Organizing co mmittee

 
References
: 
1. Bartholomew J.W. Variables influencing results, and the precise definition of steps 
in gram staining as a means of standardizing the results obtained. Stain Technol. 1962; 
37:139-155. doi:10.3109/10520296209117723 
2. Reddy B.L, Saier M.H. Topological and Phylogenetic Analyses of Bacterial Holin 
Families and Superfamilies. Biochim Biophys Acta. 2013; 1828 (11): 2654-2671. 
doi:10.1016/j.bbamem.2013.07.004 
 
 

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Poster presentation 
192 
PEPTIDES OF THE THYMOPTIN 
 
U.J. Ishimov
1,2
, Sh.S. Olimjonov
1
, A.M. Ne’matova
2
, J.F. Ziyavitdinov
1
 
1) Institute of Bioorganic Chemistry, Academy of Sciences Republic of Uzbekistan, 
Tashkent 
2) Tashkent chemical technological institute Republic of Uzbekistan, Tashkent. 
e-mail: [e-mail] 
 
Currently, one of the priority areas in the development of effective drugs is the 
search and isolation of biologically active substances, in particular, of a protein-peptide 
nature, acting in extremely low concentrations. 
Thymoptin, widely used to correct human immunity, consists of a mixture of acidic 
peptides isolated from the thymus of lambs or calves. The main thymoptin peptide, α1-
thymosin, consists of 28 amino acid residues and has an MM of 3065 Da. Another high-
abundant, β4 - thymosin, consists of 43 amino acid residues has an MM of 4982 Da. 
Thymopoetin consisting of 49 amino acid residues has an MM of 5561 Da. 
To carry out thymoptin peptide mapping, the substance was fractionated by RP-
HPLC on an Agilent Technologies 1200 instrument (USA) using a Nucleosil 5 C
18
column (4.6 mm x 250 mm) in the isocratic mode of 97% acetonitrile in water. As a 
result, 6 individual peptides were obtained, which were eluted from the column in the 
time interval of 2-6 min.
The molecular weight of major peptides with retention times in the column of 2.54 
(I), 2.71 (II), and 5.75 (III) min was determined on an Agilent Technologies 6530B 
Chip-HPLC-Q-TOF mass spectrometer. The molecular ion of the peptide - I was found 
at m/z 3065.5008, the peptide - II m/z 4919.4830, and the peptide - III m/z 5561.956. 
After trypsinolysis, MS/MS analyzes were performed and the exact molecular masses of 
fragment and daughter ions were determined. The obtained mass spectra were 
interpreted using the Mass COT and Spectrum Mill programs. As a result of the 
chromato-mass-spectrometric studies, the following fragmentary peptides were 
established: for peptide I with m/z: EVVEEAEN – 917.3978, SDAAVDTSSEITTK – 
1406.6645, EKK – 385.2325, DLK– 356.206; 
For peptide II with m/z: PDMAEIEK -913.4215, FDKSK- 605.3173, SDK - 
331.1612, ETIEQEK– 857.4131, LKK – 369.274, NPLPSK – 636.3595, TETQEK –
716.3341, QAGES–490, 2023;
For 
peptide 
III 
with 
m/z: 
SQLVANNVTLPAGEQRK–1824.9926, 
SQFLEDPSVLTK–1363.7104, 
DVYVQLYLGTLTAVKR–1839.0375, 
GKLK– 
445.3133. 
Using the Blast database, the complete primary structure and the name of the isolated 
major peptides of the Timoptin substance were established: 
Peptide I – SDAAVDTSSEITTKDLKEKKEVVEEAEN – α1 - thymosin. 
Peptide II – SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES – 
β4 - thymosin. 
Peptide III -
SQFLEDPSVLTKGKLKSQLVANNVTLPAGEQRKDVYVQLYLGTLT-
AVKRThymopoietin. 

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Poster presentation 
193