메뉴 건너뛰기




Volumn 6, Issue 8, 2015, Pages 1309-1316

Novel Hexapeptide Interacts with Tubulin and Microtubules, Inhibits Aβ Fibrillation, and Shows Significant Neuroprotection

Author keywords

A 42 peptide; microtubule; neuroprotective peptide; PC12 cell; tubulin

Indexed keywords

AMYLOID BETA PROTEIN; ASPARAGINYLALANYLVALYSERYLISOLEUCYLGLUTAMINE; BETA TUBULIN; HEXAPEPTIDE; NERVE GROWTH FACTOR; NEUROPROTECTIVE AGENT; PACLITAXEL; TUBULIN; UNCLASSIFIED DRUG; AMYLOID BETA-PROTEIN (1-42); ASN-ALA-VAL-SER-ILE-GLN; OLIGOPEPTIDE; PEPTIDE FRAGMENT;

EID: 84939803447     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/acschemneuro.5b00149     Document Type: Article
Times cited : (27)

References (29)
  • 1
    • 84927173786 scopus 로고    scopus 로고
    • The clocks that time us-circadian rhythms in neurodegenerative disorders
    • Videnovic, A., Lazar, A. S., Barker, R. A., and Overeem, S. (2014) The clocks that time us-circadian rhythms in neurodegenerative disorders Nat. Rev. Neurol. 10, 683-693 10.1038/nrneurol.2014.206
    • (2014) Nat. Rev. Neurol. , vol.10 , pp. 683-693
    • Videnovic, A.1    Lazar, A.S.2    Barker, R.A.3    Overeem, S.4
  • 2
    • 0025779179 scopus 로고
    • Solution structures of beta peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow, C. J. and Zagorski, M. G. (1991) Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition Science 253, 179-182 10.1126/science.1853202
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 4
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • LaFerla, F. M., Green, K. N., and Oddo, S. (2007) Intracellular amyloid-beta in Alzheimer's disease Nat. Rev. Neurosci. 8, 499-509 10.1038/nrn2168
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 5
    • 79955592308 scopus 로고    scopus 로고
    • Alzheimer Aβ disrupts the mitotic spindle and directly inhibits mitotic microtubule motors
    • Borysov, S. I., Granic, A., Padmanabhan, J., Walczak, C. E., and Potter, H. (2011) Alzheimer Aβ disrupts the mitotic spindle and directly inhibits mitotic microtubule motors Cell Cycle 10, 1397-1410 10.4161/cc.10.9.15478
    • (2011) Cell Cycle , vol.10 , pp. 1397-1410
    • Borysov, S.I.1    Granic, A.2    Padmanabhan, J.3    Walczak, C.E.4    Potter, H.5
  • 6
    • 84921853164 scopus 로고    scopus 로고
    • Interaction of Aβ peptide with tubulin causes an inhibition of tubulin polymerization and the apoptotic death of cancer cells
    • Saha, A., Mohapatra, S., Kurkute, P., Jana, B., Mondal, P., Bhunia, D., Ghosh, S., and Ghosh, S. (2015) Interaction of Aβ peptide with tubulin causes an inhibition of tubulin polymerization and the apoptotic death of cancer cells Chem. Commun. 51, 2249-2252 10.1039/C4CC09390A
    • (2015) Chem. Commun. , vol.51 , pp. 2249-2252
    • Saha, A.1    Mohapatra, S.2    Kurkute, P.3    Jana, B.4    Mondal, P.5    Bhunia, D.6    Ghosh, S.7    Ghosh, S.8
  • 7
    • 5144220474 scopus 로고    scopus 로고
    • Efficient reversal of Alzheimer's disease fibril formation and elimination of neurotoxicity by a small molecule
    • Blanchard, B. J., Chen, A., Rozeboom, L. M., Stafford, K. A., Weigele, P., and Ingram, V. M. (2004) Efficient reversal of Alzheimer's disease fibril formation and elimination of neurotoxicity by a small molecule Proc. Natl. Acad. Sci. U. S. A. 101, 14326-14332 10.1073/pnas.0405941101
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 14326-14332
    • Blanchard, B.J.1    Chen, A.2    Rozeboom, L.M.3    Stafford, K.A.4    Weigele, P.5    Ingram, V.M.6
  • 8
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo, A. and Yankner, B. A. (1994) Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red Proc. Natl. Acad. Sci. U. S. A. 91, 12243-12247 10.1073/pnas.91.25.12243
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 9
    • 3042547187 scopus 로고    scopus 로고
    • The Flavonoid Baicalein Inhibits Fibrillation of α-Synuclein and Disaggregates Existing Fibrils
