from 01.01.2024 until now Stavropol, Stavropol, Russian Federation
from 01.01.2000 until now Azur, Israel
VAC 3.3 Медико-биологические науки
VAC 3.4 Фармацевтические науки
UDK 612.4.05 Физика и химия секреции
UDK 612.49 Прочие секреторные процессы
GRNTI 76.00 МЕДИЦИНА И ЗДРАВООХРАНЕНИЕ
GRNTI 34.00 БИОЛОГИЯ
OKSO 31.00.00 Клиническая медицина
OKSO 06.00.00 Биологические науки
BBK 53 Клиническая медицина в целом
TBK 571 Медикобиологические дисциплины
BISAC MED MEDICAL
The book is devoted to both history and modern theory and practice of medical and veterinary use of peptides, their isolation in pure form, their laboratory chemical synthesis, as well as history of the study of the properties of various peptide substances. First it were extracts or hydrolysates from animal tissues and organs. Later it were pure peptide hormones and mediators, cytokines, antibiotics, etc. The book is intended primarily for students who are in the process of getting higher medical education in the disciplines “General Medicine”, “Pediatrics”, “Pharmacy”, “Medical Biochemistry”, “Veterinary Medicine”. It will also be useful to undergraduate, graduate and postgraduate students of higher educational institutions who are studying disciplines such as “Biology”, “Biotechnology”, “Fundamental and Applied Biology”.
peptidology, peptidomics, peptide medicine, neuropeptides, peptide hormones, cytokines, peptide antibiotics, peptide synthesis
1. Andryukov B.G., Besednova N.N., Zaporozhec T.S. K 80-letiyu sozdaniya gramicidina S: ot izucheniya asimmetrii bakterial'nyh molekul k otkrytiyu antimikrobnyh peptidov //Antibiotiki i himioter. 2022. T. 67. S. 3–4, 85–92. DOI:https://doi.org/10.37489/02352990202267348592.
2. Anohin P.K. Ocherki po fiziologii funkcional'nyh sistem. M.: Medicina, 1975. 448 s.
3. Ashmarin I.P., Kulashev A.P., Chepurnov S.A. Kaskadnye odnonapravlennye regulyatornye processy, osuschestvlyaemye korotkozhivuschimi peptidami (tiroliberin) //Fiziologicheskiy zhurnal SSSR im. I.M. Sechenova. 1989. T. 75. № 5. S. 627–632.
4. Ashmarin I.P., Obuhova M.F. Regulyatornye peptidy, funkcional'no nepreryvnaya sovokupnost' //Biohimiya. 1985. T. 51. № 4. S. 531–545.
5. Ashmarin, I.P., Obuhova M.F. Sovremennoe sostoyanie gipotezy o funkcional'nom kontinuume regulyatornyh peptidov //Vestnik Rossiyskoy akademii medicinskih nauk. M.: Medicina, 1994. № 10. S. 28–33.
6. Bekker R.A., Bykov Yu.V. Yulius Vagner-Yauregg: dve storony nobelevskoy nagrady //Dnevnik psihiatra. 2016. № 4. S. 22–24.
7. Bekker R.A., Bykov Yu.V., Morozov P.V. Vydayuschiesya psihiatry XX veka. M.: Gorodec, 2019. 256 S.
8. Bershteyn L.M. Vladimir Mihaylovich Dil'man — teoretik i praktik mediciny (k 90letiyu so dnya rozhdeniya) //Saharnyy diabet. 2015. T. 18. C. 96–98.
9. Volkov V.A., Vonskiy E.V., Kuznecova G.I. Vydayuschiesya himiki mira. M.: VSh, 1991. 656 s.
10. Dedov I.I., Shestakova M.V. K stoletiyu otkrytiya insulina //Saharnyy diabet. 2021. T. 24(1). C. 11–16.
11. Dil'man V.M. Chetyre modeli mediciny. L.: Medicina, 1987.
12. Klinicheskaya farmakologiya timogena / Red. V.S. Smirnov. SPb., 2003. 106 s.
13. Koroleva S.V., Ashmarin I.P. Put' funkcional'noy klassifikacii regulyatornyh peptidov. Priznaki divergentnoy i konvergentnoy evolyucii regulyatornyh peptidov //Zhurnal evolyucionnoy biohimii i fiziologii, 2000. SPb.: Nauka. T. 36. № 2. S. 154–159.
