{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,17]],"date-time":"2026-01-17T20:51:25Z","timestamp":1768683085285,"version":"3.49.0"},"reference-count":41,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2009,7,1]],"date-time":"2009-07-01T00:00:00Z","timestamp":1246406400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Peptides"],"published-print":{"date-parts":[[2009,7]]},"DOI":"10.1016\/j.peptides.2009.04.012","type":"journal-article","created":{"date-parts":[[2009,5,5]],"date-time":"2009-05-05T08:54:48Z","timestamp":1241513688000},"page":"1282-1287","source":"Crossref","is-referenced-by-count":10,"title":["Hybrid peptides attenuate cytotoxicity of \u03b2-amyloid by inhibiting its oligomerization: Implication from solvent effects"],"prefix":"10.1016","volume":"30","author":[{"given":"Xun","family":"Sun","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wei-hui","family":"Wu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qian","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mei-sha","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ye-ping","family":"Yu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ying","family":"Ma","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yu-fen","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yan-mei","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.peptides.2009.04.012_bib1","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/S0140-6736(06)69113-7","article-title":"Alzheimer's disease","volume":"368","author":"Blennow","year":"2006","journal-title":"Lancet"},{"key":"10.1016\/j.peptides.2009.04.012_bib2","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1073\/pnas.87.1.167","article-title":"Surface tension measurements show that chaotropic salting-in denaturants are not just water-structure breakers","volume":"87","author":"Breslow","year":"1990","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.peptides.2009.04.012_bib3","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1017\/S0033583597003363","article-title":"The Hofmeister series: salt and solvent effects on interfacial phenomena","volume":"30","author":"Cacace","year":"1997","journal-title":"Q Rev Biophys"},{"key":"10.1016\/j.peptides.2009.04.012_bib4","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1038\/nsmb1345","article-title":"Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid","volume":"14","author":"Chimon","year":"2007","journal-title":"Nat Struct Mol Biol"},{"key":"10.1016\/j.peptides.2009.04.012_bib5","doi-asserted-by":"crossref","first-page":"5012","DOI":"10.1111\/j.1742-4658.2007.06018.x","article-title":"Phosphorylation modulates the local conformation and self-aggregation ability of a peptide from the fourth tau microtubule-binding repeat","volume":"274","author":"Du","year":"2007","journal-title":"FEBS J"},{"key":"10.1016\/j.peptides.2009.04.012_bib6","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1007\/BF00652352","article-title":"Dynamic surface-tension of micellar solutions studied by the maximum bubble pressure method. 3. Theory of the solutions containing micelles","volume":"273","author":"Dushkin","year":"1995","journal-title":"Colloid Polym Sci"},{"key":"10.1016\/j.peptides.2009.04.012_bib7","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1038\/nsmb.1437","article-title":"EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers","volume":"15","author":"Ehrnhoefer","year":"2008","journal-title":"Nat Struct Mol Biol"},{"key":"10.1016\/j.peptides.2009.04.012_bib8","doi-asserted-by":"crossref","first-page":"1122","DOI":"10.1126\/science.2111583","article-title":"Cleavage of amyloid beta peptide during constitutive processing of its precursor","volume":"248","author":"Esch","year":"1990","journal-title":"Science"},{"key":"10.1016\/j.peptides.2009.04.012_bib9","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1111\/j.1399-3011.1990.tb00939.x","article-title":"Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids","volume":"35","author":"Fields","year":"1990","journal-title":"Int J Pept Protein Res"},{"key":"10.1016\/j.peptides.2009.04.012_bib10","doi-asserted-by":"crossref","first-page":"8898","DOI":"10.1021\/bi050225s","article-title":"Design of peptidyl compounds that affect beta-amyloid aggregation: importance of surface tension and context","volume":"44","author":"Gibson","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2009.04.012_bib11","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1126\/science.1072994","article-title":"Medicine\u2014the amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics","volume":"297","author":"Hardy","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.peptides.2009.04.012_bib12","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1146\/annurev.biochem.66.1.385","article-title":"Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins","volume":"66","author":"Harper","year":"1997","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.peptides.2009.04.012_bib13","doi-asserted-by":"crossref","first-page":"5099","DOI":"10.1073\/pnas.0711731105","article-title":"Stabilization