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Variable domain (V L ) gene segments exhibit variable tendencies to be associated with light chain amyloidosis (AL). While few of them are very frequent in AL and give rise to most of the amyloidogenic light chains compiled at the sequence databases, other are rarely found among the AL cases. To analyze to which extent these tendencies depend on folding stability and aggregation propensity of the germline V L  protein, we characterized V L  proteins encoded by four AL-associated germline gene segments and one not associated to AL. We found that the AL-associated germline rV L  proteins differ widely in conformational stability and propensity to  in vitro  amyloid aggregation. While  in vitro  the amyloid formation kinetics of these proteins correlate well with their folding stabilities, the folding stability does not clearly correlate with their germline’s frequencies in AL. We conclude that the association of the V L  genes segments to amyloidosis is not determined solely by the folding stability and aggregation propensity of the germline V L  protein. Other factors, such as the frequencies of destabilizing mutations and susceptibility to proteolysis, must play a role in determining the light chain amyloidogenicity.

biological chemistry

Stability and aggregation propensity do not fully account for the association of various germline variable domain gene segments with light chain amyloidosis