14. Morozov V.G., Havinson V.H. Vydelenie iz kostnogo mozga, limfocitov i timusa polipeptidov, reguliruyuschih processy mezhkletochnoy kooperacii v sisteme immuniteta //Dokl. AN SSSR. 1981a. T. 261. № 1. S. 235–239.
15. Morozov V.G., Havinson V.H. Molekulyarnye mehanizmy bioregulyacii geneticheskoy aktivnosti i kletochnogo metabolizma //Tez. dokl. XVIII Vsesoyuzn. s'ezda terapevtov. M.: Medicina, 1981b. T. 1. S. 78–80.
16. Morozov V.G., Havinson V.H. Novyy klass biologicheskih regulyatorov mnogokletochnyh sistem — citomediny //Uspehi sovrem. biologii. 1983. T. 96. № 3. S. 339–346.
17. Morozov V.G., Havinson V.H. Peptidnye bioregulyatory (25-letniy opyt eksperimental'nogo i klinicheskogo izucheniya). SPb.: Nauka, 1996. 74 s.
18. Morozov V.G., Havinson V.H. Timalin i ego immunobiologicheskaya aktivnost' / Pod red. Yu.A. Grinevicha i V.F. Chebotareva //Immunobiologiya gormonov timusa. Kiev: Zdorov'ya, 1989. S. 125–143.
19. Morozov V.G., Havinson V.H., Malinin V.V. Peptidnye timomimetiki. SPb: Nauka, 2000. 158 s.
20. Mohort T.V. Preparaty insulina — 100 let otkrytiy i uspeha //Medicinskie novosti. 2021. № 6(321). S. 5–12.
21. Okovityy S.V., Prihod'ko V.A. Topicheskie lekarstvennye preparaty dlya lecheniya infekcionno-vospalitel'nyh zabolevaniy uha i glaz. Effektivnaya farmakoterapiya. 2023. T. 19(49). S. 36–48. DOIhttps://doi.org/10.33978/23073586202319493648.
22. Sudakov K.V. Teoreticheskaya fiziologiya: razvitie v nauchnoy shkole P.K. Anohina //Vestnik Rossiyskoy akademii medicinskih nauk. M.: Medicina, 1994. № 10. S. 3–11.
23. Fiziologiya. Osnovy i funkcional'nye sistemy: kurs lekciy. Pod red. K.V.Sudakova. M.: Medicina, 2000. 784 s.
24. Havinson V.H., Seryy S.V., Malinin V.V. Sredstvo, obladayuschee immunomoduliruyuschey aktivnost'yu: Patent RF № 2080120. 1997.
25. Shabanov P.D., Lebedev A.A., Bychkov E.R. i dr. Neyrohimicheskie mehanizmy i farmakologiya grelinov //Obzory po klinicheskoy farmakologii i lekarstvennoy terapii. 2020. T. 18. № 1. S. 5–22. DOI:https://doi.org/10.7816/RCF181522
26. Yakubke H.D., Eshkayt H. Aminokisloty, peptidy, belki. 1985. 457 s.
27. Abdalla M.A., McGaw L.J. Natural Cyclic Peptides as an Attractive Modality for Therapeutics: A Mini Review //Molecules. 2018 Aug 20. Vol. 23(8). P. 2080. DOI:https://doi.org/10.3390/molecules23082080.
28. Abderhalden A., Fodor A. Synthese von hochmolecularen Polypeptiden aus Glykocoll und LLeucin. Ber., 1916. Vol. 49. Pp. 561–578.