    • Zhu, M., Rajamani, S., Kaylor, J., Han, S., Zhou, F., and Fink, A. L. (2004) The Flavonoid Baicalein Inhibits Fibrillation of α-Synuclein and Disaggregates Existing Fibrils J. Biol. Chem. 279, 26846-26857 10.1074/jbc.M403129200
    • (2004) J. Biol. Chem. , vol.279 , pp. 26846-26857
    • Zhu, M.1    Rajamani, S.2    Kaylor, J.3    Han, S.4    Zhou, F.5    Fink, A.L.6
  • 10
    • 0034612220 scopus 로고    scopus 로고
    • Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: Implications for Huntington's disease therapy
    • Heiser, V., Scherzinger, E., Boeddrich, A., Nordhoff, E., Lurz, R., Schugardt, N., Lehrach, H., and Wanker, E. E. (2000) Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: Implications for Huntington's disease therapy Proc. Natl. Acad. Sci. U. S. A. 97, 6739-6744 10.1073/pnas.110138997
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6739-6744
    • Heiser, V.1    Scherzinger, E.2    Boeddrich, A.3    Nordhoff, E.4    Lurz, R.5    Schugardt, N.6    Lehrach, H.7    Wanker, E.E.8
  • 11
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • McGovern, S. L., Caselli, E., Grigorieff, N., and Shoichet, B. K. (2002) A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening J. Med. Chem. 45, 1712-1722 10.1021/jm010533y
    • (2002) J. Med. Chem. , vol.45 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 12
    • 84877914479 scopus 로고    scopus 로고
    • NAP (davunetide) modifies disease progression in a mouse model of severe neurodegeneration: Protection against impairments in axonal transport
    • Jouroukhin, Y., Ostritsky, R., Assaf, Y., Pelled, G., Giladi, E., and Gozes, I. (2013) NAP (davunetide) modifies disease progression in a mouse model of severe neurodegeneration: protection against impairments in axonal transport Neurobiol. Dis. 56, 79-94 10.1016/j.nbd.2013.04.012
    • (2013) Neurobiol. Dis. , vol.56 , pp. 79-94
    • Jouroukhin, Y.1    Ostritsky, R.2    Assaf, Y.3    Pelled, G.4    Giladi, E.5    Gozes, I.6
  • 13
    • 84893904672 scopus 로고    scopus 로고
    • An amyloid inhibitor octapeptide forms amyloid type fibrous aggregates and affects microtubule motility
    • Biswas, A., Kurkute, P., Jana, B., Laskar, A., and Ghosh, S. (2014) An amyloid inhibitor octapeptide forms amyloid type fibrous aggregates and affects microtubule motility Chem. Commun. 50, 2604-2607 10.1039/c3cc49396b
    • (2014) Chem. Commun. , vol.50 , pp. 2604-2607
    • Biswas, A.1    Kurkute, P.2    Jana, B.3    Laskar, A.4    Ghosh, S.5
  • 16
    • 0021950830 scopus 로고
    • 4′,6-Diamidino-2-phenylindole, a fluorescent probe for tubulin and microtubules
    • Bonne, D., Heusele, C., Simon, C., and Pantaloni, D. (1984) 4′,6-Diamidino-2-phenylindole, a fluorescent probe for tubulin and microtubules J. Biol. Chem. 260, 2819-2825
    • (1984) J. Biol. Chem. , vol.260 , pp. 2819-2825
    • Bonne, D.1    Heusele, C.2    Simon, C.3    Pantaloni, D.4
  • 17
    • 0029874514 scopus 로고    scopus 로고
    • Mechanism of Action of Cryptophycin
    • Smith, C. D. and Zhang, X. (1996) Mechanism of Action of Cryptophycin J. Biol. Chem. 271, 6192-6198 10.1074/jbc.271.11.6192
    • (1996) J. Biol. Chem. , vol.271 , pp. 6192-6198
    • Smith, C.D.1    Zhang, X.2
  • 18
    • 84902250711 scopus 로고    scopus 로고
    • Targeting cytotoxicity and tubulin polymerization by metal-carbene complexes on a purine tautomer platform
    • Khanna, S., Jana, B., Saha, A., Kurkute, P., Ghosh, S., and Verma, S. (2014) Targeting cytotoxicity and tubulin polymerization by metal-carbene complexes on a purine tautomer platform Dalton Trans. 43, 9838-9842 10.1039/c4dt00529e
    • (2014) Dalton Trans. , vol.43 , pp. 9838-9842
    • Khanna, S.1    Jana, B.2    Saha, A.3    Kurkute, P.4    Ghosh, S.5    Verma, S.6
  • 20
    • 0036438914 scopus 로고    scopus 로고
    • Solution structure of the Alzheimer amyloid b-peptide (1-42) in an apolar microenvironment
