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. 2020 May 27;25(11):2498. doi: 10.3390/molecules25112498

Table 2.

IR marker bands of abnormal protein aggregation.

Marker Band of the Aggregation [cm−1] Assignment Peptide Reference
amide I (1700-1600 cm−1)
1695-1685/1633-1623 antiparallel β-sheet amyloid β1-42 oligomers [40,41]
amyloid β1-40 [42,43,44]
α-synuclein [28,47,48]
PrP82–146 [51]
1693-1685/1623–1613 antiparallel β-sheet amyloid β11-28 fragment and its mutants in 21-23 position [31]
1692/1620 antiparallel β-sheet HET218–289 [55]
1691/1630 antiparallel β-sheet Aβ 42CC oligomers/protofibrils [32]
1688/1620 antiparallel β-sheet human lysozyme, oligomers [29]
1686/1616 antiparallel β-sheet transthyretin (TTR) soluble aggregates [52]
1686/1614 antiparallel β-sheet hen egg white lysozyme (HEWL) [56]
1684/1616 β2-microglobulin (short curved structures) [54]
1684/1612 antiparallel β-sheet SH3 domain, amorphous aggregates, non-fibrilar [57]
1683/1612 ↑→ antiparallel β-sheet insulin oligomer [39]
1678-1670 β-turns amyloid β11-28 fragment and its mutants in 21-23 position [31]
1670 β-turns amyloid β1-42 oligomers and fibrils [40]
α-synuclein [28]
1669 β-turns HET218–289 [55]
1667-1661 310-helix E22K and A21G mutants of Aβ(11-28) fragment [31]
1664 β-turns SH3 fibrils/pepsin digested [57]
1660-1650 random coil and/or
helical structures
amyloid β1-42 oligomers and fibrils [40]
α-synuclein [28]
1659-1652 α-helix amyloid β11-28 fragment and its mutants in 21-23 position [31]
1658 Turns human lysozyme monomers, oligomers, fibrils [29]
1655 random coil HET218–289 [55]
1649 unstructured SH3 amorphous aggregates [57]
1648-1639 random coil amyloid β11-28 fragment and its mutants in 21-23 position [31]
1648 random coil PrP82–146 [51]
1644-1641 disordered/loops human lysozyme oligomers, fibrils [29]
1641 disordered structures SH3 fibrils/pepsin digested [57]
1635-1624 β-sheet amyloid β11-28 fragment and its mutants in 21-23 position [31]
1633 parallel β-sheet Sup35 crystals, prion-like [58]
1630 parallel β-sheets HET218–289 [55]
1630-1623 parallel β-sheet amyloid β1-42 fibrils [40,41]
amyloid β1-40 [42,43,44]
1630-1614 parallel β-sheet human lysozyme fibrils [29]
1628 parallel β-sheet α-synuclein fibrils [28]
1626 ↑ parallel β-sheet PrP82–146 fibrils [51]
1626 ↑→ parallel β-sheet insulin fibrils [39]
1625 parallel β-sheet transthyretin (TTR) fibrils [52]
1620-1618 β2-microglobulin, fibrils [54]
1620-1600 β-sheets hen egg white lysozyme (HEWL) [56]
1618 ← parallel β-sheet SH3 fibrils/pepsin digested [57]

↑ increase in intensity, ← shift towards higher wavenumbers after aggregation, → shift towards lower wavenumbers after aggregation.