29. Acher R., Chauvet J. Structure of vasopressin //Biochem. Biophys. Acta. 1953.Vol. 12. Pp. 487–488.
30. Akabori S., Ikenaka T., Matsumoto K. Asymmetric synthesis of amino acids //Proc. Jap. Acad. 1951. Vol. 27. Pp. 7–9.
31. Akabori S., Ohno K., Narita K. Hydrazinolysis of proteins and peptides: method for the characterization of carboxyl terminal amino acids in proteins. Bull. Chem. Soc. Japan 1952. Vol. 25. Pp. 214–218.
32. Anderson G.W., McGregor A.C. Tbutyloxycarbonylamino acids and their use in peptide synthesis //J. Am. Chem. Soc. 1957. Vol. 79. Pp. 6180–6183. DOI:https://doi.org/10.1021/ja01580a020.
33. Arnon S.S., Schechter R., Inglesby T.V. et al. Botulinum toxin as a biological weapon: medical and public health management //Jama. Vol. 285(8). 2001. Pp. 1059–1070.
34. Babu V.S. One hundred years of peptide chemistry //Resonance. 2001. Vol. 10(6). Pp. 68–75.
35. Baggerman G., Verleyen P., Clynen E. et al. Peptidomics //Journal of Chromatography B. 20014. Vol. 803(1). Pp. 3–16.
36. Baig M.H., Ahmad K., Saeed M. et al. Peptide based therapeutics and their use for the treatment of neurodegenerative and other diseases //Biomed Pharmacother. 2018. Vol. 103. Pp. 574–581. DOI:https://doi.org/10.1016/j.biopha.2018.04.025.
37. Barany G., Merrifield R. A new amino protecting group removable by reduction.Chemistry of the dithiasuccinoyl (dts) function //J. Am. Chem. Soc. 1977. Vol. 99. Pp. 7363–7365. DOI:https://doi.org/10.1021/ja00464a050.
38. Bartlett M.F., Roeske R., Stedman R.J. et al. Studies on the synthesis of lysine vasopressin //J. Am. Chem. Soc. 1956. Vol. 78. Pp. 2905–2906.
39. Battersby A.R, Craig L.C. The molecular weight determination of polypeptides //J. Am. Chem. Soc. 1951. Vol. 73. Pp. 1887–1888.
40. Bergmann M., Zervas L. A general process for the synthesis of peptides //Ber. Dtsch. Chem. Ges. 1932. Vol. 65B. Pp. 1192–1201.
41. Bergmann M., Zervas L. Über ein allgemeines Verfahren der PeptidSynthese //Ber Deutsch Chem Ges. 1932. Vol. 65. Pp. 1192–201.
42. Berman A.L., Kolker E., Trifonov E.N. Underlying order in protein sequence organization //P. Natl. A. Sci. USA. 1994. Vol. 91. Pp. 4044–4047. DOI:https://doi.org/10.1073/pnas.91.9.4044.
43. Carpino L.A. Oxidative reactions of hydrazines. Iv. Elimination of nitrogen from 1, 1-disubstituted 2-arenesulfonhydrazides //J. Am. Chem. Soc. 1957. Vol. 79. Pp. 4427–4431. DOI:https://doi.org/10.1021/ja01573a050.
44. Carpino L.A., Han G.Y. 9Fluorenylmethoxycarbonyl function, a new base-sensitive amino-protecting group //J. Am. Chem. Soc. 1970. Vol. 92. Pp. 5748–5749. DOI:https://doi.org/10.1021/ja00722a043.
45. Chandrudu S., Simerska P., Toth I. Chemical methods for peptide and protein production. Molecules. 2013. Vol. 18(4). Pp. 4373–88. DOI:https://doi.org/10.3390/molecules18044373.
46. Coin I., Dölling R., Krause E. et al. Depsipeptide methodology for solid phase peptide synthesis: circumventing side reactions and development of an automated technique via depsidipeptide units //J. Org Chem. 2006. Vol. 71(16). Pp. 6171–7.
