Amino acid sequence determinants in self‐assembly of insulin chiral amyloid superstructures: Role of C‐terminus of B‐chain in association of fibrils. Issue 6 (14th February 2013)

• Record Type: Journal Article
• Authors: Babenko, Viktoria; Dzwolak, Wojciech
• Is Part Of: FEBS letters. Volume 587:Issue 6(2013)
• Page Start: 625
• Page End: 630
• Publication Date: 2013-02-14
• Subjects: AFM -- atomic force microscopy -- BI -- bovine insulin -- CD -- circular dichroism -- FT-IR -- Fourier transform infrared -- HEWL -- hen egg white lysozyme -- HI -- human insulin -- ICD -- induced circular dichroism -- Ins-Core -- Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val insulin amyloid core peptide -- α-LAC -- bovine α-lactalbumin -- Lispro -- LysB28-ProB29 human insulin analog -- PI -- porcine insulin -- PLGA -- poly-l-glutamic acid -- ThT -- thioflavin T -- Amyloid fibril -- Chiral superstructure -- Induced circular dichroism -- Molecular velcro; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.02.010
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : HEWL and HEWLbind by atomic force microscopy (View interaction) Abstract : ► We compare agitation‐assisted aggregation of several proteins. ► Only dimerizing insulins can convert into amyloid chiral superstructures. ► The C‐terminal fragment of the B‐chain binds together individual fibrils.