메뉴 건너뛰기




Volumn 63, Issue 2, 2015, Pages 716-722

Alpha-substituted derivatives of cinnamaldehyde as tyrosinase inhibitors: Inhibitory mechanism and molecular analysis

Author keywords

derivatives of cinnamaldehyde; fluorescence quenching; molecular docking; tyrosinase

Indexed keywords

AMINO ACIDS; FLUORESCENCE; METAL IONS; MOLECULAR MODELING;

EID: 84921472595     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf505469k     Document Type: Article
Times cited : (84)

References (34)
  • 1
    • 0344307448 scopus 로고    scopus 로고
    • Inhibitory effects of mushroom tyrosinase by some alkylbenzaldehydes
    • Chen, Q. X.; Song, K. K.; Wang, Q.; Huang, H. Inhibitory effects of mushroom tyrosinase by some alkylbenzaldehydes J. Enzyme Inhib. Med. Chem. 2003, 18, 491-496
    • (2003) J. Enzyme Inhib. Med. Chem. , vol.18 , pp. 491-496
    • Chen, Q.X.1    Song, K.K.2    Wang, Q.3    Huang, H.4
  • 3
    • 84889580216 scopus 로고    scopus 로고
    • Tyrosinase and tyrosinase inhibitors
    • Chang, T. M. Tyrosinase and tyrosinase inhibitors J. Biocatal. Biotransform. 2012, 1, 1-2
    • (2012) J. Biocatal. Biotransform. , vol.1 , pp. 1-2
    • Chang, T.M.1
  • 4
    • 0032034869 scopus 로고    scopus 로고
    • Synthesis and in vitro cytotoxicity of cinnamaldehydes to human solid tumor cells
    • Kwon, B. M.; Lee, S. H.; Choi, S. U.; Park, S. H.; Lee, C. O.; Cho, Y. K. Synthesis and in vitro cytotoxicity of cinnamaldehydes to human solid tumor cells Arch. Pharmacal Res. 1998, 21, 147-152
    • (1998) Arch. Pharmacal Res. , vol.21 , pp. 147-152
    • Kwon, B.M.1    Lee, S.H.2    Choi, S.U.3    Park, S.H.4    Lee, C.O.5    Cho, Y.K.6
  • 5
    • 0035451659 scopus 로고    scopus 로고
    • The antimutagenic effect of vanillin and cinnamaldehyde on spontaneous mutation in Salmonella TA104 is due to a reduction in mutations at GC but not at sites
    • Shaughnessy, D. T.; Setzer, R. W.; DeMarini, D. M. The antimutagenic effect of vanillin and cinnamaldehyde on spontaneous mutation in Salmonella TA104 is due to a reduction in mutations at GC but not AT sites Mutat. Res. 2001, 480, 55-69
    • (2001) Mutat. Res. , vol.480 , pp. 55-69
    • Shaughnessy, D.T.1    Setzer, R.W.2    Demarini, D.M.3
  • 6
    • 10944258482 scopus 로고    scopus 로고
    • Antifungal activities of essential oils and their constituents from indigenous cinnamon (Cinnamomum osmophloeum) leaves against wood decay fungi
    • Wang, S. Y.; Chen, P. F.; Chang, S. T. Antifungal activities of essential oils and their constituents from indigenous cinnamon (Cinnamomum osmophloeum) leaves against wood decay fungi Bioresour. Technol. 2005, 96, 813-818
    • (2005) Bioresour. Technol. , vol.96 , pp. 813-818
    • Wang, S.Y.1    Chen, P.F.2    Chang, S.T.3
  • 7
    • 24944461923 scopus 로고    scopus 로고
    • Chemical polymorphism and antifungal activity of essential oils from leaves of different provenances of indigenous cinnamon (Cinnamomum osmophloeum)
    • Cheng, S. S.; Liu, J. Y.; Hsui, Y. R.; Chang, S. T. Chemical polymorphism and antifungal activity of essential oils from leaves of different provenances of indigenous cinnamon (Cinnamomum osmophloeum) Bioresour. Technol. 2006, 97, 306-312
    • (2006) Bioresour. Technol. , vol.97 , pp. 306-312
    • Cheng, S.S.1    Liu, J.Y.2    Hsui, Y.R.3    Chang, S.T.4
  • 8
    • 16244397279 scopus 로고    scopus 로고