of a beta-hairpin in monomeric Alzheimer's amyloid-beta peptide inhibits amyloid formation","volume":"105","author":"Hoyer","year":"2008","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.peptides.2009.04.012_bib14","doi-asserted-by":"crossref","first-page":"27916","DOI":"10.1074\/jbc.M602061200","article-title":"Acceleration of amyloid beta-peptide aggregation by physiological concentrations of calcium","volume":"281","author":"Isaacs","year":"2006","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2009.04.012_bib15","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/0014-5793(94)01137-0","article-title":"Increased beta-amyloid release and levels of amyloid precursor protein (APP) in fibroblast cell lines from family members with the Swedish Alzheimer's disease APP670\/671 mutation","volume":"354","author":"Johnston","year":"1994","journal-title":"FEBS Lett"},{"key":"10.1016\/j.peptides.2009.04.012_bib16","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1038\/325733a0","article-title":"The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor","volume":"325","author":"Kang","year":"1987","journal-title":"Nature"},{"key":"10.1016\/j.peptides.2009.04.012_bib17","doi-asserted-by":"crossref","first-page":"50310","DOI":"10.1074\/jbc.M405600200","article-title":"Amyloid beta-induced changes in nitric oxide production and mitochondrial activity lead to apoptosis","volume":"279","author":"Keil","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2009.04.012_bib18","doi-asserted-by":"crossref","first-page":"40730","DOI":"10.1074\/jbc.M305466200","article-title":"Targeted control of kinetics of beta-amyloid self-association by surface tension-modifying peptides","volume":"278","author":"Kim","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2009.04.012_bib19","doi-asserted-by":"crossref","first-page":"15178","DOI":"10.1021\/bi00254a029","article-title":"Contribution of the surface free energy perturbation to protein\u2013solvent interactions","volume":"33","author":"Kita","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2009.04.012_bib20","doi-asserted-by":"crossref","first-page":"9989","DOI":"10.1073\/pnas.96.18.9989","article-title":"Amyloid diseases: abnormal protein aggregation in neurodegeneration","volume":"96","author":"Koo","year":"1999","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.peptides.2009.04.012_bib21","doi-asserted-by":"crossref","first-page":"10191","DOI":"10.1523\/JNEUROSCI.3432-04.2004","article-title":"Synaptic targeting by Alzheimer's-related amyloid beta oligomers","volume":"24","author":"Lacor","year":"2004","journal-title":"J Neurosci"},{"key":"10.1016\/j.peptides.2009.04.012_bib22","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1038\/nature05290","article-title":"A century-old debate on protein aggregation and neurodegeneration enters the clinic","volume":"443","author":"Lansbury","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.peptides.2009.04.012_bib23","doi-asserted-by":"crossref","first-page":"3342","DOI":"10.1073\/pnas.96.7.3342","article-title":"Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease","volume":"96","author":"Lansbury","year":"1999","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.peptides.2009.04.012_bib24","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1038\/nature04533","article-title":"A specific amyloid-beta protein assembly in the brain impairs memory","volume":"440","author":"Lesne","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.peptides.2009.04.012_bib25","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1046\/j.1471-4159.1997.69020581.x","article-title":"Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction","volume":"69","author":"Liu","year":"1997","journal-title":"J Neurochem"},{"key":"10.1016\/j.peptides.2009.04.012_bib26","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1073\/pnas.93.3.1125","article-title":"On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants","volume":"93","author":"Lomakin","year":"1996","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.peptides.2009.04.012_bib27","doi-asserted-by":"crossref","first-page":"7882","DOI":"10.1021\/bi002734u","article-title":"Structure\u2013function relationships for inhibitors of beta-amyloid toxicity containing the recognition sequence KLVFF","volume":"40","author":"Lowe","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2009.04.012_bib28","doi-asserted-by":"crossref","first-page":"4245","DOI":"10.1073\/pnas.82.12.4245","article-title":"Amyloid plaque core protein in Alzheimer disease and