Table 4. Consequences of Glycation on Various Proteins and Their Cytotoxicity.

protein	glycating agent	aggregate morphology	cytotoxicity	cell lines used	refs
Aβ-peptide	glucose	amyloid aggregation (accelerated)	non-cytotoxic	neuroblastoma cells	(29)(30),
β2-microglobulin	d-ribose	granular morphology to amyloid aggregation	cytotoxic	human SH-SY5Y neuroblastoma and human foreskin fibroblast FS2 cells	(31)(32),
	d-glucose	amyloid fibril formation (inhibition)
insulin	methylglyoxal	native-like aggregate	not determined		(33)(34),
	glucose (reducing conditions)	amyloid formation (accelerate)
	glucose (non-reducing conditions)	amyloid formation (inhibition)
cytochrome c	methylglyoxal	native-like aggregates	non-cytotoxic		(35)
α-synuclein	methylglyoxal	amyloid fibrils (inhibition)	non-cytotoxic	HeLa and SH-SY5Y cells	(36)
	d-ribose	molten globule-like aggregates	high cytotoxicity	SH-SY5Y cells	(37)
Lyz	d-glucose, d-fructose, d-ribose (most effective)	cross-linked β-sheet-rich, amorphous and globular oligomers	not determined		(39)
albumin	d-ribose	β-rich aggregates evolve to amyloid fibrils	highly cytotoxic	neurotypic SH-SY5Y and MCF-7 cells	(40−)
W7FW14F apomyoglobin	d-ribose	amyloid fibrils	non-cytotoxic	NIH-3T3 cells	(44)(45),
α-LA	glyoxal	mixture of globular and fibrillar aggregates	mildly cytotoxic	HeLa cells	this study
Lyz	glyoxal	amyloid fibrils	mildly cytotoxic	HeLa cells	this study
CA	glyoxal	globular aggregates	mildly cytotoxic	HeLa cells	this study
Myo	glyoxal	globular aggregates	cytotoxic	HeLa cells	this study