47. Conibear A.C., Watson E.E., Payne R.J. et al. Native chemical ligation in protein synthesis and semisynthesis //Chem Soc Rev. 2018. Vol. 47(24). Pp. 9046–9068. DOI:https://doi.org/10.1039/c8cs00573g.
48. Consden R., Gordon A.H., Martin A.J.P. et al. Gramicidin S: the sequence of the amino acid residues //Biochem. J. 1947. Vol. 41. Pp. 596–602.
49. Curtius T. Synthetische Versuche mit Hippurazid //Ber. Dtsch. Chem. Ges. 1902. Vol. 35. Pp. 3226–3228.
50. Curtius T. Uber die Einwirkkung von Chlorbenzoyl auf Glycocollsilber (vorlaufige Mitt.) //J. Prakt. Chemie. 1881. Vol. 2. Pp. 239–240.
51. Curtius T. Ueber einige neue der Hippursäure analog constituirte, synthetisch dargestellte Amidosäuren //J. Prakt Chemie. 1882. Vol. 26. Pp. 145–208.
52. Curtius T. Verkettung von Amidosäuren. I. Abhandlung //J Prakt Chemie. 1904. Vol. 70(1). Pp. 57–72.
53. Curtius T., Gumlich O. Verkettung von Amidosäuren; VII. Abhandlung. Kettenbildung zwischen Hippurazid und βAminoαoxypropionsäure und βAminobuttersäure //J Prakt Chemie. 1904. Vol. 70(1). Pp. 195–223.
54. Curtius T., Müller E. Verkettung von Amidosäuren; VIII. Abhandlung. Über Hippurylγaminobuttersäure und Hippurylβphenylαalanin //J. Prakt Chemie. 1904. Vol. 70(1). Pp. 223–229.
55. Da’san M.J. Thirteen decades of peptide synthesis: key developments in solid phase peptide synthesis and amide bond formation utilized in peptide ligation //Amino acids. 2018. Vol. 50(1). Pp. 39–68.
56. Dawson P.E., Muir T.W., ClarkLewis I. et al. Synthesis of proteins by native chemical ligation //Science. 1994. Vol. 266. Pp. 776–778.
57. Deamer D. First life: Discovering the connections between stars, cells, and how life began. Univ of California Press, 2012.
58. Du Vigneaud V., Miller G.L. A synthesis of glutathione //J. Biol. Chem. 1936. Vol. 116. Pp. 469–476.
59. Du Vigneaud V., Ressler C., Swan J.M. et al. The synthesis of an octapeptide amide with the hormonal activity of oxytocin //J. Am Chem Soc. 1953. Vol. 75. Pp. 4879–80.
60. Du Vigneaud V., Ressler C., Swan J.M. et al. The synthesis of oxytocin //J. Am. Chem. Soc. 1954. Vol. 76. Pp. 3115–3121.
61. Du Vigneaud V., Ressler C., Trippet S. The sequence of amino acids in oxytocin with a proposal for the structure of oxytocin //J. Biol. Chem. 1953. Vol. 205. Pp. 949–957.
62. DuarteMata D.I., SalinasCarmona M.C. Antimicrobial peptides´ immune modulation role in intracellular bacterial infection //Front Immunol. 2023 Mar 28. Vol. 14. P. 1119574. DOI:https://doi.org/10.3389/fimmu.2023.1119574.
63. Fischer E. Synthese von Polypeptiden, IX. Chloride der Aminosa¨uren und ihrer Acylderivate //Ber. Dtsch. Chem. Ges. 1905. Vol. 38. Pp. 605–620.
64. Fischer E. Synthetical chemistry in its relation to biology (Faraday Lecture) //J. Chem Soc Chem Commun. 1907. Vol. 91. Pp. 1749–65.
65. Fischer E. Untersuchungen uber Aminos auren, Polypeptide and Proteine (1899–1906) //J. Springer: Berlin, 1906. Pp. 1–83.
66. Fischer E. Untersuchungen uber Aminos auren, Polypeptide and Proteine (1907–1909) //J. Springer: Berlin, 1923. Pp. 1–21.
