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Volumn 18, Issue 3, 2015, Pages 499-507

In silico evaluation of potential DPP-III inhibitor precursors from dietary proteins

Author keywords

Bioactive peptide; Dietary protein; Dipeptidyl peptidase (DPP) III; In silico analysis; Inhibitor

Indexed keywords

ANIMALS; OILSEEDS;

EID: 84921340620     PISSN: 10942912     EISSN: 15322386     Source Type: Journal    
DOI: 10.1080/10942912.2013.787626     Document Type: Article
Times cited : (14)

References (37)
  • 1
    • 65849395509 scopus 로고    scopus 로고
    • Enkephalinase inhibitors: Potential agents for the management of pain
    • Thanawala, V.; Kadam, V.J.; Ghosh, R. Enkephalinase inhibitors: Potential agents for the management of pain. Current Drug Targets 2008, 9, 887-894.
    • (2008) Current Drug Targets , vol.9 , pp. 887-894
    • Thanawala, V.1    Kadam, V.J.2    Ghosh, R.3
  • 3
    • 80054748041 scopus 로고    scopus 로고
    • Interaction of goat brain enkephalin degrading enzymes with analgesic and antihypertensive drugs
    • Dhanda, S.; Singh, J.; Singh, H. Interaction of goat brain enkephalin degrading enzymes with analgesic and antihypertensive drugs. Medicinal Chemistry Research 2011, 20, 1294-1297.
    • (2011) Medicinal Chemistry Research , vol.20 , pp. 1294-1297
    • Dhanda, S.1    Singh, J.2    Singh, H.3
  • 4
    • 84856424923 scopus 로고    scopus 로고
    • Enkephalin degrading enzymes: Metalloproteases with high potential for drug development
    • Khaket, T.P.; Singh, J.; Attri, P.; Dhanda, S. Enkephalin degrading enzymes: Metalloproteases with high potential for drug development. Current Pharmaceutical Design 2012, 18, 220-230.
    • (2012) Current Pharmaceutical Design , vol.18 , pp. 220-230
    • Khaket, T.P.1    Singh, J.2    Attri, P.3    Dhanda, S.4
  • 5
    • 42949134480 scopus 로고    scopus 로고
    • Hydrolysis of various bioactive peptides by goat brain dipeptidylpeptidase-III
    • Dhanda, S.; Singh, H.; Singh, J. Hydrolysis of various bioactive peptides by goat brain dipeptidylpeptidase-III. Cell Biochemistry and Function 2008, 23 (3), 339-345.
    • (2008) Cell Biochemistry and Function , vol.23 , Issue.3 , pp. 339-345
    • Dhanda, S.1    Singh, H.2    Singh, J.3
  • 6
    • 40949154724 scopus 로고    scopus 로고
    • Functional characterization and specific effects of various peptides on enzymatic activity of a DPP-III homologue from goat brain
    • Dhanda, S.; Singh, H.; Singh, J.; Singh, T.P. Functional characterization and specific effects of various peptides on enzymatic activity of a DPP-III homologue from goat brain. Journal of Enzyme Inhibition and Medicinal Chemistry 2008, 23, 174-181.
    • (2008) Journal of Enzyme Inhibition and Medicinal Chemistry , vol.23 , pp. 174-181
    • Dhanda, S.1    Singh, H.2    Singh, J.3    Singh, T.P.4
  • 7
    • 0019404594 scopus 로고
    • Mechanism of kyotorphin-induced release of Met-enkephalin from guinea pigs striatum and spinal cord
    • Shiomi, H.; Kuraishi, Y.; Ueda, H.; Harada, Y.; Amano, H.; Takagi, H. Mechanism of kyotorphin-induced release of Met-enkephalin from guinea pigs striatum and spinal cord. Brain Research 1981, 221, 161-169.
    • (1981) Brain Research , vol.221 , pp. 161-169
    • Shiomi, H.1    Kuraishi, Y.2    Ueda, H.3    Harada, Y.4    Amano, H.5    Takagi, H.6
  • 8
    • 0034111712 scopus 로고    scopus 로고
    • Characterization of tynorphin, a potent endogenous inhibitor of dipeptidyl peptidase-III
    • Yamamoto, Y.; Hashimoto, J.; Shimamura, M.; Yamaguchi, T.; Hazato, T. Characterization of tynorphin, a potent endogenous inhibitor of dipeptidyl peptidase-III. Peptides 2000, 21 (4), 503-508.
