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Volumn 13, Issue 8 B, 2009, Pages 2304-2316

Small-molecule peptides inhibit Z α1-antitrypsin polymerization

Author keywords

Antitrypsin; Cirrhosis; Combinatorial chemistry; Emphysema; Peptide; Polymerization; Surface plasmon resonance; Urea gel

Indexed keywords

ALPHA 1 ANTITRYPSIN; BIOPOLYMER; PEPTIDE;

EID: 72949086203     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1582-4934.2008.00608.x     Document Type: Article
Times cited : (34)

References (48)
  • 1
    • 0023898432 scopus 로고
    • Molecular basis of alpha-1-antitrypsin deficiency
    • Brantly M, Nukiwa T, Crystal RG. Molecular basis of alpha-1-antitrypsin deficiency. Am J Med. 1988 84 : 13 31.
    • (1988) Am J Med. , vol.84 , pp. 13-31
    • Brantly, M.1    Nukiwa, T.2    Crystal, R.G.3
  • 2
    • 0032085755 scopus 로고    scopus 로고
    • Alpha1-antitrypsin deficiency, cirrhosis and emphysema
    • Mahadeva R, Lomas DA. Alpha1-antitrypsin deficiency, cirrhosis and emphysema. Thorax. 1998 53 : 501 505.
    • (1998) Thorax. , vol.53 , pp. 501-505
    • Mahadeva, R.1    Lomas, D.A.2
  • 4
    • 0021747157 scopus 로고
    • 1-proteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model, and preliminary analysis of the implications for function
    • 1- proteinase inhibitor: crystal structure analysis of two crystal modifications, molecular model, and preliminary analysis of the implications for function. J Mol Biol. 1984 177 : 531 557.
    • (1984) J Mol Biol. , vol.177 , pp. 531-557
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3
  • 5
    • 0031036673 scopus 로고    scopus 로고
    • Major proteinase movement upon stable serpin-pro teinase complex formation
    • Stratikos E, Gettins PWG. Major proteinase movement upon stable serpin-pro teinase complex formation. Proc Natl Acad Sci USA. 1997 94 : 453 458.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 453-458
    • Stratikos, E.1    Gettins, P.W.G.2
  • 6
    • 0033608984 scopus 로고    scopus 로고
    • Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 Å and full insertion of the reactive center loop into β-Sheet A
    • Stratikos E, Gettins PWG. Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 Å and full insertion of the reactive center loop into β-Sheet A. Proc Natl Acad Sci USA. 1999 96 : 4808 4813.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4808-4813
    • Stratikos, E.1    Gettins, P.W.G.2
  • 7
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington JA, Read RJ, Carrell RW. Structure of a serpin-protease complex shows inhibition by deformation. Nature. 2000 407 : 923 926.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 8
    • 0037011795 scopus 로고    scopus 로고
    • 1-Antitrypsin deficiency - A model for conformational diseases
    • 1-Antitrypsin deficiency - A model for conformational diseases. N Eng J Med. 2002 346 : 45 53.
    • (2002) N Eng J Med. , vol.346 , pp. 45-53
    • Lomas, D.A.1    Carrell, R.W.2
  • 10
    • 0026755363 scopus 로고
    • The mechanism of Z alpha1-antitrypsin accumulation in the liver
    • Lomas DA, Evans DL, Finch JT, et al. The mechanism of Z alpha1-antitrypsin accumulation in the liver. Nature. 1992 357 : 605 607.
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3
  • 13
    • 0015496403 scopus 로고
    • Alpha1 antitrypsin in the livers of patients with emphysema
    • Lieberman J, Mittman C, Gordon HW. Alpha1 antitrypsin in the livers of patients with emphysema. Science. 1972 175 : 63 5.
    • (1972) Science , vol.175 , pp. 63-5
    • Lieberman, J.1    Mittman, C.2    Gordon, H.W.3
  • 15
    • 2442488539 scopus 로고    scopus 로고