Down syndrome","volume":"82","author":"Masters","year":"1985","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.peptides.2009.04.012_bib29","doi-asserted-by":"crossref","first-page":"4282","DOI":"10.1021\/ja067367+","article-title":"Understanding the molecular basis for the inhibition of the Alzheimer's A beta-peptide oligomerization by human serum albumin using saturation transfer difference and off-resonance relaxation NMR spectroscopy","volume":"129","author":"Milojevic","year":"2007","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.peptides.2009.04.012_bib30","doi-asserted-by":"crossref","first-page":"1951","DOI":"10.1084\/jem.185.11.1951","article-title":"Isolation, structure elucidation, and synthesis of a macrophage stimulatory lipopeptide from Mycoplasma fermentans acting at picomolar concentration","volume":"185","author":"Muhlradt","year":"1997","journal-title":"J Exp Med"},{"key":"10.1016\/j.peptides.2009.04.012_bib31","first-page":"374","article-title":"First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro","volume":"74","author":"Naiki","year":"1996","journal-title":"Lab Invest"},{"key":"10.1016\/j.peptides.2009.04.012_bib32","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1016\/S0006-3495(01)75786-4","article-title":"Fluctuations and the Hofmeister effect","volume":"81","author":"Neagu","year":"2001","journal-title":"Biophys J"},{"key":"10.1016\/j.peptides.2009.04.012_bib33","doi-asserted-by":"crossref","first-page":"3570","DOI":"10.1021\/bi982119e","article-title":"Recognition sequence design for peptidyl modulators of beta-amyloid aggregation and toxicity","volume":"38","author":"Pallitto","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2009.04.012_bib34","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.R800036200","article-title":"Amyloid beta-protein assembly and Alzheimer's disease","author":"Roychaudhuri","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2009.04.012_bib35","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1002\/bip.10441","article-title":"An autocatalytic reaction, as a model for the kinetics of the aggregation of beta-amyloid","volume":"71","author":"Sabate","year":"2003","journal-title":"Biopolymers"},{"key":"10.1016\/j.peptides.2009.04.012_bib36","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1126\/science.289.5483.1317","article-title":"Nucleated conformational conversion and the replication of conformational information by a prion determinant","volume":"289","author":"Serio","year":"2000","journal-title":"Science"},{"key":"10.1016\/j.peptides.2009.04.012_bib37","doi-asserted-by":"crossref","first-page":"2383","DOI":"10.1016\/S0006-3495(93)81312-2","article-title":"Light scattering analysis of fibril growth from the amino-terminal fragment beta(1-28) of beta-amyloid peptide","volume":"65","author":"Shen","year":"1993","journal-title":"Biophys J"},{"key":"10.1016\/j.peptides.2009.04.012_bib38","doi-asserted-by":"crossref","first-page":"2333","DOI":"10.1016\/S0006-3495(03)74657-8","article-title":"Comparison of the effects of surface tension and osmotic pressure on the interfacial hydration of a fluid phospholipid bilayer","volume":"85","author":"Soderlund","year":"2003","journal-title":"Biophys J"},{"key":"10.1016\/j.peptides.2009.04.012_bib39","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/j.cell.2005.02.008","article-title":"Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective","volume":"120","author":"Tanzi","year":"2005","journal-title":"Cell"},{"key":"10.1016\/j.peptides.2009.04.012_bib40","doi-asserted-by":"crossref","first-page":"31657","DOI":"10.1074\/jbc.M804722200","article-title":"Sequestration of copper from \u03b2-amyloid promotes selective lysis by Cyclen-hybrid cleavage agents","volume":"283","author":"Wu","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2009.04.012_bib41","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.bbrc.2008.06.035","article-title":"TiO2 nanoparticles promote beta-amyloid fibrillation in vitro","volume":"373","author":"Wu","year":"2008","journal-title":"Biochem Biophys Res Commun"}],"container-title":["Peptides"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0196978109001557?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0196978109001557?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,12,20]],"date-time":"2018-12-20T05:21:46Z","timestamp":1545283306000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0196978109001557"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,7]]},"references-count":41,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2009,7]]}},"alternative-id":["S0196978109001557"],"URL":"https:\/\/doi.org\/10.1016\/j.peptides.2009.04.012","relation":{},"ISSN":["0196-9781"],"issn-type":[{"value":"0196-9781","type":"print"}],"subject":[],"published":{"date-parts":[[2009,7]]}}}