    • A toxicologic and dermatologic assessment of cinnamyl alcohol, cinnamaldehyde, and cinnamic acid when used as fragrance ingredients
    • Bickers, D.; Calow, P.; Greim, H.; Hanifin, J. M.; Rogers, A. E.; Saurat, J. H.; Sipes, I. G.; Smith, R. L.; Tagami, H. A toxicologic and dermatologic assessment of cinnamyl alcohol, cinnamaldehyde, and cinnamic acid when used as fragrance ingredients Food Chem. Toxicol. 2005, 43, 799-836
    • (2005) Food Chem. Toxicol. , vol.43 , pp. 799-836
    • Bickers, D.1    Calow, P.2    Greim, H.3    Hanifin, J.M.4    Rogers, A.E.5    Saurat, J.H.6    Sipes, I.G.7    Smith, R.L.8    Tagami, H.9
  • 9
    • 0033230675 scopus 로고    scopus 로고
    • Tyrosinase inhibitory activity of the olive oil flavor compounds
    • Isao, K.; Ikuyo, K.-H. Tyrosinase inhibitory activity of the olive oil flavor compounds J. Agric. Food Chem. 1999, 47, 4574-4578
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 4574-4578
    • Isao, K.1    Ikuyo, K.-H.2
  • 11
    • 0032970672 scopus 로고    scopus 로고
    • Inhibition of human tumor growth by 2′-hydroxy- and 2′-benzoyloxycinnamaldehydes
    • Lee, C. W.; Hong, D. H.; Han, S. B.; Park, S. H.; Kim, H. K.; Kwon, B. M.; Kim, H. M. Inhibition of human tumor growth by 2′-hydroxy- and 2′-benzoyloxycinnamaldehydes Planta Med. 1999, 65, 263-266
    • (1999) Planta Med. , vol.65 , pp. 263-266
    • Lee, C.W.1    Hong, D.H.2    Han, S.B.3    Park, S.H.4    Kim, H.K.5    Kwon, B.M.6    Kim, H.M.7
  • 12
    • 33644747263 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of dimeric cinnamaldehydes as potent antitumor agents
    • Shin, D. S.; Kim, J. H.; Lee, S. K.; Han, D. C.; Son, K. H. Synthesis and biological evaluation of dimeric cinnamaldehydes as potent antitumor agents Bioorg. Med. Chem. 2006, 14, 2498-2506
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 2498-2506
    • Shin, D.S.1    Kim, J.H.2    Lee, S.K.3    Han, D.C.4    Son, K.H.5
  • 13
    • 0023715711 scopus 로고
    • Studies on the metabolic fate of a-bromocinnamaldehyde (an anti-fungal agent) in rat
    • Akimoto, Y.; Nito, S.; Urakubo, G. Studies on the metabolic fate of a-bromocinnamaldehyde (an anti-fungal agent) in rat Pharm. Soc. Jpn. 1988, 34 (4) 303-312
    • (1988) Pharm. Soc. Jpn. , vol.34 , Issue.4 , pp. 303-312
    • Akimoto, Y.1    Nito, S.2    Urakubo, G.3
  • 14
    • 84863116655 scopus 로고    scopus 로고
    • Synthesis and antityrosinase mechanism of benzaldehyde thiosemicarbazones: Novel tyrosinase inhibitors
    • Chen, L. H.; Hu, Y. H.; Wei, S.; Song, K. K.; Liu, X.; Jia, Y. L.; Zhuang, J. X.; Chen, Q. X. Synthesis and antityrosinase mechanism of benzaldehyde thiosemicarbazones: Novel tyrosinase inhibitors J. Agric. Food Chem. 2012, 60, 1542-1547
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 1542-1547
    • Chen, L.H.1    Hu, Y.H.2    Wei, S.3    Song, K.K.4    Liu, X.5    Jia, Y.L.6    Zhuang, J.X.7    Chen, Q.X.8
  • 15
    • 21544481468 scopus 로고    scopus 로고
    • Inhibition of the activity of mushroom tyrosinase by alkylbenzoic acids
    • Huang, X. H.; Chen, Q. X.; Wang, Q.; Song, K. K.; Wang, J.; Li, S.; Guan, X. Inhibition of the activity of mushroom tyrosinase by alkylbenzoic acids Food Chem. 2006, 94, 1-6
    • (2006) Food Chem. , vol.94 , pp. 1-6
    • Huang, X.H.1    Chen, Q.X.2    Wang, Q.3    Song, K.K.4    Wang, J.5    Li, S.6    Guan, X.7
  • 16
    • 84861142860 scopus 로고    scopus 로고