    • 1-Antitrypsin polymerizes in the lung and acts as a neutrophil chemoattractant
    • 1- Antitrypsin polymerizes in the lung and acts as a neutrophil chemoattractant. Chest. 2004 125 : 1952 1957.
    • (2004) Chest. , vol.125 , pp. 1952-1957
    • Mulgrew, A.T.1    Taggart, C.C.2    Lawless, M.W.3
  • 16
    • 19944430698 scopus 로고    scopus 로고
    • 1-antitrypsin co-localize with neutrophils in emphysematous alveoli and are chemotactic in vivo
    • 1- antitrypsin co-localize with neutrophils in emphysematous alveoli and are chemotactic in vivo. Am J Pathol. 2005 166 : 377 386.
    • (2005) Am J Pathol. , vol.166 , pp. 377-386
    • Mahadeva, R.1    Atkinson, C.2    Li, Z.3
  • 17
    • 20744450475 scopus 로고    scopus 로고
    • Alpha1-antitrypsin deficiency
    • Stoller JK, Aboussouan LS. Alpha1-antitrypsin deficiency. Lancet. 2005 365 : 2225 2236.
    • (2005) Lancet , vol.365 , pp. 2225-2236
    • Stoller, J.K.1    Aboussouan, L.S.2
  • 18
    • 0036789017 scopus 로고    scopus 로고
    • Serpinopathies and the conformational dementias
    • Lomas DA, Carrell RW. Serpinopathies and the conformational dementias. Nat Rev Genet. 2002 3 : 759 768.
    • (2002) Nat Rev Genet. , vol.3 , pp. 759-768
    • Lomas, D.A.1    Carrell, R.W.2
  • 19
    • 0034721790 scopus 로고    scopus 로고
    • 1-antitrypsin polymers are formed by reactive loop beta-sheet A linkage
    • 1-antitrypsin polymers are formed by reactive loop beta-sheet A linkage. J Biol Chem. 2000 275 : 33663 33668.
    • (2000) J Biol Chem. , vol.275 , pp. 33663-33668
    • Sivasothy, P.1    Dafforn, T.R.2    Gettins, P.G.W.3
  • 20
    • 0025226070 scopus 로고
    • Structural transition of alpha1-antitrypsin by a peptide sequentially similar to beta-strand s4A
    • Schulze AJ, Baumann U, Knof S, et al. Structural transition of alpha1-antitrypsin by a peptide sequentially similar to beta-strand s4A. Eur J Biochem. 1990 194 : 51 6.
    • (1990) Eur J Biochem. , vol.194 , pp. 51-6
    • Schulze, A.J.1    Baumann, U.2    Knof, S.3
  • 21
    • 0026701963 scopus 로고
    • Kinetic characterization of the substrate reaction between a complex of antithrombin with a synthetic reactive-bond loop tetradecapeptide and four target proteinases of the inhibitor
    • Björk I, Nordling K, Larsson I, et al. Kinetic characterization of the substrate reaction between a complex of antithrombin with a synthetic reactive-bond loop tetradecapeptide and four target proteinases of the inhibitor. J Biol Chem. 1992 267 : 19047 19050.
    • (1992) J Biol Chem. , vol.267 , pp. 19047-19050
    • Björk, I.1    Nordling, K.2    Larsson, I.3
  • 22
    • 0029866947 scopus 로고    scopus 로고
    • Probing serpin reactive loop conformations by proteolytic cleavage
    • Chang WSW, Wardell MR, Lomas DA, et al. Probing serpin reactive loop conformations by proteolytic cleavage. Biochem J. 1996 314 : 647 653.
    • (1996) Biochem J. , vol.314 , pp. 647-653
    • Chang, W.S.W.1    Wardell, M.R.2    Lomas, D.A.3
  • 23
    • 0030819064 scopus 로고    scopus 로고
    • Mechanisms of antithrombin polymerisation and heparin activation probed by insertion of synthetic reactive loop peptides
    • Fitton HL, Pike RN, Carrell RW, et al. Mechanisms of antithrombin polymerisation and heparin activation probed by insertion of synthetic reactive loop peptides. Biol Chem. 1997 378 : 1059 1063.
    • (1997) Biol Chem. , vol.378 , pp. 1059-1063
    • Fitton, H.L.1    Pike, R.N.2    Carrell, R.W.3
  • 24
    • 0032538299 scopus 로고    scopus 로고
    • Implications for function and therapy of a 2.9 Å structure of binary-complexed antithrombin
    • Skinner R, Chang WSW, Jin L, et al. Implications for function and therapy of a 2.9 Å structure of binary-complexed antithrombin. J Mol Biol. 1998 283 : 9 14.