67. Fischer E., Fourneau E. Ueber einige Derivate des Glykocolls //Ber Deutsch Chem Ges. 1901. Vol. 34. Pp. 2868–77.
68. Galdiero S., Gomes P.A.C. PeptideBased Drugs and Drug Delivery //Systems. Molecules. 2017. Vol. 22(12). DOI:https://doi.org/10.3390/molecules22122185.
69. Gallardo Becerra L., Cervantes Echeverría M., Cornejo Granados F. et al. Perspectives in Searching Antimicrobial Peptides (AMPs) Produced by the Microbiota //Microb Ecol. 2023 Dec 1. Vol. 87(1). P. 8. DOI:https://doi.org/10.1007/s00248023023138.
70. Gan B.H., Gaynord J., Rowe S.M. et al. The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions //Chem Soc Rev. 2021 Jul 5. Vol. 50(13). Pp. 7820–7880. DOI:https://doi.org/10.1039/d0cs00729c.
71. Goodman M., Cai W., Smith N. The bold legacy of Emil Fischer //J. Pept Sci 9. 2003. Pp. 594–603.
72. Grapsas I., Cho Y.J., Mobashery S. N(tertbutoxycarbonyloxy)-5-norbornene endo(2, 3)-dicarboximide, a reagent for the regioselective introduction of the tert-butoxycarbonyl (boc) protective group at unhindered amines: Application to amino glycoside chemistry //J. Org. Chem. 1994. Vol. 59. Pp. 1918–1922. DOI:https://doi.org/10.1021/jo00086a055.
73. Gutte B., Merrifield R.B. The total synthesis of an enzyme with ribonuclease A activity //J. Am Chem. Soc. 1969. Vol. 91. Pp. 501–2.
74. Harington C.R., Mead T.H. Synthesis of glutathione. Biochem //J. 1935. Vol. 29. Pp. 1602–1611.
75. Hirschmann R., Nutt R.F., Veber D.F. et al. Studies on the total synthesis of an enzyme. V. The preparation of enzymatically active material //J. Am Chem Soc. 1969. Vol. 91. Pp. 507–8.
76. Hopkins F.G. Glutathione: a reinvestigation //J. Biol. Chem. 1929. Vol. 84. Pp. 269–320.
77. Ivanov V.T., Blishchenko E.Y., Sazonova O.V. et al. What to synthesize? From Emil Fischer to peptidomics //J. Pept Sci. 2003. Vol. 9(9). Pp. 553–62.
78. Izumi Y., Tasumi S., Imaida M. et al. The preparation of optically active alphaCsubstituted glutamic acid //Bull. Chem. Jap. 1965. Vol. 38. Pp. 1338–1340.
79. Jiao Z.T., Luo Q. Molecular Mechanisms and Health Benefits of Ghrelin: A Narrative Review. Nutrients. 2022 Oct 8. Vol. 14(19). P. 4191. DOI:https://doi.org/10.3390/nu14194191.
80. Kemp D., Leung S.L., Kerkman D.J. Models that demonstrate peptide bond formation by prior thiol capture i. Capture by disulfide formation //Tetrahedron Lett. 1981. Vol. 22. Pp. 181–184. DOI:https://doi.org/10.1016/00404039(81)800494.
81. Kendall E.C., Mason H.L., McKenzie B.F. A study of glutathione. III. The structure of glutathione //J. Biol. Chem. 1930. Vol. 87. Pp. 55–79.
82. Khorana H.G. The use of dicyclohexylcarbodiimide in the synthesis of peptides //Chem. Ind. London. 1955. Vol. 33. Pp. 1087–1088.
83. Kimmerlin T., Seebach D. ‘100 years of peptide synthesis’: ligation methods for peptide and protein synthesis with applications to βpeptide assemblies. //The Journal of peptide research. 2005. Vol. 65(2). Pp. 229–260.
