Amorphous Aggregation of Cytochrome c with Inherently Low Amyloidogenicity Is Characterized by the Metastability of Supersaturation and the Phase Diagram

Langmuir : the ACS Journal of Surfaces and Colloids
Yuxi LinYoung-Ho Lee

Abstract

Despite extensive studies on the folding and function of cytochrome c, the mechanisms underlying its aggregation remain largely unknown. We herein examined the aggregation behavior of the physiologically relevant two types of cytochrome c, metal-bound cytochrome c, and its fragment with high amyloidogenicity as predicted in alcohol/water mixtures. Although the aggregation propensity of holo cytochrome c was low due to high solubility, markedly unfolded apo cytochrome c, lacking the heme prosthetic group, strongly promoted the propensity for amorphous aggregation with increases in hydrophobicity. Silver-bound apo cytochrome c increased the capacity of fibrillar aggregation (i.e., protofibrils or immature fibrils) due to subtle structural changes of apo cytochrome c by strong binding of silver. However, mature amyloid fibrils were not detected for any of the cytochrome c variants or its fragment, even with extensive ultrasonication, which is a powerful amyloid inducer. These results revealed the intrinsically low amyloidogenicity of cytochrome c, which is beneficial for its homeostasis and function by facilitating the folding and minimizing irreversible amyloid formation. We propose that intrinsically low amyloidogenicity of cyto...Continue Reading

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Citations

Jun 14, 2017·Physical Chemistry Chemical Physics : PCCP·Misaki KinoshitaYoung-Ho Lee
Mar 2, 2018·Protein Science : a Publication of the Protein Society·Young-Ho Lee, Ayyalusamy Ramamoorthy
Feb 15, 2019·Biotechnic & Histochemistry : Official Publication of the Biological Stain Commission·M JahanshahiG Bahlakeh
Dec 1, 2020·Biophysical Chemistry·Magdalena I IvanovaAyyalusamy Ramamoorthy
Apr 3, 2018·Journal of the American Chemical Society·Dinendra L AbeyawardhaneHeather R Lucas

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