    • (2000) Peptides , vol.21 , Issue.4 , pp. 503-508
    • Yamamoto, Y.1    Hashimoto, J.2    Shimamura, M.3    Yamaguchi, T.4    Hazato, T.5
  • 9
    • 33847625986 scopus 로고    scopus 로고
    • Novel amidino-substituted benzimidazoles, synthesis of compounds and inhibition of dipeptidyl peptidase III
    • Agic, D.; Hranjec, M.; Jajcanin, N.; Starcevic, K.; Karminski-Zamola, G.; Abramic, M. Novel amidino-substituted benzimidazoles, synthesis of compounds and inhibition of dipeptidyl peptidase III. Bioorganic Chemistry 2007, 35, 153-169.
    • (2007) Bioorganic Chemistry , vol.35 , pp. 153-169
    • Agic, D.1    Hranjec, M.2    Jajcanin, N.3    Starcevic, K.4    Karminski-Zamola, G.5    Abramic, M.6
  • 11
    • 0036889977 scopus 로고    scopus 로고
    • Spinorphin as an endogenous inhibitor of enkephalin-degrading enzymes, roles in pain and inflammation
    • Yamamoto, Y.; Ono, H.; Ueda, A.; Shimamura, M.; Nishimura, K.; Hazato, T. Spinorphin as an endogenous inhibitor of enkephalin-degrading enzymes, roles in pain and inflammation. Current Protein and Peptide Science 2002, 3 (6), 587-599.
    • (2002) Current Protein and Peptide Science , vol.3 , Issue.6 , pp. 587-599
    • Yamamoto, Y.1    Ono, H.2    Ueda, A.3    Shimamura, M.4    Nishimura, K.5    Hazato, T.6
  • 12
    • 34147123803 scopus 로고    scopus 로고
    • Food-derived peptides with biological activity, from research to food applications
    • Hartmann, R.; Meisel, H. Food-derived peptides with biological activity, from research to food applications. Current Opinion in Biotechnology 2007, 18 (2), 163-169.
    • (2007) Current Opinion in Biotechnology , vol.18 , Issue.2 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 13
    • 34548484135 scopus 로고    scopus 로고
    • Fractionation and identification of ACE-inhibitory peptides from -lactalbumin and β-casein produced by thermolysin-catalysed hydrolysis
    • Otte, J.; Shalaby, S.M.A.; Zakora, M.; Nielsen, M.S. Fractionation and identification of ACE-inhibitory peptides from -lactalbumin and β-casein produced by thermolysin-catalysed hydrolysis. International Dairy Journal 2007, 17, 1460-1472.
    • (2007) International Dairy Journal , vol.17 , pp. 1460-1472
    • Otte, J.1    Shalaby, S.M.A.2    Zakora, M.3    Nielsen, M.S.4
  • 14
    • 36749005569 scopus 로고    scopus 로고
    • Optimizing angiotensin-Iconverting enzyme inhibitory activity of Pacific hake (Merluccius productus) fillet hydrolysate using response surface methodology and ultrafiltration
    • Cinq-Mars, C.D.; Li-Chan, E.C.Y. Optimizing angiotensin-Iconverting enzyme inhibitory activity of Pacific hake (Merluccius productus) fillet hydrolysate using response surface methodology and ultrafiltration. Journal of Agricultural and Food Chemistry 2007, 55, 9380-9388.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 9380-9388
    • Cinq-Mars, C.D.1    Li-Chan, E.C.Y.2
  • 15
    • 58249134379 scopus 로고    scopus 로고
    • Optimisation of hydrolysis conditions for the production of the angiotensin-I converting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology
    • Guo, Y.; Pan, D.; Tanokura, M. Optimisation of hydrolysis conditions for the production of the angiotensin-I converting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology. Food Chemistry 2009, 114, 328-333.
    • (2009) Food Chemistry , vol.114 , pp. 328-333
    • Guo, Y.1    Pan, D.2    Tanokura, M.3
  • 16
    • 59649100770 scopus 로고    scopus 로고
    • Comparison of ACE inhibitory and DPPH radical scavenging activities of fish muscle hydrolysates
    • Nakajima, K.; Yoshie-Stark, Y.; Ogushi, M. Comparison of ACE inhibitory and DPPH radical scavenging activities of fish muscle hydrolysates. Food Chemistry 2009, 114, 844-851.
