Cosmic Peptides research library

Thymosin α1

A 28-residue N-acetylated, strongly acidic peptide originally isolated from thymus tissue.

Last reviewed · Editorial policy

A 28-residue N-acetylated, strongly acidic peptide originally isolated from thymus tissue. Every value on this page is calculated from the structure shown, by the method and constants in the sources below; measured values for a particular lot are on its certificate of analysis.

Structure

Three-letter code: Ac-Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn-OH

One-letter code: SDAAVDTSSE ITTKDLKEKK EVVEEAEN

  • 28 residues
  • N-terminus: N-acetyl
  • C-terminus: free acid

Calculated properties

Calculated from the structure
PropertyValue
Molecular formulaC129H215N33O55
CAS Registry Number62304-98-7
Average molecular weight3,108.32 g/mol
Monoisotopic mass3,106.5041 Da
Net charge at pH 7-6.0
Isoelectric point3.81
Molar absorption coefficient, 280 nmNo tryptophan, tyrosine or cystine: no absorbance at 280 nm; quantify at 205–220 nm instead.
Hydropathy (GRAVY)-1.03
Net charge across the pH range
pH 2pH 4pH 6pH 7pH 8pH 10pH 12
3.9-1.0-5.9-6.0-6.0-6.5-9.8

Composition: Glu 6, Lys 4, Ala 3, Asp 3, Ser 3, Thr 3, Val 3, Asn 1, Ile 1, Leu 1.

Expected mass spectrometry ions

The protonated ions expected in positive-mode electrospray, from the monoisotopic mass, and the common sodium and potassium adducts. MALDI spectra show mainly [M+H]+.

Expected ions (monoisotopic)
Ionm/z
[M+H]+3,107.5114
[M+2H]2+1,554.2593
[M+3H]3+1,036.5087
[M+4H]4+777.6333
[M+5H]5+622.3081
[M+Na]+3,129.4933
[M+K]+3,145.4673

Isotope pattern

Natural carbon-13, nitrogen-15, oxygen-18, sulfur-34 and deuterium spread each ion over a cluster of peaks about 1 Da apart (1/z on the m/z scale). For a molecule this size the monoisotopic peak is not the tallest: the most abundant is M+1. A spectrum read at its tallest peak, or a deconvoluted mass from it, sits about 1.00 Da above the monoisotopic mass.

050100MM+1M+2M+3M+4M+5M+6M+7
Calculated isotope pattern of the neutral molecule, from IUPAC isotopic abundances.
Isotope peaks (relative abundance, most abundant = 100)
PeakAbundanceNeutral mass[M+H]+[M+2H]2+[M+3H]3+[M+4H]4+[M+5H]5+
M (monoisotopic)64.03,106.50413,107.51141,554.25931,036.5087777.6333622.3081
M+1100.03,107.50713,108.51431,554.76081,036.8430777.8840622.5087
M+284.83,108.50983,109.51711,555.26221,037.1772778.1347622.7092
M+351.23,109.51253,110.51981,555.76351,037.5115778.3854622.9098
M+424.43,110.51523,111.52251,556.26491,037.8457778.6361623.1103
M+59.83,111.51783,112.52511,556.76621,038.1799778.8867623.3108
M+63.43,112.52043,113.52761,557.26751,038.5141779.1374623.5113
M+71.03,113.52293,114.53021,557.76871,038.8482779.3880623.7119

Fragment ions (MS/MS)

Collision-induced fragmentation breaks peptide bonds along the backbone. Fragments that keep the N-terminus are b ions; those that keep the C-terminus are y ions. Reading the ladder confirms the sequence residue by residue. Singly charged monoisotopic values, with doubly charged values beside them. The b ion containing every residue is rarely seen and the y ion containing every residue is the precursor itself, so neither is listed.