    • NMR, HPLC-ESI-MS, and MALDI-TOF MS analysis of condensed tannins from Delonix regia (Bojer ex Hook.) Rat and their bioactivities
    • Chai, W. M.; Shi, Y.; Feng, H. L.; Qiu, L.; Zhou, H. C.; Deng, Z. W.; Yan, C. L.; Chen, Q. X. NMR, HPLC-ESI-MS, and MALDI-TOF MS analysis of condensed tannins from Delonix regia (Bojer ex Hook.) Rat and their bioactivities J. Agric. Food Chem. 2012, 60, 5013-5022
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 5013-5022
    • Chai, W.M.1    Shi, Y.2    Feng, H.L.3    Qiu, L.4    Zhou, H.C.5    Deng, Z.W.6    Yan, C.L.7    Chen, Q.X.8
  • 17
    • 78649672810 scopus 로고    scopus 로고
    • Inhibition kinetics of chlorobenzaldehyde thiosemicarbazones on mushroom tyrosinase
    • Li, Z. C.; Chen, L. H.; Yu, X. J.; Hu, Y. H.; Song, K. K.; Zhou, X. W.; Chen, Q. X. Inhibition kinetics of chlorobenzaldehyde thiosemicarbazones on mushroom tyrosinase J. Agric. Food Chem. 2010, 58, 12537-12540
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 12537-12540
    • Li, Z.C.1    Chen, L.H.2    Yu, X.J.3    Hu, Y.H.4    Song, K.K.5    Zhou, X.W.6    Chen, Q.X.7
  • 18
    • 70350565386 scopus 로고    scopus 로고
    • Inhibitory effects of p -alkylbenzoic acids on the activity of polyphenol oxidase from potato (Solanum tuberosum)
    • Lin, M.; Ke, L. N.; Han, P.; Qiu, L.; Chen, Q. X.; Lin, H. T.; Wang, Q. Inhibitory effects of p -alkylbenzoic acids on the activity of polyphenol oxidase from potato (Solanum tuberosum) Food Chem. 2010, 119, 660-663
    • (2010) Food Chem. , vol.119 , pp. 660-663
    • Lin, M.1    Ke, L.N.2    Han, P.3    Qiu, L.4    Chen, Q.X.5    Lin, H.T.6    Wang, Q.7
  • 20
    • 0035847062 scopus 로고    scopus 로고
    • Effect of captopril on mushroom tyrosinase activity in vitro
    • Espin, J. C.; Wichers, H. J. Effect of captopril on mushroom tyrosinase activity in vitro Biochim. Biophys. Acta 2001, 1544, 289-300
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 289-300
    • Espin, J.C.1    Wichers, H.J.2
  • 21
    • 33244460034 scopus 로고    scopus 로고
    • Flavonoids as mushroom tyrosinase inhibitors: A fluorescence quenching study
    • Kim, D.; Park, J.; Kim, J.; Han, C.; Yoon, J.; Kim, N.; Seo, J.; Lee, C. Flavonoids as mushroom tyrosinase inhibitors: A fluorescence quenching study J. Agric. Food Chem. 2006, 54, 935-941
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 935-941
    • Kim, D.1    Park, J.2    Kim, J.3    Han, C.4    Yoon, J.5    Kim, N.6    Seo, J.7    Lee, C.8
  • 22
    • 1642317115 scopus 로고    scopus 로고
    • Binding of wogonin to human serum albumin: A common binding site of wogonin in subdomain IIA
    • Tian, J.; Liu, J.; Xie, J.; Yao, X.; Hu, Z.; Chen, X. Binding of wogonin to human serum albumin: A common binding site of wogonin in subdomain IIA J. Photochem. Photobiol., B 2004, 74, 39-45
    • (2004) J. Photochem. Photobiol., B , vol.74 , pp. 39-45
    • Tian, J.1    Liu, J.2    Xie, J.3    Yao, X.4    Hu, Z.5    Chen, X.6
  • 23
    • 80054846424 scopus 로고    scopus 로고
    • Mechanism of inhibition of arginine kinase by flavonoids consistent with thermodynamics of docking simulation
    • Wang, H. R.; Zhu, W. J.; Wang, X. Y. Mechanism of inhibition of arginine kinase by flavonoids consistent with thermodynamics of docking simulation Int. J. Biol. Macromol. 2011, 49, 985-991
    • (2011) Int. J. Biol. Macromol. , vol.49 , pp. 985-991
    • Wang, H.R.1    Zhu, W.J.2    Wang, X.Y.3
  • 24
