References
- M. Li, M. Liu, Y. Shang, C. Ren, J. Liu, H. Jin and Z. Wang, The substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides, RSC Adv. 10(23) (2020) 13900–13906; https://doi.org/10.1039/C9RA10325B
- M. Abdulbagi, L. Wang, O. Siddig, B. Di and B. Li, d-amino acids and d-amino acid-containing peptides: Potential disease biomarkers and therapeutic targets?, Biomolecules 11(11) (2021) Article ID 1716 (14 pages); https://doi.org/10.3390/biom11111716
- A. A. Ageeva, A. B. Doktorov, N. E. Polyakov and T. V. Leshina, Chiral linked systems as a model for understanding d-amino acids influence on the structure and properties of amyloid peptides, Int. J. Mol. Sci. 23(6) (2022) Article ID 3060 (18 pages); https://doi.org/10.3390/ijms23063060
- A. Jilek and G. Kreil, d-amino acids in animal peptides, Monatsh. Chem. 139 (2008) 1–5; https://doi.org/10.1007/s00706-007-0780-5
- P. Conti, L. Tamborini and A. Pinto, Drug discovery targeting amino acid racemases, Chem. Rev. 111(11) (2011) 6919–6946; https://doi.org/10.1021/cr2000702
- E. Rosini, P. D’Antona and L.Pollegioni, Biosensors for d-amino acids: Detection methods and applications, Int. J. Mol. Sci. 21(13) (2020) Article ID 4574 (16 pages); https://doi.org/10.3390/ijms21134574
- P. Turcic, M. Bradamante, K. Houra, N. Stambuk, T. Kelava, P. Konjevoda, S. Kazazic, D. Vikic--Topic and B. Pokric, Effects of alpha-melanocortin enantiomers on acetaminophen-induced hepatotoxicity in CBA mice, Molecules 14(12) (2009) 5017–5026; https://doi.org/10.3390/molecules14125017
- C. Jia, C. B. Lietz, Q. Yu and L. Li, Site-specific characterization of d-amino acid containing peptide epimers by ion mobility spectrometry, Anal. Chem. 86 (2014) 2972–2981; https://doi.org/10.1021/ac4033824
- M. V. Humpola, R. Spinelli, M. Erben, V. Perdomo, G. G. Tonarelli, F. Albericio and A. S. Siano, d- and N-methyl amino acids for modulating the therapeutic properties of antimicrobial peptides and lipopeptides, Antibiotics 12(5) (2023) Article ID 821 (15 pages); https://doi.org/10.3390/antibiotics12050821
- G. Murtas and L. Pollegioni, d-amino acids as novel blood-based biomarkers, Curr. Med. Chem. 29(24) (2022) 4202–4215; https://dx.doi.org/10.2174/0929867328666211125092438
- Y. Shi, Z. Hussain and Y. Zhao, Promising application of d-amino acids toward clinical therapy, Int. J. Mol. Sci. 23(18) (2022) Article ID 10794 (18 pages); https://doi.org/10.3390/ijms231810794
- G. Murtas and L. Pollegioni, d-Amino acids and cancer: Friends or foes?, Int. J. Mol. Sci. 24(4) (2023) Article ID 3274 (12 pages); https://doi.org/10.3390/ijms24043274
- R. P. Millar, Y. F. Zhu, C. Chen and R. S. Struthers, Progress towards the development of non-peptide orally-active gonadotropin-releasing hormone (GnRH) antagonists: Therapeutic implications, Br. Med. Bull. 56(3) (2000) 761–772; https://doi.org/10.1258/0007142001903346
- J. M. Cullen and M. Cascella, Physiology, Enkephalin, in StatPearls [Internet], StatPearls Publishing, Treasure Island 2025; https://www.ncbi.nlm.nih.gov/books/NBK557764/N
- J. Tian, W. Fu, Z. Xie, Y. Zhao, H. Yang and J. Zhao, Methionine enkephalin (MENK) protected macrophages from ferroptosis by downregulating HMOX1 and ferritin, Proteome Sci. 22 (2024) Article ID 2 (15 pages); https://doi.org/10.1186/s12953-024-00228-x
- X. Wang, S. Li, S. Yan, Y. Shan, X. Wang, Z. Jingbo, Y. Wang, F. Shan, N. Griffin and X. Sun, Methionine enkephalin inhibits colorectal cancer by remodeling the immune status of the tumor microenvironment, Int. Immunopharmacol. 111 (2022) Article ID 109125 (12 pages); https://doi.org/10.1016/j.intimp.2022.109125
- V. Asokan, A. M. Koundinya and V. Aranganathan, An overview of opioid peptides: Their sources and molecular sequences, J. Opioid Management 21 (2025) 439–459; https://doi.org/10.5055/jom.0954Y
- Y. Tuo, C. Tian, L. Lu and M. Xiang, The paradoxical role of methionine enkephalin in tumor responses, Eur. J. Pharmacol. 882 (2020) Article ID 173253 (10 pages); https://doi.org/10.1016/j.ejphar.2020.173253
- N. Qu, R. Wang, Y. Meng, N. Liu, J. Zhai and F. Shan, Methionine enkephalin inhibited cervical carcinoma via apoptosis promotion and reduction of myeloid derived suppressor cell infiltrated in tumor, Int. Immunopharmacol. 110 (2022) Article ID 108933 (10 pages); https://doi.org/10.1016/j.intimp.2022.108933
- R. Martinić, H. Šošić, P. Turčić, P. Konjevoda, A. Fučić, R. Stojković, G. Aralica, M. Gabričević, T. Weitner and N. Štambuk, Hepatoprotective effects of Met-enkephalin on acetaminophen-induced liver lesions in male CBA mice, Molecules 19(8) (2014) 11833–11845; https://doi.org/10.3390/molecules190811833
- B. D. Janković and D. Marić, Enkephalins as Regulators of Inflammatory Immune Reactions, in Neuropeptides and Immunoregulation (Ed. B. Scharrer, E. M. Smith and G. B. Stefano) Springer-Verlag, Berlin 1994, pp. 76–100.