    • (2009) Food Chemistry , vol.114 , pp. 844-851
    • Nakajima, K.1    Yoshie-Stark, Y.2    Ogushi, M.3
  • 18
    • 80051558901 scopus 로고    scopus 로고
    • QSAR-aided in silico approach in evaluation of food proteins as precursors of ACE inhibitory peptides
    • Gu, Y.; Majumder, K.; Wu, J. QSAR-aided in silico approach in evaluation of food proteins as precursors of ACE inhibitory peptides. Food Research International 2011, 44, 2465-2474.
    • (2011) Food Research International , vol.44 , pp. 2465-2474
    • Gu, Y.1    Majumder, K.2    Wu, J.3
  • 19
    • 84860318855 scopus 로고    scopus 로고
    • Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach
    • Lacroix, I.M.E.; Li-Chan, E.C.Y. Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach. Journal of Functional Foods 2012, 4, 403-422.
    • (2012) Journal of Functional Foods , vol.4 , pp. 403-422
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 20
    • 0026644571 scopus 로고
    • Hormonal milieu affects tail flick latency in female rats and may be attenuated by access to sucrose
    • Frye, C.A.; Bock, B.C.; Kanarek, R.B. Hormonal milieu affects tail flick latency in female rats and may be attenuated by access to sucrose. Physiology and Behavior 1992, 52, 699-706.
    • (1992) Physiology and Behavior , vol.52 , pp. 699-706
    • Frye, C.A.1    Bock, B.C.2    Kanarek, R.B.3
  • 21
    • 0031020813 scopus 로고    scopus 로고
    • Suckling and sucrose ingestion suppress persistent hyperalgesia and spinal Fos expression after forepaw inflammation in infant rats
    • Ren, K.; Blass, E.M.; Zhou, Q.; Dubner, R. Suckling and sucrose ingestion suppress persistent hyperalgesia and spinal Fos expression after forepaw inflammation in infant rats. Proceedings of the National Academy of Science USA 1997, 94, 1471-1475.
    • (1997) Proceedings of the National Academy of Science USA , vol.94 , pp. 1471-1475
    • Ren, K.1    Blass, E.M.2    Zhou, Q.3    Dubner, R.4
  • 22
    • 0027500855 scopus 로고
    • Modulation of learning, pain thresholds, and thermoregulation in the rats by preparations of free purified alpha linolenic and linolenic acids, determination of their optimal ratio
    • Yehuda, S.; Carasso, R.L. Modulation of learning, pain thresholds, and thermoregulation in the rats by preparations of free purified alpha linolenic and linolenic acids, determination of their optimal ratio. Proceedings of the National Academy of Science USA 1993, 90, 10345-10349.
    • (1993) Proceedings of the National Academy of Science USA , vol.90 , pp. 10345-10349
    • Yehuda, S.1    Carasso, R.L.2
  • 23
    • 0028330851 scopus 로고
    • Cardiovascular and analgesic effects of a highly palatable diet in spontaneously hypertensive and Wistar-Kyoto rats
    • Zhang, T.; Reid, K.; Acuff, C.G. Cardiovascular and analgesic effects of a highly palatable diet in spontaneously hypertensive and Wistar-Kyoto rats. Pharmacology Biochemistry and Behavior Journal 1994, 48, 57-61.
    • (1994) Pharmacology Biochemistry and Behavior Journal , vol.48 , pp. 57-61
    • Zhang, T.1    Reid, K.2    Acuff, C.G.3
  • 24
    • 0020387132 scopus 로고    scopus 로고
    • Mood, performance, and pain sensitivity, changes induced by food constituents
    • Lieberman, H.R.; Corkin, S.; Spring, B.J. Mood, performance, and pain sensitivity, changes induced by food constituents. Journal of Psychiatric Research 17 (2), 135-145.
    • Journal of Psychiatric Research , vol.17 , Issue.2 , pp. 135-145
    • Lieberman, H.R.1    Corkin, S.2    Spring, B.J.3
  • 26
    • 0019962543 scopus 로고
    • Alteration of human pain thresholds by nutritional manipulation and L-tryptophan supplementation