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftinka, M. R.; Ghirona, C. A. Fluorescence quenching studies with proteins Anal. Biochem. 1981, 114, 199-227
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftinka, M.R.1    Ghirona, C.A.2
  • 25
    • 13544275107 scopus 로고    scopus 로고
    • Binding of the bioactive component Jatrorrhizine to human serum albumin
    • Li, Y.; He, W.; Liu, J.; Sheng, F.; Hu, Z.; Chen, X. Binding of the bioactive component Jatrorrhizine to human serum albumin Biochim. Biophys. Acta 2005, 1722, 15-21
    • (2005) Biochim. Biophys. Acta , vol.1722 , pp. 15-21
    • Li, Y.1    He, W.2    Liu, J.3    Sheng, F.4    Hu, Z.5    Chen, X.6
  • 26
    • 43749120522 scopus 로고    scopus 로고
    • Study on the interaction between cinnamic acid and human serum albumin by fluorescence quenching method
    • Zhao, Y.; Cao, Y.; Han, F. M.; Chen, Y. Study on the interaction between cinnamic acid and human serum albumin by fluorescence quenching method Spectrosc. Spectral Anal. 2008, 44, 904-907
    • (2008) Spectrosc. Spectral Anal. , vol.44 , pp. 904-907
    • Zhao, Y.1    Cao, Y.2    Han, F.M.3    Chen, Y.4
  • 28
    • 79956132740 scopus 로고    scopus 로고
    • Exploring the mechanism of fluorescence quenching in proteins induced by tetracycline
    • Anand, U.; Jash, C.; Boddepalli, R. K.; Shrivastava, A.; Mukherjee, S. Exploring the mechanism of fluorescence quenching in proteins induced by tetracycline J. Phys. Chem. B 2011, 115, 6312-6320
    • (2011) J. Phys. Chem. B , vol.115 , pp. 6312-6320
    • Anand, U.1    Jash, C.2    Boddepalli, R.K.3    Shrivastava, A.4    Mukherjee, S.5
  • 29
    • 84861142860 scopus 로고    scopus 로고
    • Structure characterization and anti-tyrosinase mechanism of polymeric proanthocyanidins fractionated from kiwifruit pericarp
    • Chai, W. M.; Shi, Y.; Feng, H. L.; Qiu, L.; Zhou, H. C.; Deng, Z. W.; Yan, C. L.; Chen, Q. X. Structure characterization and anti-tyrosinase mechanism of polymeric proanthocyanidins fractionated from kiwifruit pericarp J. Agric. Food Chem. 2012, 60, 5013-5022
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 5013-5022
    • Chai, W.M.1    Shi, Y.2    Feng, H.L.3    Qiu, L.4    Zhou, H.C.5    Deng, Z.W.6    Yan, C.L.7    Chen, Q.X.8
  • 30
    • 84921474818 scopus 로고
    • Preparation antimicrobial activity of α-bromo-cinnamaldehyde and its application
    • Xiao, K. J.; Ning, Z. X. Preparation antimicrobial activity of α-bromo-cinnamaldehyde and its application Food Mach. 1995, 5, 26-28
    • (1995) Food Mach. , vol.5 , pp. 26-28
    • Xiao, K.J.1    Ning, Z.X.2
  • 31
    • 84874186509 scopus 로고    scopus 로고
    • Molecular inhibitory mechanism of tricin on tyrosinase
    • Mu, Y.; Li, L.; Hu, S. Q. Molecular inhibitory mechanism of tricin on tyrosinase Spectrochim. Acta, Part A 2013, 107, 235-240
    • (2013) Spectrochim. Acta, Part A , vol.107 , pp. 235-240
    • Mu, Y.1    Li, L.2    Hu, S.Q.3
  • 34
    • 84921444001 scopus 로고
    • Study on the toxicities of alpha-bromocinnamaldehyde and structure-effect relationship
    • Lu, D.; Bi, J.; He, Q. Y.; Wang, J.; Chen, Y. F.; Yin, M. Q. Study on the toxicities of alpha-bromocinnamaldehyde and structure-effect relationship Carcinog., Teratog. Mutagen. 1992, 4 (5) 22-25
    • (1992) Carcinog., Teratog. Mutagen. , vol.4 , Issue.5 , pp. 22-25
    • Lu, D.1    Bi, J.2    He, Q.Y.3    Wang, J.4    Chen, Y.F.5    Yin, M.Q.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.