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. Author manuscript; available in PMC: 2025 Nov 1.
Published in final edited form as: Biochim Biophys Acta Gen Subj. 2024 Aug 6;1868(11):130690. doi: 10.1016/j.bbagen.2024.130690

Table 2.

Summary of FTIR data for the sample bulk solutions of SAA1–13 and its associated mutants. FTIR of the washed fibrils are also shown for samples that displayed helical bands on the FTIR spectra of their bulk solutions.

Preparation Peptide FTIR (cm−1)
amide III amide II amide I
Bulk Solution SAA1–13 1230 1527 1626, 1697
SAA1–13S5A 1230 1527 1628, 1697
SAA1–13D12N 1230 1527 1626, 1697
SAA1–13D12A 1230 1529 1626, 1697
SAA1–13E9Q 1234, 1315 1547 1626, 1656, 1680, 1699
SAA1–13E9A 1234, 1313 1545 1626, 1656, 1680, 1699
SAA1–13R1Cit 1242 1624, 1658, 1681, 1697
SAA1–13R1A 1242 1624, 1655, 1678, 1699
SAA1–13S5A (no heparin) 1230, 1315 1527, 1547 1625, 1656, 1680, 1697
Washed Fibrils SAA1–13E9Q 1527 1626, 1697
SAA1–13E9A 1527 1626, 1697
SAA1–13S5A (no heparin) 1527 1625, 1697

Samples were incubated with heparin except for the last entry.

Amide I, II, and III peaks taken as the minima of the second-derivative spectra.

§

Amyloid morphology as deduced from the TEM data.