    • (1998) J Mol Biol. , vol.283 , pp. 9-14
    • Skinner, R.1    Chang, W.S.W.2    Jin, L.3
  • 26
    • 4444332086 scopus 로고    scopus 로고
    • How small peptides block and reverse serpin polymerization
    • Zhou A, Stein PE, Huntington JA, et al. How small peptides block and reverse serpin polymerization. J Mol Biol. 2004 342 : 931 941.
    • (2004) J Mol Biol. , vol.342 , pp. 931-941
    • Zhou, A.1    Stein, P.E.2    Huntington, J.A.3
  • 27
    • 34247626017 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopic study of serpin depolymerization by computationally designed peptides
    • Chowdhury P, Wang W, Lavender S, et al. Fluorescence correlation spectroscopic study of serpin depolymerization by computationally designed peptides. J Mol Biol. 2007 369 : 462 473.
    • (2007) J Mol Biol. , vol.369 , pp. 462-473
    • Chowdhury, P.1    Wang, W.2    Lavender, S.3
  • 28
    • 0037366605 scopus 로고    scopus 로고
    • The combinatorial synthesis of bicyclic privileged structures or privileged substructures
    • Horton DA, Bourne GT, Smythe ML. The combinatorial synthesis of bicyclic privileged structures or privileged substructures. Chem Rev. 2003 103 : 893 930.
    • (2003) Chem Rev. , vol.103 , pp. 893-930
    • Horton, D.A.1    Bourne, G.T.2    Smythe, M.L.3
  • 29
    • 0032807739 scopus 로고    scopus 로고
    • Combinatorial approaches to materials design
    • McFarland EW, Weinberg WH. Combinatorial approaches to materials design. TIBTECH. 1999 17 : 107 115.
    • (1999) TIBTECH. , vol.17 , pp. 107-115
    • McFarland, E.W.1    Weinberg, W.H.2
  • 30
    • 33750449952 scopus 로고    scopus 로고
    • A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide
    • Kim W, Kim Y, Min J, et al. A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide. ACS Chem Biol. 2006 1 : 461 469.
    • (2006) ACS Chem Biol. , vol.1 , pp. 461-469
    • Kim, W.1    Kim, Y.2    Min, J.3
  • 32
    • 0036007197 scopus 로고    scopus 로고
    • Combinatorial chemistry: 20 years on
    • Furka Á. Combinatorial chemistry: 20 years on. Drug Discov Today. 2002 7 : 1 7.
    • (2002) Drug Discov Today. , vol.7 , pp. 1-7
    • Furka, Á.1
  • 35
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou PY, Fasman GD. Empirical predictions of protein conformation. Annu Rev Biochem. 1978 47 : 251 276.
    • (1978) Annu Rev Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 36
    • 0028577207 scopus 로고
    • An all D-amino acid opioid peptide with central analgesic activity from a combinatorial library
    • Dooley CT, Chung NN, Wilkes BC, et al. An all D-amino acid opioid peptide with central analgesic activity from a combinatorial library. Science. 1994 266 : 2019 2022.
    • (1994) Science , vol.266 , pp. 2019-2022
    • Dooley, C.T.1    Chung, N.N.2    Wilkes, B.C.3
  • 37
    • 0031573094 scopus 로고    scopus 로고
    • Tight-binding streptavidin ligands from a cyclic peptide library
    • Yu Z, Tu J, Chu YH. Tight-binding streptavidin ligands from a cyclic peptide library. Anal Chem. 1997 69 : 4515 4518.
    • (1997) Anal Chem. , vol.69 , pp. 4515-4518
    • Yu, Z.1    Tu, J.2    Chu, Y.H.3
  • 38
    • 0042121237 scopus 로고    scopus 로고
    • Multiple sequence alignment with the Clustal series of programs
    • Chenna R, Sugawara H, Koike T, et al. Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res. 2003 31 : 3497 3500.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3497-3500
    • Chenna, R.1    Sugawara, H.2    Koike, T.3
  • 39
    • 33845931650 scopus 로고    scopus 로고
    • Survey of the year 2005 commercial optical biosensor literature