    • Seltzer, S.; Stoch, R.; Marcus, R.; Jackson, E.J. Alteration of human pain thresholds by nutritional manipulation and L-tryptophan supplementation. Pain 1982, 13, 385-392.
    • (1982) Pain , vol.13 , pp. 385-392
    • Seltzer, S.1    Stoch, R.2    Marcus, R.3    Jackson, E.J.4
  • 27
    • 70349931376 scopus 로고    scopus 로고
    • Angiotensin-I converting enzyme inhibitory activity of hydrolysates from oat (Avena sativa) proteins by in silico and in vitro analyses
    • Cheung, I.W.Y.; Nakayama, S.; Hsu, M.N.K.; Samaranayaka, A.G.P.; Li-Chan, E.C.Y. Angiotensin-I converting enzyme inhibitory activity of hydrolysates from oat (Avena sativa) proteins by in silico and in vitro analyses. Journal of Agricultural and Food Chemistry 2009, 57, 9234-9242.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 9234-9242
    • Cheung, I.W.Y.1    Nakayama, S.2    Hsu, M.N.K.3    Samaranayaka, A.G.P.4    Li-Chan, E.C.Y.5
  • 29
    • 0037216795 scopus 로고    scopus 로고
    • Computer-aided characteristics of proteins as potential precursors of bioactive peptides
    • Dziuba, J.; Iwaniak, A.; Minkiewicz, P. Computer-aided characteristics of proteins as potential precursors of bioactive peptides. Polimery 2003, 48, 50-53.
    • (2003) Polimery , vol.48 , pp. 50-53
    • Dziuba, J.1    Iwaniak, A.2    Minkiewicz, P.3
  • 30
    • 0020465332 scopus 로고
    • Dipeptidylaminopeptidase-III of rat brain selective affinity for enkephalin and angiotensin
    • Lee, C.M.; Snyder, S.H. Dipeptidylaminopeptidase-III of rat brain selective affinity for enkephalin and angiotensin. Journal of Biological Chemistry 1982, 257, 12043-12050.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 12043-12050
    • Lee, C.M.1    Snyder, S.H.2
  • 32
    • 33847633060 scopus 로고    scopus 로고
    • Human dipeptidyl peptidase III acts as a post-proline-cleaving enzyme on endomorphins
    • Barsun, M.; Jajcanin, N.; Vukelic, B.; Spoljaric, J.; Abramic, M. Human dipeptidyl peptidase III acts as a post-proline-cleaving enzyme on endomorphins. Biological Chemistry 2007, 388, 343-348.
    • (2007) Biological Chemistry , vol.388 , pp. 343-348
    • Barsun, M.1    Jajcanin, N.2    Vukelic, B.3    Spoljaric, J.4    Abramic, M.5
  • 33
    • 0035076596 scopus 로고    scopus 로고
    • Soy-containing diet suppresses chronic neuropathic sensory disorders in rats
    • Shir, Y.; Sheth, R.; Campbell, J.N.; Raja, S.N.; Seltzer, Z. Soy-containing diet suppresses chronic neuropathic sensory disorders in rats. Anesthesia and Analgesia 2001, 92, 1029-1034.
    • (2001) Anesthesia and Analgesia , vol.92 , pp. 1029-1034
    • Shir, Y.1    Sheth, R.2    Campbell, J.N.3    Raja, S.N.4    Seltzer, Z.5
  • 36
    • 33645501006 scopus 로고    scopus 로고
    • New insights in biologically active proteins and peptides derived from hen egg
    • Mine, Y.; Kovacs-Nolan, J. New insights in biologically active proteins and peptides derived from hen egg. Worlds Poultry Science Journal 2006, 62, 87-96.
    • (2006) Worlds Poultry Science Journal , vol.62 , pp. 87-96
    • Mine, Y.1    Kovacs-Nolan, J.2
  • 37
    • 0030810645 scopus 로고    scopus 로고
    • Hemoglobin as a source of endogenous bioactive peptides, the concept of tissue specific peptide pool
    • Ivanov, V.T.; Karelin, A.A.; Philippova, M.M,;, Nazimov, I.V.; Pletnev, V.Z. Hemoglobin as a source of endogenous bioactive peptides, the concept of tissue specific peptide pool. Biopolymers 1997, 43 (2), 171-188.
    • (1997) Biopolymers , vol.43 , Issue.2 , pp. 171-188
    • Ivanov, V.T.1    Karelin, A.A.2    Philippova, M.M.3    Nazimov, I.V.4    Pletnev, V.Z.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.