Title : Covalently attached fatty acyl chains alter the aggregation behavior of an amyloidogenic peptide derived from human β(2)-microglobulin.

Pub. Date : 2013 Dec

PMID : 24243599






2 Functional Relationships(s)
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1 In this paper, we have investigated the ability of covalently linked long-chain fatty acids in modulating the self-assembly of an aromatic amino acid-rich highly amyloidogenic sequence derived from the amino acid region 59-71 of human beta2-microglobulin by thioflavin T (ThT) fluorescence microscopy, circular dichroism, and fluorescence spectroscopy. thioflavin T beta-2-microglobulin Homo sapiens
2 In this paper, we have investigated the ability of covalently linked long-chain fatty acids in modulating the self-assembly of an aromatic amino acid-rich highly amyloidogenic sequence derived from the amino acid region 59-71 of human beta2-microglobulin by thioflavin T (ThT) fluorescence microscopy, circular dichroism, and fluorescence spectroscopy. thioflavin T beta-2-microglobulin Homo sapiens