    • Rich RL, Myszka DG. Survey of the year 2005 commercial optical biosensor literature. J Mol Recognit. 2006 19 : 478 534.
    • (2006) J Mol Recognit. , vol.19 , pp. 478-534
    • Rich, R.L.1    Myszka, D.G.2
  • 40
    • 15544374363 scopus 로고    scopus 로고
    • Using surface plasmon resonance to directly determine binding affinities of combinatorially selected cyclopeptides and their linear analogs to a streptavidin chip
    • Chang YP, Chu YH. Using surface plasmon resonance to directly determine binding affinities of combinatorially selected cyclopeptides and their linear analogs to a streptavidin chip. Anal Biochem. 2005 340 : 74 9.
    • (2005) Anal Biochem. , vol.340 , pp. 74-9
    • Chang, Y.P.1    Chu, Y.H.2
  • 41
    • 33750614316 scopus 로고    scopus 로고
    • Using surface plasmon resonance to directly measure slow binding of low-molecular mass inhibitors to a VanX chip
    • Chang YP, Tseng MJ, Chu YH. Using surface plasmon resonance to directly measure slow binding of low-molecular mass inhibitors to a VanX chip. Anal Biochem. 2006 359 : 63 71.
    • (2006) Anal Biochem. , vol.359 , pp. 63-71
    • Chang, Y.P.1    Tseng, M.J.2    Chu, Y.H.3
  • 42
    • 35848929750 scopus 로고    scopus 로고
    • 1- antitrypsin and increase the clearance of intracellular aggregates
    • 1-antitrypsin and increase the clearance of intracellular aggregates. J Med Chem. 2007 50 : 5357 5363.
    • (2007) J Med Chem. , vol.50 , pp. 5357-5363
    • Mallya, M.1    Phillips, R.L.2    Saldanha, S.A.3
  • 43
    • 0022591495 scopus 로고
    • The classification of amino acid conservation
    • Taylor WR. The classification of amino acid conservation. J Theor Biol. 1986 119 : 205 218.
    • (1986) J Theor Biol. , vol.119 , pp. 205-218
    • Taylor, W.R.1
  • 44
    • 3342889562 scopus 로고    scopus 로고
    • Different conformational changes within the F-Helix occur during serpin folding, polymerization, and proteinase inhibition
    • Cabrita LD, Dai W, Bottomley SP. Different conformational changes within the F-Helix occur during serpin folding, polymerization, and proteinase inhibition. Biochemistry. 2004 43 : 9834 9839.
    • (2004) Biochemistry. , vol.43 , pp. 9834-9839
    • Cabrita, L.D.1    Dai, W.2    Bottomley, S.P.3
  • 45
    • 0034976979 scopus 로고    scopus 로고
    • 1-antitrypsin that play structural and functional roles
    • 1- antitrypsin that play structural and functional roles. Protein Sci. 2001 10 : 1446 1453.
    • (2001) Protein Sci. , vol.10 , pp. 1446-1453
    • Lee, C.1    Maeng, J.S.2    Kocher, J.P.3
  • 46
    • 0036433482 scopus 로고    scopus 로고
    • 1- antitrypsin deficiency
    • 1-antitrypsin deficiency. Chest. 2002 122 : 1818 1829.
    • (2002) Chest. , vol.122 , pp. 1818-1829
    • De Serres, F.J.1
  • 47
    • 0038216603 scopus 로고    scopus 로고
    • Augmentation therapy with alpha1-antitrypsin: Patterns of use and adverse events
    • Stoller JK, Fallat R, Schluchter MD, et al. Augmentation therapy with alpha1-antitrypsin: patterns of use and adverse events. Chest. 2003 123 : 1425 1434.
    • (2003) Chest. , vol.123 , pp. 1425-1434
    • Stoller, J.K.1    Fallat, R.2    Schluchter, M.D.3
  • 48
    • 0037952677 scopus 로고    scopus 로고
    • Cost-effectiveness analysis of augmentation therapy for severe alpha1-antitrypsin deficiency
    • Gildea TR, Shermock KM, Singer ME, et al. Cost-effectiveness analysis of augmentation therapy for severe alpha1-antitrypsin deficiency. Am J Respir Crit Care Med. 2003 167 : 1387 1392.
    • (2003) Am J Respir Crit Care Med. , vol.167 , pp. 1387-1392
    • Gildea, T.R.1    Shermock, K.M.2    Singer, M.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.