Amyloid-β (1–42) and Amyloid-β (1–40) compared

Amyloid-β (1–40) is the first 40 residues of amyloid-β (1–42). The two residues it lacks, Ile41 and Ala42, are hydrophobic, and they make Aβ(1–42) far more prone to aggregate.

Sequences side by side

Amyloid-β (1–40) is a continuous stretch of Amyloid-β (1–42): 40 residues in common, aligned below by Amyloid-β (1–42)'s numbering. In each column the upper residue is Amyloid-β (1–42)'s and the lower is Amyloid-β (1–40)'s. Positions outside the shorter sequence are dimmed.

Both have the same termini: free amine and free acid.

Calculated properties

Calculated from each structure

Property	Amyloid-β (1–42)	Amyloid-β (1–40)	Difference (Amyloid-β (1–40) − Amyloid-β (1–42))
Residues	42	40	−2
Molecular formula	C203H311N55O60S	C194H295N53O58S
Monoisotopic mass (Da)	4,511.2696	4,327.1484	−184.1212
Average mass (g/mol)	4,514.11	4,329.87	−184.24
Net charge at pH 7	-2.3	-2.3	0.0
Isoelectric point	5.43	5.43	0.00
Hydropathy (GRAVY)	0.20	0.06	−0.15
ε280 (M−1 cm−1)	1,490	1,490

Telling them apart by mass spectrometry

The monoisotopic masses differ by 184.1212 Da, which any routine mass spectrometer resolves.

Expected protonated ions (monoisotopic m/z)

Ion	Amyloid-β (1–42)	Amyloid-β (1–40)
[M+H]+	4,512.2769	4,328.1557
[M+2H]2+	2,256.6421	2,164.5815
[M+3H]3+	1,504.7638	1,443.3901
[M+4H]4+	1,128.8247	1,082.7944

Telling them apart by HPLC

Amyloid-β (1–42) is the more hydrophobic by the Kyte–Doolittle average (a difference of 0.15), so in reversed-phase HPLC it would usually be expected to elute later. Retention depends on the whole molecule and on the method, so the order is confirmed by running both, or by mass spectrometry of each peak.

Analytical variants each can form

The sequence-specific variants from each entry. A variant only one of them can form is a quick way to tell which is which, and a reminder of what to look for in each.

Sequence-specific variants

Variant	Mass change	Amyloid-β (1–42)	Amyloid-β (1–40)
Methionine oxidation	+15.995 Da per oxidized residue	Yes	Yes
Asparagine deamidation	+0.984 Da	Yes	Yes
Glutamine deamidation	+0.984 Da	Yes	Yes

Full details, with isotope patterns and fragment ions, are on each entry: Amyloid-β (1–42) and Amyloid-β (1–40). Both are compared with the rest of their family on the family page.

Sources & Further Reading

1. Prohaska T, Irrgeher J, Benefield J, Böhlke JK, Chesson LA, Coplen TB, et al. Standard atomic weights of the elements 2021 (IUPAC Technical Report). Pure and Applied Chemistry 2022;94(5):573–600. doi:10.1515/pac-2019-0603
2. Wang M, Huang WJ, Kondev FG, Audi G, Naimi S. The AME 2020 atomic mass evaluation (II). Tables, graphs and references. Chinese Physics C 2021;45(3):030003. doi:10.1088/1674-1137/abddaf
3. Rice P, Longden I, Bleasby A. EMBOSS: the European Molecular Biology Open Software Suite. Trends in Genetics 2000;16(6):276–277. doi:10.1016/S0168-9525(00)02024-2
4. Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Science 1995;4(11):2411–2423. doi:10.1002/pro.5560041120
5. Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology 1982;157(1):105–132. doi:10.1016/0022-2836(82)90515-0
6. Meija J, Coplen TB, Berglund M, Brand WA, De Bièvre P, Gröning M, et al. Isotopic compositions of the elements 2013 (IUPAC Technical Report). Pure and Applied Chemistry 2016;88(3):293–306. doi:10.1515/pac-2015-0503
7. Roepstorff P, Fohlman J. Letter to the editors: proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomedical Mass Spectrometry 1984;11(11):601. doi:10.1002/bms.1200111109
8. Biemann K. Contributions of mass spectrometry to peptide and protein structure. Biomedical and Environmental Mass Spectrometry 1988;16(1–12):99–111. doi:10.1002/bms.1200160119
9. Geiger T, Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. Journal of Biological Chemistry 1987;262(2):785–794. doi:10.1016/S0021-9258(19)75855-4
10. Manning MC, Chou DK, Murphy BM, Payne RW, Katayama DS. Stability of protein pharmaceuticals: an update. Pharmaceutical Research 2010;27(4):544–575. doi:10.1007/s11095-009-0045-6
11. D'Hondt M, Bracke N, Taevernier L, Gevaert B, Verbeke F, Wynendaele E, et al. Related impurities in peptide medicines. Journal of Pharmaceutical and Biomedical Analysis 2014;101:2–30. doi:10.1016/j.jpba.2014.06.012

Cosmic Peptides. (2026, October 25). Amyloid-β (1–42) and Amyloid-β (1–40) compared. Cosmic Peptides Research Library. Retrieved October 26, 2026, from https://cosmicpeptides.com/research/peptides/compare/amyloid-beta-1-42-vs-amyloid-beta-1-40

@misc{cosmicpeptides_research_peptides_compare_amyloid_beta_1_42_vs_amyloid_beta_1_40,
  author       = {{Cosmic Peptides}},
  title        = {Amyloid-β (1–42) and Amyloid-β (1–40) compared},
  howpublished = {Cosmic Peptides Research Library},
  year         = {2026},
  month        = oct,
  url          = {https://cosmicpeptides.com/research/peptides/compare/amyloid-beta-1-42-vs-amyloid-beta-1-40},
  urldate      = {2026-10-26},
  note         = {Last reviewed 2026-10-25}
}

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