84. King D.S., Fields C.G., Fields G.B. A cleavage method which minimizes side reactions following fmoc solid phase peptide synthesis //Int. J. Pept. Prot. Res. 2009. Vol. 36. Pp. 255–266. DOI:https://doi.org/10.1111/j.13993011.1990.tb00976.x.
85. Kojima M. et al. Ghrelin is a growth hormone releasing acylated peptide from stomach //Nature. 1999. Vol. 402. Pp. 656–660.
86. Lau J.L., Dunn M.K. Therapeutic peptides: Historical perspectives, current development trends, and future directions //Bioorg Med Chem. 2018. Vol. 26(10). Pp. 2700–2707. DOI:https://doi.org/10.1016/j.bmc.2017.06.052.
87. LauxBiehlmann A., Mouheiche J., Vèrièpe J. et al. Endogenous morphine and its metabolites in mammals: history, synthesis, localization and perspectives //Neuroscience. 2013. Vol. 233. Pp. 95–117.
88. Lee S.H., Yoon K.H. A Century of Progress in Diabetes Care with Insulin: A History of Innovations and Foundation for the Future //Diabetes Metab J. 2021 Sep. Vol. 45(5). Pp. 629–640. DOI:https://doi.org/10.4093/dmj.2021.0163.
89. Lewis G.F., Brubaker P.L. The discovery of insulin revisited: lessons for the modern era //J. Clin Invest. 2021 Jan 4. Vol. 131(1). P. e142239. DOI:https://doi.org/10.1172/JCI142239.
90. Lichtenthaler F.W. Emil Fischer, his personality, his achievements, and his scientific progeny //Eur. J. Org. Chem. 2002. Vol. 24. Pp. 4095–4122. DOI:https://doi.org/10.1002/10990690(200212)2002:24<4095::AIDEJOC4095>3.0.CO;22.
91. Liu C.F., Rao C., Tam J.P. Orthogonal ligation of unprotected peptide segments through pseudoproline formation for the synthesis of hiv1 protease analogs //J. Am. Chem. Soc. 1996. Vol. 118. Pp. 307–312. DOI:https://doi.org/10.1021/ja952790w.
92. Liu C.F., Tam J.P. Peptide segment ligation strategy without use of protecting groups //Proc. Natl. Acad. Sci. USA. 1994. Vol. 91(14). Pp. 6584–8.
93. LópezOtín C., Matrisian L.M. Emerging roles of proteases in tumour suppression //Nature reviews cancer. 2007. Vol. 7(10). P. 800.
94. Magner L.N., Kim O.J. A history of medicine. CRC Press. 2017.
95. Mazurkiewicz-Pisarek A., Baran J., Ciach T. Antimicrobial Peptides: Challenging Journey to the Pharmaceutical, Biomedical, and Cosmeceutical Use //Int. J. Mol. Sci. 2023 May 20. Vol. 24(10). P. 9031. DOI:https://doi.org/10.3390/ijms24109031.
96. McKay F.C., Albertson N.F. New aminemasking groups for peptide synthesis //J. Am Chem Soc. 1967. Vol. 79. Pp. 4686–4690.
97. Merrifield B. Solid phase synthesis //Science. 1986. Vol. 232. Pp. 341–47.
98. Merrifield B. The chemical synthesis of proteins //Protein Sci. 1996. Vol. 5. Pp. 1947–51.
99. Merrifield R.B. Solid phase peptide synthesis. I. The synthesis of a tetrapeptide //J. Am. Chem. Soc. 1963. Vol. 85. Pp. 2149–2154. DOI:https://doi.org/10.1021/ja00897a025.
100. Merrifield R.B., Stewart J.M., Jernberg N. Instrument for automated synthesis of peptides //Anal. Chem. 1966. Vol. 38. Pp. 1905–14.
101. Mhlongo J.T., Waddad A.Y., Albericio F. et al. Antimicrobial Peptide Synergies for Fighting Infectious Diseases //Adv Sci (Weinh). 2023 Sep. Vol. 10(26). DOI:https://doi.org/10.1002/advs.202300472.