- X. Bai, F. Shan, N. Qu, H. Huang, M. Handley, N. Griffin, S. Zhang and X. Cao, Regulatory role of methionine enkephalin in myeloid-derived suppressor cells and macrophages in human cutaneous squamous cell carcinoma, Int. Immunopharmacol. 99 (2021) Article ID 107996 (6 pages); https://doi.org/10.1016/j.intimp.2021.107996
- P. Konjevoda, N. Štambuk, G. Aralica and B. Pokrić, Cytoprotective effects of met-enkephalin and α-MSH on ethanol induced gastric lesions in rats, J. Physiol. (Paris) 95(1–6) (2001) 277–281; https://doi.org/10.1016/s0928-4257(01)00038-9
- N. Štambuk, N. Kopjar, K. Šentija, V. Garaj-Vrhovac, D. Vikić-Topić, B. Marušić-Della Marina, V. Brinar, M. Trbojević-Čepe, N. Žarković, B. Ćurković, Ð. Babić-Naglić, M. Hadžija, N. Zurak, Z. Brzović, R. Martinić, V. Štambuk, P. Konjevoda, N. Ugrinović, I. Pavlić-Renar, Z. Biđin and B. Pokrić, Cytogenetic effects of Met-enkephalin (peptid-M) on human lymphocytes, Croat. Chem. Acta 71(3) (1998) 591–605; https://hrcak.srce.hr/132370
- D. Tjesić-Drinković, N. Štambuk, D. Tjesić-Drinković, P. Konjevoda, N. Gotovac, T. Ćurović and A. Votava Raić, Met-enkephalin effects on histamine-induced bronhoconstriction in guinea pigs, Coll. Antropol. 29(2) (2005) 689–692; https://hrcak.srce.hr/5330
- P. Konjevoda, N. Štambuk, D. Vikić-Topić, A. Boban-Blagaić, S. Vikić-Topić, V. Mrljak, J. Pavan, P. Ramadan and Z. Biđin, Protective effects of met-enkephalin on alcohol induced gastric lesions, Croat. Chem. Acta 73(4) (2000) 1111–1121; https://hrcak.srce.hr/131992
- A. D. Miller, Sense-antisense (complementary) peptide interactions and the proteomic code; potential opportunities in biology and pharmaceutical science, Expert Opin. Biol. Ther. 15(2) (2015) 245–267; https://doi.org/10.1517/14712598.2015.983069
- K. Hinz, M. Niu, H. M. Ni and W. X. Ding, Targeting autophagy for acetaminophen-induced liver injury: An update, Livers 4(3) (2024) 377–387; https://doi.org/10.3390/livers4030027
- F. Guarner, N. K. Boughton-Smith, G. J. Blackwell and S. Moncada, Reduction by prostacyclin of acetaminophen-induced liver toxicity in the mouse, Hepatology 8(2) (1988) 248–253; https://doi.org/10.1002/hep.1840080210
- H. Jaeschke and A. Ramachandran, Acetaminophen hepatotoxicity: Paradigm for understanding mechanisms of drug-induced liver injury, Annu. Rev. Pathol. 19 (2024) 453–478; https://doi.org/10.1146/annurev-pathmechdis-051122-094016
- P. Turcic, N. Stambuk, P. Konjevoda, T. Kelava, M. Gabricevic, R. Stojkovic and G. Aralica, Modulation of γ2-MSH hepatoprotection by antisense peptides and melanocortin subtype 3 and 4 receptor antagonists, Med. Chem. 11(3) (2015) 286–295; https://dx.doi.org/10.2174/1573406410666140914161421
- V. M. Silva, C. Chen, G. E. Hennig, H. E. Whiteley and E. J. Manautou, Changes in susceptibility to acetaminophen-induced liver injury by the organic anion indocyanine green, Food Chem. Tox. 39(3) (2001) 271–278; https://doi.org/10.1016/s0278-6915(00)00138-1
- K. Houra, P. Turčić, M. Gabričević, T. Weitner, P. Konjevoda and N. Štambuk, Interaction of α-melanocortin and its pentapeptide antisense LVKAT: Effects on hepatoprotection in male CBA mice, Molecules 16(9) (2011) 7331–7343; https://doi.org/10.3390/molecules16097331
