دورية أكاديمية
أعرض في EDS

Chaperone-like activity of the N-terminal region of a human small heat shock protein and chaperone-functionalized nanoparticles.

التفاصيل البيبلوغرافية
العنوان: Chaperone-like activity of the N-terminal region of a human small heat shock protein and chaperone-functionalized nanoparticles.
المؤلفون: Gliniewicz EF; Department of Chemistry, Mount Holyoke College, South Hadley, Massachusetts., Chambers KM; Department of Chemistry, Mount Holyoke College, South Hadley, Massachusetts., De Leon ER; Department of Chemistry, Mount Holyoke College, South Hadley, Massachusetts., Sibai D; Department of Chemistry, Mount Holyoke College, South Hadley, Massachusetts., Campbell HC; Department of Chemistry, Mount Holyoke College, South Hadley, Massachusetts., McMenimen KA; Department of Chemistry, Mount Holyoke College, South Hadley, Massachusetts.
المصدر: Proteins [Proteins] 2019 May; Vol. 87 (5), pp. 401-415. Date of Electronic Publication: 2019 Feb 07.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Wiley-Liss Country of Publication: United States NLM ID: 8700181 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1097-0134 (Electronic) Linking ISSN: 08873585 NLM ISO Abbreviation: Proteins Subsets: MEDLINE
أسماء مطبوعة: Publication: New York, NY : Wiley-Liss
Original Publication: New York : Alan R. Liss, c1986-
مواضيع طبية MeSH: Heat-Shock Proteins/*chemistry , Heat-Shock Proteins, Small/*chemistry , Metal Nanoparticles/*chemistry , Molecular Chaperones/*chemistry, Amino Acid Sequence/genetics ; Gold/chemistry ; Heat-Shock Proteins/genetics ; Heat-Shock Proteins, Small/genetics ; Humans ; Models, Molecular ; Molecular Chaperones/genetics ; Protein Aggregates/genetics ; Protein Binding/genetics ; Protein Folding ; Protein Multimerization/genetics ; Substrate Specificity
مستخلص: Small heat shock proteins (sHsps) are molecular chaperones employed to interact with a diverse range of substrates as the first line of defense against cellular protein aggregation. The N-terminal region (NTR) is implicated in defining features of sHsps; notably in their ability to form dynamic and polydisperse oligomers, and chaperone activity. The physiological relevance of oligomerization and chemical-scale mode(s) of chaperone function remain undefined. We present novel chemical tools to investigate chaperone activity and substrate specificity of human HspB1 (B1NTR), through isolation of B1NTR and development of peptide-conjugated gold nanoparticles (AuNPs). We demonstrate that B1NTR exhibits chaperone capacity for some substrates, determined by anti-aggregation assays and size-exclusion chromatography. The importance of protein dynamics and multivalency on chaperone capacity was investigated using B1NTR-conjugated AuNPs, which exhibit concentration-dependent chaperone activity for some substrates. Our results implicate sHsp NTRs in chaperone activity, and demonstrate the therapeutic potential of sHsp-AuNPs in rescuing aberrant protein aggregation.
(© 2019 Wiley Periodicals, Inc.)
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معلومات مُعتمدة: R15 GM120654 United States GM NIGMS NIH HHS; R15GM120654-01 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: molecular chaperone; mutagenesis; nanotechnology; protein chemistry; small heat shock protein (sHsp)
المشرفين على المادة: 0 (HSPB1 protein, human)
0 (Heat-Shock Proteins)
0 (Heat-Shock Proteins, Small)
0 (Molecular Chaperones)
0 (Protein Aggregates)
7440-57-5 (Gold)
تواريخ الأحداث: Date Created: 20190127 Date Completed: 20200420 Latest Revision: 20200501
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC6607909
DOI: 10.1002/prot.25662
PMID: 30684363
قاعدة البيانات: MEDLINE
الوصف
تدمد:1097-0134
DOI:10.1002/prot.25662