet amyloid polypeptide) monomers and oligomers. MS analysis showed that the hIAPP monomers and oligomers were multiply charged. MS/MS analysis indicated that the hIAPP monomers adopt different structures depending on the parent ion charge state. The fragmentation patterns indicated structural similarity of M²⁺ & M³⁺ and M⁴⁺ & M⁵⁺ (M = monomer). MS/MS analysis of the dimers showed that D⁵⁺ (D = dimer) comprised M²⁺ and M³⁺ subunits, and the peptide bond dissociated in the 15−37 residue region of the monomer subunit.

使用ESI-MS的碰撞诱导解离（CID）获得有关hIAPP（人类胰岛淀粉样多肽）单体和寡聚体早期聚集的结构信息。MS分析表明，hIAPP单体和低聚物是多电荷的。MS / MS分析表明，hIAPP单体根据母体离子电荷状态采用不同的结构。断裂模式表明M ²⁺和M ³⁺和M ⁴⁺和M ⁵⁺（M =单体）的结构相似性。对二聚体的MS / MS分析表明，D ⁵⁺（D =二聚体）包含M ²⁺和M ³⁺亚基，并且肽键在单体亚基的15-37残基区域解离。