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.