102. Mwangi J., Kamau P.M., Thuku R.C. et al. Design methods for antimicrobial peptides with improved performance //Zool Res. 2023 Nov 18. Vol. 44(6). Pp. 1095–1114. DOI:https://doi.org/10.24272/j.issn.20958137.2023.246.
103. Nicolet B.H. The structure of glutathione //J. Biol. Chem. 1930. Vol. 88. Pp. 389–393.
104. Nilsson B.L., Soellner M.B., Raines R.T. Chemical synthesis of proteins //Annu Rev Biophys Biomol Struct. 2005. Vol. 34. Pp. 91–118.
105. Obradovic M., SudarMilovanovic E., Soskic S. et al. Leptin and Obesity: Role and Clinical Implication //Front Endocrinol (Lausanne). 2021 May 18. Vol. 12. P. 585887. DOI:https://doi.org/10.3389/fendo.2021.585887
106. Olfa M.K., Yosra H., Ikram G. et al. Neuroprotection with the Endozepine Octadecaneuropeptide, ODN //Current pharmaceutical design. 2018. Vol. 24(33). Pp. 3918–3925.
107. Ovchinnikov Yu. A., Ivanov V.T. The cyclic peptides: structure, conformation and function //The Proteins. Academic Press: New York, 1982. Vol. 5. Pp. 307–642.
108. Pavithrra G., Rajasekaran R. Gramicidin Peptide to Combat Antibiotic Resistance: A Review //International Journal of Peptide Research and Therapeutics. 2019. Vol. 26. Pp. 191–199.
109. Pedersen K.O., Synge R.L.M. Diffusion experiments on gramicidin S, tyrocidine, and gramicidin //Acta. Chem. Scand. 1948. Vol. 2. Pp. 408–413.
110. Pedersen S.L., Tofteng A.P., Malik L. et al. Microwave heating in solid-phase peptide synthesis //Chem. Soc. Rev. 2012. Vol. 41. Pp. 1826–1844. DOI:https://doi.org/10.1039/c1cs15214a.
111. Perakakis N., Farr O.M., Mantzoros C.S. Leptin in Leanness and Obesity: JACC State-of-the-Art Review //J. Am. Coll. Cardiol. 2021 Feb 16. Vol. 77(6). Pp. 745–760. DOI:https://doi.org/10.1016/j.jacc.2020.11.069.
112. Pertwee R.G. Endocannabinoids and their pharmacological actions //In Endocannabinoids. Springer, Cham. 2015. Pp. 1–37.
113. Philipson L.H., Bell G., Polonsky K.S. et al. 1930–2014: Discoverer of proinsulin //Proc. Natl. Acad. Sci. USA. 2015. Vol. 112(4). Pp. 940–1. DOI:https://doi.org/10.1073/pnas.1423774112.
114. Pietta P., Marshall G.R. Amide protection and amide supports in solid phase peptide synthesis //J. Chem. Soc. Chem. Comm. 1970. Vol. 11. Pp. 650–651.
115. Rajchakit U., Sarojini V. Recent developments in antimicrobial peptide conjugated gold nanoparticles //Bioconjugate chemistry. 2017. Vol. 28(11). Pp. 2673–2686.
116. Rendell M. Insulin: moments in history //Drug Development Research. 2008. Vol. 69(3). Pp. 95–100.
117. Rink H. Solidphase synthesis of protected peptide fragments using a trialkoxydiphenylmethylester resin //Tetrahedron Lett. 1987. Vol. 28. Pp. 3787–3790. DOI:https://doi.org/10.1016/S00404039(00)963846.
118. Sakakibara S., Kishida Y., Nishizawa R. et al. Use of anhydrous hydrogen fluoride in peptide synthesis //Procedures for the syntheses of simple peptides. Bull. Chem. Soc. Jpn. 1968. Vol. 41. P. 438. DOI:https://doi.org/10.1246/bcsj.41.438.
119. Sakakibara S., Shimonishi Y. New method for releasing oxytocin from fullyprotected nonapeptides using anhydrous hydrogen fluoride //Bull. Chem. Soc. Japan 1965. Vol. 38. Pp. 1412–1413.