    • Crescenzi, O., Tomaselli, S., Guerrini, R., Salvadori, S., D'Ursi, A. M., Temussi, P. A., and Picone, D. (2002) Solution structure of the alzheimer amyloid b-peptide (1-42) in an apolar microenvironment Eur. J. Biochem. 269, 5642-5648 10.1046/j.1432-1033.2002.03271.x
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5642-5648
    • Crescenzi, O.1    Tomaselli, S.2    Guerrini, R.3    Salvadori, S.4    D'Ursi, A.M.5    Temussi, P.A.6    Picone, D.7
  • 21
    • 0035902507 scopus 로고    scopus 로고
    • Inhibition of beta-Amyloid (40) Fibrillogenesis and disassembly of beta-amyloid (40) fibrils by short beta-amyloid congeners containing N-methyl amino acids at alternate residues
    • Gordon, D. J., Sciarretta, K. L., and Meredith, S. C. (2001) Inhibition of beta-Amyloid (40) Fibrillogenesis and disassembly of beta-amyloid (40) fibrils by short beta-amyloid congeners containing N-methyl amino acids at alternate residues Biochemistry 40, 8237-8245 10.1021/bi002416v
    • (2001) Biochemistry , vol.40 , pp. 8237-8245
    • Gordon, D.J.1    Sciarretta, K.L.2    Meredith, S.C.3
  • 22
    • 3442899664 scopus 로고    scopus 로고
    • β-Sheet Breakers for Alzheimer's Disease Therapy
    • Bieler, S. and Soto, C. (2004) β-Sheet Breakers for Alzheimer's Disease Therapy Curr. Drug Targets 5, 553-558 10.2174/1389450043345290
    • (2004) Curr. Drug Targets , vol.5 , pp. 553-558
    • Bieler, S.1    Soto, C.2
  • 24
    • 84892948998 scopus 로고    scopus 로고
    • Efficacy of cyclin dependent kinase 4 inhibitors as potent neuroprotective agents against insults relevant to Alzheimer's disease
    • Sanphui, P., Pramanik, S. K., Chatterjee, N., Moorthi, P., Banerji, B., and Biswas, S. C. (2013) Efficacy of cyclin dependent kinase 4 inhibitors as potent neuroprotective agents against insults relevant to Alzheimer's disease PLoS One 8, e78842 10.1371/journal.pone.0078842
    • (2013) PLoS One , vol.8 , pp. 78842
    • Sanphui, P.1    Pramanik, S.K.2    Chatterjee, N.3    Moorthi, P.4    Banerji, B.5    Biswas, S.C.6
  • 26
    • 84878796119 scopus 로고    scopus 로고
    • Nerve growth factor and Alzheimer's disease: New facts for an old hypothesis
    • Cattaneo, A. and Calissano, P. (2012) Nerve growth factor and Alzheimer's disease: new facts for an old hypothesis Mol. Neurobiol. 46, 588-604 10.1007/s12035-012-8310-9
    • (2012) Mol. Neurobiol. , vol.46 , pp. 588-604
    • Cattaneo, A.1    Calissano, P.2
  • 27
    • 0345704610 scopus 로고
    • Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Greene, L. A. and Tischler, A. S. (1976) Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor Proc. Natl. Acad. Sci. U. S. A. 73, 2424-2428 10.1073/pnas.73.7.2424
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2424-2428
    • Greene, L.A.1    Tischler, A.S.2
  • 28
    • 0037147122 scopus 로고    scopus 로고
    • Nerve growth factor (NGF) down-regulates the Bcl-2 homology 3 (BH3) domain-only protein Bim and suppresses its proapoptotic activity by phosphorylation
    • Biswas, S. C. and Greene, L. A. (2002) Nerve growth factor (NGF) down-regulates the Bcl-2 homology 3 (BH3) domain-only protein Bim and suppresses its proapoptotic activity by phosphorylation J. Biol. Chem. 277, 49511-49516 10.1074/jbc.M208086200
    • (2002) J. Biol. Chem. , vol.277 , pp. 49511-49516
    • Biswas, S.C.1    Greene, L.A.2
  • 29
    • 0034954603 scopus 로고    scopus 로고
    • The MLK family mediates c-Jun N-terminal kinase activation in neuronal apoptosis
    • Xu, Z., Maroney, A. C., Dobrzanski, P., Kukekov, N. V., and Greene, L. A. (2001) The MLK family mediates c-Jun N-terminal kinase activation in neuronal apoptosis Mol. Cell. Biol. 21, 4713-4724 10.1128/MCB.21.14.4713-4724.2001
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4713-4724
    • Xu, Z.1    Maroney, A.C.2    Dobrzanski, P.3    Kukekov, N.V.4    Greene, L.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.