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자료유형
학술저널
저자정보
Seo Yeon Kim (Kumoh National Institute of Technology) Ho-Tae Kim (Kumoh National Institute of Technology)
저널정보
한국질량분석학회 Mass Spectrometry Letters Mass Spectrometry Letters Vol.15 No.4
발행연도
2024.12
수록면
195 - 201 (7page)

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The monomer and oligomer peptide complexes of the amyloidogenic human islet amyloid polypeptide 1-19 (hIAPP19) and non-amyloidogenic rat islet amyloid polypeptide 1-19 (rIAPP19) were investigated using electrospray ionization (ESI)-mass spectrometry (MS). The dissociation of monomers and oligomers was investigated by tandem mass spectrometry (MS/MS) using collision-induced dissociation (CID). Peptide bond dissociation in the Arg8–Ser19 region of hIAPP19 was mainly observed in the tandem mass spectra of the monomers and oligomers. The fragmentat ion pattern of the hIAPP19 D<sup>3+</sup>(= [dimer+3H]<sup>3+</sup>) complex was similar to that of the M<sup>2+</sup> (= [monomer+2H]<sup>2+</sup>) tandem mass spectrum in the form of {M + (fragmention of M<sup>2+</sup>)}. In the case of the hIAPP T<sup>4+</sup> (= [trimer+4H]<sup>4+</sup>) complex, the (monomer–D<sup>3+</sup>)<sup>4+</sup> complex geometry was assumed to be stable based on the presence of {M + (fragment ion of D<sup>3+</sup>)} ions in the tandem mass spectrum of the T<sup>4+</sup> complex. The interaction geometry of [(disulfide bond (S-S) in Cys2 - Cys7 region)–((S-S) in Cys2 - Cys7 region)] was proposed for the dimer and trimer complexes of hIAPP19 based on the observation of three characteristic fragment ions: (i) [MS]<sup>2+</sup>, [M+S]<sup>2+</sup>, [D-S]<sup>3+</sup>, and [D+S]<sup>3+</sup>, (ii) y18, and (iii) bu (u = 8–18) fragment ion series in the Arg8 - Ser19 region. The tandem mass spectrum of rIAPP19 differed from that of hIAPP19. Fragment ions originating from the Cys2–Cys7 region were observed in the M<sup>2+</sup> tandem mass spectrum of rIAPP19 as [yn+S]<sup>2+</sup> (n = 13 – 17) and [zn+S]<sup>2+</sup> (n = 13 – 15).

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Abstract
Introduction
Experimental
Results and Discussion
Conclusion
References

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