120. Šakić Z., Rudež K.D., Radoš Kajić A. et al. Celebrating 100 years of insulin use //Acta. Clin. Croat. 2022 Nov. Vol. 61(3). Pp. 482–487. DOI:https://doi.org/10.20471/acc.2022.61.03.13.
121. Sanger F. Chemistry of insulin //Br. Med. Bull. 1960. Vol. 16. Pp. 183–186.
122. Sanger F., Smith L.F. The structure of insulin. Endeavour 1957. Vol. 16. Pp. 48–53.
123. Schnölzer M., Alewood P., Jones A. et al. In situ neutralization in boc chemistry solid phase peptide synthesis //Int. J. Pept. Prot. Res. 2009. Vol. 40. Pp. 180–193. DOI:https://doi.org/10.1111/j.13993011.1992.tb00291.x.
124. Sheehan J.C., Hess G.P. A new method of forming peptides bonds //J. Am. Chem. Soc. 1955. Vol. 77. Pp. 1067–1068.
125. Sieber P. A new acidlabile anchor group for the solidphase synthesis of cterminal peptide amides by the fmoc method //Tetrahedron Lett. 1987. Vol. 28. Pp. 2107–2110. DOI:https://doi.org/10.1016/S00404039(00)960556.
126. Sifferd R.H., du Vigneaud V. A new synthesis of carnosine, with some observations on the splitting of the benzyl group from carbobenzoxy derivatives and from benzylthioethers //J. Biol. Chem. 1935. Vol. 108. Pp. 753–761.
127. Singh A., Duche R.T., Wandhare A.G. et al. MilkDerived Antimicrobial Peptides: Overview, Applications, and Future Perspectives //Probiotics Antimicrob Proteins. 2023 Feb. Vol. 15(1). Pp. 44–62. DOI:https://doi.org/10.1007/s1260202210004y.
128. Smith P.S. Carbon-to-nitrogen migrations; what the last decade has brought //Trans. NY Acad. Sci. 1969. Vol. 31. Pp. 504–515.
129. Sneader W. Drug discovery: a history //John Wiley & Sons. 2005.
130. Steiner D.F. The proinsulin C-peptide — a multi-role model //Experimental Diabesity Research. 2004. Vol. 5(1). Pp. 7–14.
131. Suresh Babu V.V. One hundred years of peptide chemistry //Resonance. 2001. Vol. 6(10). Pp. 68–75.
132. Takebayashi M. The Curtius rearrangement: A historical description of its discovery and explanation //Kagakushi Kenkyu. 1989. Vol. 16. Pp. 149–153.
133. Tanford C., Reynolds J. Oxford University Press. 2001. 304 Pp.
134. Tuppy H., Michl H. Uber die chemische struktur des oxytocine //Monatsh. Chem. 1953. Vol. 84. Pp. 1011–1020.
135. Uhlig T. et al. The emergence of peptides in the pharmaceutical business: From exploration to exploitation //EuPA Open Proteomics. 2014. Vol. 4. Pp. 58–69.
136. Van Beek C., Leonid V. Sobolev. 1876–1919. Diabetes. 1958 May — Jun. Vol. 7(3). Pp. 245–8. DOI:https://doi.org/10.2337/diab.7.3.245.
137. Wang G., Vaisman I.I., van Hoek M.L. Machine Learning Prediction of Antimicrobial Peptides //Methods Mol Biol. 2022. Vol. 2405. Pp. 1–37. DOI:https://doi.org/10.1007/9781071618554_1.
138. Wang S.S. Palkoxybenzyl alcohol resin and palkoxybenzyloxycarbonylhydrazide resin for solid phase synthesis of protected peptide fragments //J. Am. Chem. Soc. 1973. Vol. 95. Pp. 1328–1333.
139. Zamyatnin A.A. EROPMoscow. Endogenous regulatory oligopeptide knowledge base. 2002. URL: http://erop.inbi.ras.ru.