b and y ions
b#b+b2+Residuey+y2+y#
1130.049965.5286Ser——28
2245.0768123.0420Asp2,978.46881,489.738027
3316.1139158.5606Ala2,863.44191,432.224626
4387.1510194.0792Ala2,792.40481,396.706025
5486.2195243.6134Val2,721.36761,361.187524
6601.2464301.1268Asp2,622.29921,311.653323
7702.2941351.6507Thr2,507.27231,254.139822
8789.3261395.1667Ser2,406.22461,203.615921
9876.3581438.6827Ser2,319.19261,160.099920
101,005.4007503.2040Glu2,232.16051,116.583919
111,118.4848559.7460Ile2,103.11801,052.062618
121,219.5325610.2699Thr1,990.0339995.520617
131,320.5801660.7937Thr1,888.9862944.996716
141,448.6751724.8412Lys1,787.9385894.472915
151,563.7021782.3547Asp1,659.8436830.425414
161,676.7861838.8967Leu1,544.8166772.912013
171,804.8811902.9442Lys1,431.7326716.369912
181,933.9237967.4655Glu1,303.6376652.322411
192,062.01861,031.5130Lys1,174.5950587.801110
202,190.11361,095.5604Lys1,046.5000523.75379
212,319.15621,160.0817Glu918.4051459.70628
222,418.22461,209.6159Val789.3625395.18497
232,517.29301,259.1501Val690.2941345.65076
242,646.33561,323.6714Glu591.2257296.11655
252,775.37821,388.1927Glu462.1831231.59524
262,846.41531,423.7113Ala333.1405167.07393
272,975.45791,488.2326Glu262.1034131.55532
28——Asn133.060867.03401

Immonium ions (low-mass markers of the residues present): Ala 44.0495, Ser 60.0444, Val 72.0808, Thr 74.0600, Ile 86.0964, Leu 86.0964, Asn 87.0553, Asp 88.0393, Lys 101.1073, Glu 102.0550.

What to watch for analytically

Variants this sequence can give, from its chemistry. They are what an HPLC or mass spectrometry result for this peptide is read against; none is a statement about a particular lot. Where synthesis variants come from is explained in How synthetic peptides are made.

Sequence-specific variants
VariantMass changeWhy
Asparagine deamidation+0.984 DaAsparagine at position 28 can deamidate to aspartic or isoaspartic acid through a succinimide intermediate. Moisture, higher pH and warmth speed it up.
Synthesis-related variantsminus a residue (deletion)As for any synthetic peptide, deletion sequences and incompletely deprotected forms can occur.

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

See also

Cite this page

Text

Cosmic Peptides. (2026, October 25). Thymosin α1: peptide reference entry. Cosmic Peptides Research Library. Retrieved October 26, 2026, from https://cosmicpeptides.com/research/peptides/thymosin-alpha-1

BibTeX

@misc{cosmicpeptides_research_peptides_thymosin_alpha_1,
  author       = {{Cosmic Peptides}},
  title        = {Thymosin α1: peptide reference entry},
  howpublished = {Cosmic Peptides Research Library},
  year         = {2026},
  month        = oct,
  url          = {https://cosmicpeptides.com/research/peptides/thymosin-alpha-1},
  urldate      = {2026-10-26},
  note         = {Last reviewed 2026-10-25}
}

RIS

TY  - ELEC
AU  - Cosmic Peptides
TI  - Thymosin α1: peptide reference entry
T2  - Cosmic Peptides Research Library
PB  - Cosmic Peptides
PY  - 2026
DA  - 2026/10/25
UR  - https://cosmicpeptides.com/research/peptides/thymosin-alpha-1
Y2  - 2026/10/26
LA  - en
ER  - 

Cite the date the page was last reviewed, October 25, 2026, as its version. Reference managers such as Zotero can save this page directly.

Changes to this page

  1. Updated Peptide mass match, isotope patterns and fragment ions

    Check the masses from a spectrum or a certificate against a sequence; every reference entry and calculation now shows its isotope pattern and its b- and y-ion ladder.

  2. Published Peptide reference: 24 entries and a property table

    Identity, calculated properties, expected mass spectrometry ions and analytical notes for 24 research peptides, all calculated from the structure, with the full table as CSV and JSON.

Changes of substance are listed here; wording changes are not. Every correction is also on the corrections log.

For in vitro laboratory research only. Not for human or veterinary use. This library describes chemistry, analytical methods and published laboratory research; it gives no guidance on use in people or animals.