- N. Štambuk, Z. Manojlović, P. Turčić, R. Martinić, P. Konjevoda, T. Weitner, P. Wardega and M. Gabričević, A simple three-step method for design and affinity testing of new antisense peptides: An example of erythropoietin, Int. J. Mol. Sci. 15(6) (2014) 9209–9223; https://doi.org/10.3390/ijms15069209
- H. Gampp, M. Maeder, C. J. Meyer and A. D. Zuberbühler, Calculation of equilibrium constants from multiwavelength spectroscopic data-I: Mathematical considerations, Talanta 32(2) (1985) 95–101; https://doi.org/10.1016/0039-9140(85)80035-7
- H. Gampp, M. Maeder, C. J. Meyer and A. D. Zuberbühler, Calculation of equilibrium constants from multiwavelength spectroscopic data-II132, 95.: Specfit: Two user-friendly programs in basic and standard FORTRAN 77, Talanta 32(4) (1985) 257–264; https://doi.org/10.1016/0039-9140(85)80077-1
- H. Gampp, M. Maeder, C. J. Meyer and A. D. Zuberbühler, Calculation of equilibrium constants from multiwavelength spectroscopic data-IV: Model-free least-squares refinement by use of evolving factor analysis, Talanta 33(12) (1986) 943–951; https://doi.org/10.1016/0039-9140(86)80233-8
- V. Blagaić, K. Houra, P. Turčić, N. Stambuk, P. Konjevoda, A. Boban-Blagaić, T. Kelava, M. Kos, G. Aralica and F. Culo, The influence of α-, β-, and γ-melanocyte stimulating hormone on acetaminophen induced liver lesions in male CBA mice, Molecules 15(3) (2010) 1232–1241; https://doi.org/10.3390/molecules15031232
- H. Jaeschke, Role of inflammation in the mechanism of acetaminophen-induced hepatotoxicity, Expert Opin. Drug Metab. Toxicol. 1(3) (2005) 389–397; https://doi.org/10.1517/17425255.1.3.389
- S. D. Nelson and S. A. Bruschi, Mechanisms of Acetaminophen-induced Liver Disease, in Drug-Induced Liver Disease (Ed. N. Kaplowitz and L. D. DeLeve), Informa Healthcare, New York 2007, pp. 353–388.
- E. J. Calabrese and L. A. Baldwin, Hormesis: The dose-response revolution, Annu. Rev. Pharmacol. Toxicol. 43 (2003) 175–197; https://doi.org/10.1146/annurev.pharmtox.43.100901.140223
- T. P. Khaket, J. Singh, P. Attri and S. Dhanda, Enkephalin degrading enzymes: Metalloproteases with high potential for drug development, Curr. Pharm. Des. 18(2) (2012) 220–230; https://doi.org/10.2174/138161212799040547
- N. Štambuk, P. Konjevoda, A. Boban-Blagaić and B. Pokrić, Molecular recognition theory of the complementary (antisense) peptide interactions, Theory Biosci. 123(4) (2005) 265–275; https://doi.org/10.1016/j.thbio.2005.02.001
- J. C. Biro, The proteomic code: A molecular recognition code for proteins, Theor. Biol. Med. Model. 4 (2007) 1–45; https://doi.org/10.1186/1742-4682-4-45
- M. García-Domínguez, Enkephalins and pain modulation: Mechanisms of action and therapeutic perspectives, Biomolecules 14 (2024) Article ID 926 (23 pages); https://doi.org/10.3390/biom14080926
- N. Štambuk, P. Konjevoda, P. Turčić, H. Šošić, G. Aralica, D. Babić, S. Seiwerth, Ž. Kaštelan, R. Novak Kujundžić, P. Wardega, J. Barać Žutelija, A. Gudelj Gračanin and M. Gabričević, Targeting tumor markers with antisense peptides: An example of human prostate specific antigen, Int. Mol. Sci. 20(9) (2019) Article ID 2090 (20 pages); https://doi.org/10.3390/ijms20092090